We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Coenzyme A (HMDB01423)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-06-21 14:47:57
Accession Number HMDB01423
Secondary Accession Numbers Not Available
Common Name Coenzyme A
Description Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidization of fatty acids, and the oxidation of pyruvate in the citric acid cycle. It is adapted from beta-mercaptoethylamine, panthothenate and adenosine triphosphate. Acetyl-CoA is an important molecule itself. It is the precursor to HMG CoA, which is a vital component in cholesterol and ketone synthesis. Furthermore, it contributes an acetyl group to choline to produce acetylcholine, in a reaction catalysed by choline acetyltransferase. Its main task is conveying the carbon atoms within the acetyl group to the citric acid cycle to be oxidized for energy production. -- Wikipedia
Synonyms
  1. Acetoacetyl coenzyme A sodium salt
  2. CoA
  3. CoA-SH
  4. CoASH
  5. Coenzyme A
  6. Coenzyme A hydrate
  7. Depot-Zeel
  8. Propionyl CoA
  9. S-propanoate Coenzyme A
  10. S-propionate Coenzyme A
  11. Zeel
  12. [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl 3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate
  13. coenzymes A
  14. Coenzyme A-SH
  15. Coenzyme ASH
  16. CoA hydrate
  17. Propionyl Coenzyme A
  18. S-propanoate CoA
  19. S-propionate CoA
  20. S-propanoic acid
  21. S-propanoate
Chemical IUPAC Name [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-[[hydroxy-[hydroxy-[3-hydroxy-2,2-dimethyl-3-[2-(2-sulfanylethylcarbamoyl)ethylcarbamoyl]propoxy]phosphoryl]oxy-phosphoryl]oxymethyl]oxolan-3-yl]oxyphosphonic acid
Chemical Formula C21H36N7O16P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Short chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • secondary carboxylic acid amide
  • thiol (sulfanyl compound)
  • alkylthiol
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Alanine and aspartate metabolism
  • Component of Aminosugars metabolism
  • Component of Arginine and proline metabolism
  • Component of Bile acid biosynthesis
  • Component of Butanoate metabolism
  • Component of C5-Branched dibasic acid metabolism
  • Component of Fatty acid metabolism
  • Component of Glutamate metabolism
  • Component of Glycerolipid metabolism
  • Component of Glycerophospholipid metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Glycosphingolipid metabolism
  • Component of Glyoxylate and dicarboxylate metabolism
  • Component of Inositol metabolism
  • Component of Propanoate metabolism
  • Component of Pyruvate metabolism
  • Component of Tryptophan metabolism
Application
Source
  • Endogenous
Average Molecular Weight 767.534
Monoisotopic Molecular Weight 767.115234
Isomeric SMILES CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCS
Canonical SMILES CC(C)(COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCS
KEGG Compound ID C00010 Link Image
BioCyc ID CO-A Link Image
BiGG ID 33502 Link Image
Wikipedia Link Coenzyme A Link Image
NuGOwiki Link HMDB01423 Link Image
Metagene Link HMDB01423 Link Image
METLIN ID 6235 Link Image
PubChem Compound 6816 Link Image
PubChem Substance 8154436 Link Image
ChEBI ID 15346 Link Image
CAS Registry Number 85-61-0
InChI Identifier InChI=1/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16?,20-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 21.9 mg/mL [MEYLAN,WM et al. (1996)]; 4.64 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.61 [Predicted by ALOGPS]; -5.8 [Predicted by PubChem via XLOGP]; -5.34 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1A59 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • endoplasmic reticulum
  • golgi apparatus
  • lysosome
  • mitochondria
  • nucleus
  • peroxisome
Biofluid Location Not Available
Tissue Location
Tissue References
Adipose Tissue
Fibroblasts
Skeletal Muscle
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
Beta-Alanine Metabolism SMP00007 Link Image map00410 Link Image
Bile Acid Biosynthesis SMP00035 Link Image map00120 Link Image
Butyrate Metabolism SMP00073 Link Image map00650 Link Image
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
Ethanol Degradation SMP00449 Link Image
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Ketone Body Metabolism SMP00071 Link Image map00072 Link Image
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids SMP00482 Link Image
Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids SMP00481 Link Image
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids SMP00480 Link Image
Oxidation of Branched Chain Fatty Acids SMP00030 Link Image
Pantothenate and CoA Biosynthesis SMP00027 Link Image map00770 Link Image
Phenylacetate Metabolism SMP00126 Link Image map00360 Link Image
Plasmalogen Synthesis SMP00479 Link Image
Threonine and 2-Oxobutanoate Degradation SMP00452 Link Image
Transfer of Acetyl Groups into Mitochondria SMP00466 Link Image
General References
  1. Yano S, Li L, Le TP, Moseley K, Guedalia A, Lee J, Gonzalez I, Boles RG: Infantile mitochondrial DNA depletion syndrome associated with methylmalonic aciduria and 3-methylcrotonyl-CoA and propionyl-CoA carboxylase deficiencies in two unrelated patients: a new phenotype of mtDNA depletion syndrome. J Inherit Metab Dis. 2003;26(5):481-8. [PubMed Link Image]
  2. Roe CR, Sweetman L, Roe DS, David F, Brunengraber H: Treatment of cardiomyopathy and rhabdomyolysis in long-chain fat oxidation disorders using an anaplerotic odd-chain triglyceride. J Clin Invest. 2002 Jul;110(2):259-69. [PubMed Link Image]
  3. Kretschmer RE, Bachmann C: Methylcitric acid determination in amniotic fluid by electron-impact mass fragmentography. J Clin Chem Clin Biochem. 1988 May;26(5):345-8. [PubMed Link Image]
  4. Osmundsen H, Bremer J, Pedersen JI: Metabolic aspects of peroxisomal beta-oxidation. Biochim Biophys Acta. 1991 Sep 11;1085(2):141-58. [PubMed Link Image]
  5. Reihner E, Angelin B, Rudling M, Ewerth S, Bjorkhem I, Einarsson K: Regulation of hepatic cholesterol metabolism in humans: stimulatory effects of cholestyramine on HMG-CoA reductase activity and low density lipoprotein receptor expression in gallstone patients. J Lipid Res. 1990 Dec;31(12):2219-26. [PubMed Link Image]
  6. Bergstrom T, Greter J, Levin AH, Steen G, Tryding N, Wass U: Propionyl-CoA carboxylase deficiency: case report, effect of low-protein diet and identification of 3-oxo-2-methylvaleric acid 3-hydroxy-2-methylvaleric acid, and maleic acid in urine. Scand J Clin Lab Invest. 1981 Apr;41(2):117-26. [PubMed Link Image]
  7. Salen G, Batta AK, Tint GS, Shefer S: Comparative effects of lovastatin and chenodeoxycholic acid on plasma cholestanol levels and abnormal bile acid metabolism in cerebrotendinous xanthomatosis. Metabolism. 1994 Aug;43(8):1018-22. [PubMed Link Image]
  8. Lehnert W, Junker A: [2-Methyl-3-oxovaleric acid: a characteristic metabolite in propionic acidemia] Clin Chim Acta. 1980 May 21;104(1):47-51. [PubMed Link Image]
  9. Wendel U, Zass R, Leupold D: Contribution of odd-numbered fatty acid oxidation to propionate production in neonates with methylmalonic and propionic acidaemias. Eur J Pediatr. 1993 Dec;152(12):1021-3. [PubMed Link Image]
  10. Wikipedia Link Image
Metabolic Enzymes
  1. ATP-citrate synthase
  2. Acetyl-CoA acetyltransferase, cytosolic
  3. Diamine acetyltransferase 2
  4. Arylamine N-acetyltransferase 1
  5. 5-aminolevulinate synthase, nonspecific, mitochondrial precursor
  6. General transcription factor 3C polypeptide 4
  7. Choline O-acetyltransferase
  8. Histone acetyltransferase PCAF
  9. Carnitine O-acetyltransferase
  10. Diamine acetyltransferase 1
  11. Serotonin N-acetyltransferase
  12. 3-ketoacyl-CoA thiolase, mitochondrial
  13. Testis-specific chromodomain protein Y 1
  14. Fatty acid synthase
  15. Histone acetyltransferase HTATIP
  16. Nuclear receptor coactivator 1
  17. Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
  18. Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
  19. Citrate synthase, mitochondrial precursor
  20. Testis-specific chromodomain protein Y 2
  21. Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
  22. Trifunctional enzyme subunit beta, mitochondrial precursor
  23. 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial precursor
  24. Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor
  25. Glucosamine 6-phosphate N-acetyltransferase
  26. Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor
  27. Peroxisomal carnitine O-octanoyltransferase
  28. Carnitine O-palmitoyltransferase I, muscle isoform
  29. Carnitine O-palmitoyltransferase I, liver isoform
  30. 2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
  31. Sterol O-acyltransferase 2
  32. Sterol O-acyltransferase 1
  33. N-acetylglutamate synthase, mitochondrial precursor
  34. Bile acid CoA:amino acid N-acyltransferase
  35. Long-chain-fatty-acid--CoA ligase 4
  36. Long-chain-fatty-acid--CoA ligase 1
  37. Long-chain-fatty-acid--CoA ligase 6
  38. Long-chain-fatty-acid--CoA ligase 5
  39. Long-chain-fatty-acid--CoA ligase 3
  40. Serine palmitoyltransferase 2
  41. Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
  42. Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
  43. 3-hydroxy-3-methylglutaryl-coenzyme A reductase
  44. Cytosolic acyl coenzyme A thioester hydrolase
  45. Acyl-coenzyme A thioesterase 2
  46. Acyl-coenzyme A thioesterase 8
  47. Palmitoyl-protein thioesterase 1 precursor
  48. Dihydroxyacetone phosphate acyltransferase
  49. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
  50. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
  51. Bifunctional coenzyme A synthase
  52. General control of amino acid synthesis protein 5-like 2
  53. Succinate-CoA ligase, ADP-forming, beta subunit
  54. Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial precursor
  55. Acetoacetyl-CoA synthetase
  56. Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
  57. Diacylglycerol O-acyltransferase 2
  58. 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
  59. 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial precursor
  60. Acyl-CoA wax alcohol acyltransferase 1
  61. Acyl-CoA wax alcohol acyltransferase 2
  62. Arylamine N-acetyltransferase 2
  63. Putative uncharacterized protein
  64. ACSS2 protein
  65. cDNA FLJ75707, highly similar to Homo sapiens serine palmitoyltransferase, long chain base subunit 1
  66. cDNA FLJ78080, highly similar to Human ALAS 5-aminolevulinate synthase
  67. Elongator complex protein 3
  68. 2-oxoglutarate dehydrogenase E1 component-like, mitochondrial precursor
  69. 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
  70. Carnitine O-octanoyltransferase
  71. Putative uncharacterized protein DKFZp451P0819
  72. Acyl-CoA thioesterase 4
  73. 1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha) (1-acylglycerol-3-phosphate O-acyltransferase 1 (Lysophosphatidic acid acyltransferase, alpha), isoform CRA_b)
  74. Testis spermatogenesis apoptosis-related protein 7 (1-acylglycerol-3- phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta), isoform CRA_b)
  75. Lysocardiolipin acyltransferase (Uncharacterized protein LYCAT)
  76. ACAA1 protein
  77. CREBBP variant protein (Fragment)
  78. Histone acetyltransferase MYST4
  79. MYST3 protein (Fragment)
  80. Nuclear receptor coactivator 3 (Nuclear receptor coactivator 3, isoform CRA_g)
  81. Probable histone acetyltransferase MYST1
  82. Histone acetyltransferase 1 (Histone acetyltransferase 1, isoform CRA_b)
  83. CLOCK (cDNA FLJ78672, highly similar to Homo sapiens clock homolog (mouse) (CLOCK), mRNA)
  84. Heparan-alpha-glucosaminide N-acetyltransferase
  85. cDNA FLJ76905, highly similar to Homo sapiens N-myristoyltransferase 1 (NMT1), mRNA (N-myristoyltransferase 1, isoform CRA_b)
  86. cDNA FLJ16680 fis, clone TLIVE2008221, highly similar to Acyl-coenzyme A thioesterase 12 (EC 3.1.2.1)
  87. cDNA FLJ41040 fis, clone LIVER1000017, highly similar to Bile acyl-CoA synthetase (EC 6.2.1.7)
  88. cDNA, FLJ93082, Homo sapiens carnitine palmitoyltransferase II (CPT2), nuclear geneencoding mitochondrial protein, mRNA (Carnitine palmitoyltransferase II)
  89. Putative uncharacterized protein
  90. Palmitoyl-protein thioesterase 2 (HCG1999928, isoform CRA_a)
  91. cDNA, FLJ93492, highly similar to Homo sapiens pyruvate dehydrogenase (lipoamide) beta (PDHB), mRNA (Pyruvate dehydrogenase (Lipoamide) beta, isoform CRA_a)
  92. cDNA, FLJ92720, Homo sapiens aldehyde dehydrogenase 6 family, member A1 (ALDH6A1),nuclear gene encoding mitochondrial protein, mRNA (Aldehyde dehydrogenase 6 family, member A1, isoform CRA_b)
  93. cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
  94. Putative uncharacterized protein
  95. cDNA FLJ13828 fis, clone THYRO1000605, highly similar to Histone acetyltransferase MYST2 (EC 2.3.1.48)
  96. E1A binding protein p300
  97. cDNA, FLJ96671, Homo sapiens 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (soluble) (HMGCS1), mRNA (3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (Soluble), isoform CRA_a)
  98. Diacylglycerol O-acyltransferase homolog 1 (Mouse) (Diacylglycerol O-acyltransferase homolog 1 (Mouse), isoform CRA_a)
  99. Glycylpeptide N-tetradecanoyltransferase
Enzyme 1 [top]
Enzyme 1 ID 5239
Enzyme 1 Name ATP-citrate synthase
Enzyme 1 Synonyms
  1. ATP-citrate
  2. pro-S--lyase
  3. Citrate cleavage enzyme
Enzyme 1 Gene Name ACLY
Enzyme 1 Protein Sequence >ATP-citrate synthase
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM
Enzyme 1 Number of Residues 1101
Enzyme 1 Molecular Weight 120841
Enzyme 1 Theoretical pI 7.34
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 28935 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P53396 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ACLY_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3318 bp
ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCGACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGCCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGACGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGTGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCTGGGCA
CCGGCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTTCTCCTCAACGCC
CAGCGGGAGACATCGACTCCAGCCCCCAGCAGGACAGCATCTTTTTATGAGTCCATGGTC
GATGAGGTCAGGGCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAA
GATTCAGTCCCAAGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCAC
ACCAAGGCCATTGTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGAC
TATGTCTGCTCCCGAGACGAGCCCTCAGTGGCTGCCATGGTCTATCCTTTCACTGGGGAC
CACAAGCAGAAGTTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATG
GCTGATGCCATGAGGAAGCACCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGC
TCTGCCTATGACAGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATC
ATAGCTGAAGGCATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAG
GGAGTGACCATCATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATT
GGCAACACAGGTGGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCCCCAGGCAGCT
GTGGCCTATGTCTCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGG
ACCACGGATGGCGTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACA
TTCATGGATCATGTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTT
GGAGAGATTGGGGGCACTGAGGAATATAAGATTTCCCGGGGCATCAAGGAGGGCCGCCTC
ACTAAGCCCATCGTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTC
CAGTTTGGCCATGCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAAC
CAGGCTTTGAAGGAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATC
ATCCAGTCTGTATACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTG
CCGCCCCCAACCGTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAA
CCTGCCTCGTTCATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGC
ATGCCCATCACTGAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGCCCTCGGCCTCCTC
TGGTTCCAGAAAAGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTG
ACAGCTGATCACGGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGCACC
GCGGTGGAGCTGGTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGG
GGTGCCTTGGATGCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCC
ATGGAGTTTGTGAACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGA
GTGAAGTCGATAAACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAG
CACTTCCCTGCCACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCG
AAGAAGCCAAATCTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATG
CTTAGAAACTGTGGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCC
CTCAATGGCATCTTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAG
AAGAGGCTGAAGCAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCG
GAACACATGAGCATGTAA
Enzyme 1 GenBank Gene ID X64330 Link Image
Enzyme 1 GeneCard ID ACLY Link Image
Enzyme 1 GenAtlas ID ACLY Link Image
Enzyme 1 HGNC ID HGNC:115 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17q12-q21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5242
Enzyme 2 Name Acetyl-CoA acetyltransferase, cytosolic
Enzyme 2 Synonyms
  1. Cytosolic acetoacetyl-CoA thiolase
  2. Acetyl CoA transferase-like protein
Enzyme 2 Gene Name ACAT2
Enzyme 2 Protein Sequence >Acetyl-CoA acetyltransferase, cytosolic
MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHV
LAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGME
NMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDK
VAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLT
DGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPA
IKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGC
RILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE
Enzyme 2 Number of Residues 397
Enzyme 2 Molecular Weight 41351
Enzyme 2 Theoretical pI 6.92
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function 2 acetyl-CoA = CoA + acetoacetyl-CoA
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 2 acetyl-CoA = CoA + acetoacetyl-CoA
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-26
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 546901 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BWD1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name THIC_HUMAN Link Image
Enzyme 2 PDB ID 1WL5 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1194 bp
ATGAATGCAGGCTCAGATCCTGTGGTCATCGTCTCGGCGGCGCGGACCATCATAGGTTCC
TTCAATGGTGCCTTAGCTGCTGTTCCTGTCCAGGACCTGGGCTCCACTGTCATCAAAGAA
GTCTTGAAGAGGGCCACTGTGGCTCCGGAAGATGTGTCTGAGGTCATCTTTGGACATGTC
TTGGCAGCAGGCTGTGGGCAGAATCCTGTTAGACAAGCCAGTGTGGGTGCAGGAATTCCC
TACTCTGTTCCAGCATGGAGCTGCCAGATGATCTGTGGGTCAGGCCTAAAAGCTGTGTGC
CTTGCAGTCCAGTCAATAGGGATAGGAGACTCCAGCATTGTGGTTGCAGGAGGCATGGAA
AATATGAGCAAGGCTCCTCACTTGGCTTACTTGAGAACAGGAGTAAAGATAGGTGAGATG
CCACTGACTGACAGTATACTCTGTGATGGTCTTACAGATGCATTTCACAACTGTCATATG
GGTATTACAGCTGAAAATGTAGCCACAAAATGGCAAGTGAGTAGAGAAGATCAGGACAAG
GTTGCAGTTCTGTCCCAGAACAGGACAGAGAATGCACAGAAAGCTGGCCATTTTGACAAA
GAGATTGTACCAGTTTTGGTGTCAACTAGAAAAGGTCTTATTGAAGTTAAAACAGATGAG
TTTCCTCGCCATGGGAGCAACATAGAAGCCATGTCCAAGCTAAAGCCTTACTTTCTTACT
GATGGAACGGGAACAGTCACCCCAGCCAATGCTTCAGGAATAAATGATGGTGCTGCAGCT
GTTGCTCTTATGAAGAAGTCAGAAGCTGATAAACGTGGGCTTACACCTTTAGCACGGATA
GTTTCCTGGTCCCAAGTGGGTGTGGAGCCTTCCATTATGGGAATAGGACCAATTCCAGCC
ATAAAGCAAGCTGTTACAAAAGCAGGTTGGTCACTGGAAGATGTTGACATATTTGAAATC
AATGAAGCCTTTGCAGCTGTCTCTGCTGCAATAGTTAAAGAACTTGGATTAAACCCAGAG
AAGGTCAATATTGAAGGAGGGGCTATAGCCTTGGGCCACCCTCTTGGAGCATCTGGCTGT
CGAATTCTTGTGACCCTGTTACACACACTGGAGAGAATGGGCAGAAGTCGTGGTGTTGCA
GCCCTGTGCATTGGGGGTGGGATGGGAATAGCAATGTGTGTTCAGAGAGAATGA
Enzyme 2 GenBank Gene ID S70154 Link Image
Enzyme 2 GeneCard ID ACAT2 Link Image
Enzyme 2 GenAtlas ID ACAT2 Link Image
Enzyme 2 HGNC ID HGNC:94 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6q25.3-q26
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Song XQ, Fukao T, Yamaguchi S, Miyazawa S, Hashimoto T, Orii T: Molecular cloning and nucleotide sequence of complementary DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase. Biochem Biophys Res Commun. 1994 May 30;201(1):478-85. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5244
Enzyme 3 Name Diamine acetyltransferase 2
Enzyme 3 Synonyms
  1. Spermidine/spermine N(1- acetyltransferase 2
  2. Polyamine N-acetyltransferase 2
Enzyme 3 Gene Name SAT2
Enzyme 3 Protein Sequence >Diamine acetyltransferase 2
MASVRIREAKEGDCGDILRLIRELAEFEKLSDQVKISEEALRADGFGDNPFYHCLVAEIL
PAPGKLLGPCVVGYGIYYFIYSTWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDK
GCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEGWHFFCFQGEATRKLAGK
Enzyme 3 Number of Residues 170
Enzyme 3 Molecular Weight 19155
Enzyme 3 Theoretical pI 5.84
Enzyme 3 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 3 General Function Transcription
Enzyme 3 Specific Function Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine
Enzyme 3 Pathways
Enzyme 3 Reactions
  • acetyl-CoA + an alkane-alpha,omega -diamine = CoA + an N-acetyldiamine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 19070527 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q96F10 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SAT2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >513 bp
ATGGCTTCCGTGCGGATCCGAGAGGCCAAGGAGGGAGACTGTGGAGATATCCTGAGGCTG
ATTCGGGAGCTAGCCGAATTCGAAAAACTCTCGGATCAGGTGAAGATCAGTGAAGAAGCC
CTGAGAGCAGATGGCTTTGGAGACAATCCTTTCTATCACTGTTTGGTAGCAGAGATTCTT
CCAGCGCCCGGGAAGCTACTGGGGCCCTGCGTGGTGGGCTATGGGATATACTATTTCATC
TACAGTACATGGAAGGGACGCACCATTTATCTGGAGGATATCTATGTGATGCCAGAATAT
CGGGGTCAAGGGATTGGTTCCAAAATAATCAAAAAGGTGGCTGAGGTGGCCTTGGATAAG
GGCTGCTCCCAATTCCGCCTGGCCGTCCTGGACTGGAACCAGAGGGCCATGGACTTGTAC
AAGGCCCTAGGAGCCCAAGATCTGACGGAAGCTGAGGGCTGGCACTTCTTCTGCTTTCAA
GGAGAGGCAACGAGAAAGTTGGCAGGAAAGTGA
Enzyme 3 GenBank Gene ID AF348524 Link Image
Enzyme 3 GeneCard ID SAT2 Link Image
Enzyme 3 GenAtlas ID SAT2 Link Image
Enzyme 3 HGNC ID HGNC:23160 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17p13.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Chen Y, Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase. Biochem J. 2003 Aug 1;373(Pt 3):661-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5249
Enzyme 4 Name Arylamine N-acetyltransferase 1
Enzyme 4 Synonyms
  1. Arylamide acetylase 1
  2. Monomorphic arylamine N-acetyltransferase
  3. MNAT
  4. N- acetyltransferase type 1
  5. NAT-1
Enzyme 4 Gene Name NAT1
Enzyme 4 Protein Sequence >Arylamine N-acetyltransferase 1
MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVV
RRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYI
VDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDL
LEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLT
HRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI
Enzyme 4 Number of Residues 290
Enzyme 4 Molecular Weight 33899
Enzyme 4 Theoretical pI 6.51
Enzyme 4 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • arylamine N-acetyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 4 Specific Function Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • acetyl-CoA + an arylamine = CoA + an N-acetylarylamine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 34994 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P18440 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ARY1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >873 bp
ATGGACATTGAAGCATATCTTGAAAGAATTGGCTATAAGAAGTCTAGGAACAAATTGGAC
TTGGAAACATTAACTGACATTCTTCAACACCAGATCCGAGCTGTTCCCTTTGAGAACCTT
AACATCCATTGTGGGGATGCCATGGACTTAGGCTTAGAGGCCATTTTTGATCAAGTTGTG
AGAAGAAATCGGGGTGGATGGTGTCTCCAGGTCAATCATCTTCTGTACTGGGCTCTGACC
ACTATTGGTTTTGAGACCACGATGTTGGGAGGGTATGTTTACAGCACTCCAGCCAAAAAA
TACAGCACTGGCATGATTCACCTTCTCCTGCAGGTGACCATTGATGGCAGGAACTACATT
GTCGATGCTGGGTTTGGACGCTCATACCAGATGTGGCAGCCTCTGGAGTTAATTTCTGGG
AAGGATCAGCCTCAGGTGCCTTGTGTCTTCCGTTTGACGGAAGAGAATGGATTCTGGTAT
CTAGACCAAATCAGAAGGGAACAGTACATTCCAAATGAAGAATTTCTTCATTCTGATCTC
CTAGAAGACAGCAAATACCGAAAAATCTACTCCTTTACTCTTAAGCCTCGAACAATTGAA
GATTTTGAGTCTATGAATACATACCTGCAGACATCTCCATCATCTGTGTTTACTAGTAAA
TCATTTTGTTCCTTGCAGACCCCAGATGGGGTTCACTGTTTGGTGGGCTTCACCCTCACC
CATAGGAGATTCAATTATAAGGACAATACAGATCTAATAGAGTTCAAGACTCTGAGTGAG
GAAGAAATAGAAAAAGTGCTGAAAAATATATTTAATATTTCCTTGCAGAGAAAGCTTGTG
CCCAAACATGGTGATAGATTTTTTACTATTTAG
Enzyme 4 GenBank Gene ID X17059 Link Image
Enzyme 4 GeneCard ID NAT1 Link Image
Enzyme 4 GenAtlas ID NAT1 Link Image
Enzyme 4 HGNC ID HGNC:7645 Link Image
Enzyme 4 Chromosome Location 8
Enzyme 4 Locus 8p23.1-p21.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Blum M, Grant DM, McBride W, Heim M, Meyer UA: Human arylamine N-acetyltransferase genes: isolation, chromosomal localization, and functional expression. DNA Cell Biol. 1990 Apr;9(3):193-203. [PubMed Link Image]
  2. Ohsako S, Deguchi T: Cloning and expression of cDNAs for polymorphic and monomorphic arylamine N-acetyltransferases from human liver. J Biol Chem. 1990 Mar 15;265(8):4630-4. [PubMed Link Image]
  3. Vatsis KP, Weber WW: Structural heterogeneity of Caucasian N-acetyltransferase at the NAT1 gene locus. Arch Biochem Biophys. 1993 Feb 15;301(1):71-6. [PubMed Link Image]
  4. Doll MA, Jiang W, Deitz AC, Rustan TD, Hein DW: Identification of a novel allele at the human NAT1 acetyltransferase locus. Biochem Biophys Res Commun. 1997 Apr 28;233(3):584-91. [PubMed Link Image]
  5. Butcher NJ, Ilett KF, Minchin RF: Functional polymorphism of the human arylamine N-acetyltransferase type 1 gene caused by C190T and G560A mutations. Pharmacogenetics. 1998 Feb;8(1):67-72. [PubMed Link Image]
  6. Lo-Guidice JM, Allorge D, Chevalier D, Debuysere H, Fazio F, Lafitte LJ, Broly F: Molecular analysis of the N-acetyltransferase 1 gene (NAT1*) using polymerase chain reaction-restriction fragment-single strand conformation polymorphism assay. Pharmacogenetics. 2000 Jun;10(4):293-300. [PubMed Link Image]
  7. Ebisawa T, Deguchi T: Structure and restriction fragment length polymorphism of genes for human liver arylamine N-acetyltransferases. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1252-7. [PubMed Link Image]
  8. Delomenie C, Goodfellow GH, Krishnamoorthy R, Grant DM, Dupret JM: Study of the role of the highly conserved residues Arg9 and Arg64 in the catalytic function of human N-acetyltransferases NAT1 and NAT2 by site-directed mutagenesis. Biochem J. 1997 Apr 1;323 ( Pt 1):207-15. [PubMed Link Image]
  9. Hughes NC, Janezic SA, McQueen KL, Jewett MA, Castranio T, Bell DA, Grant DM: Identification and characterization of variant alleles of human acetyltransferase NAT1 with defective function using p-aminosalicylate as an in-vivo and in-vitro probe. Pharmacogenetics. 1998 Feb;8(1):55-66. [PubMed Link Image]
  10. Lin HJ, Probst-Hensch NM, Hughes NC, Sakamoto GT, Louie AD, Kau IH, Lin BK, Lee DB, Lin J, Frankl HD, Lee ER, Hardy S, Grant DM, Haile RW: Variants of N-acetyltransferase NAT1 and a case-control study of colorectal adenomas. Pharmacogenetics. 1998 Jun;8(3):269-81. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5251
Enzyme 5 Name 5-aminolevulinate synthase, nonspecific, mitochondrial precursor
Enzyme 5 Synonyms
  1. 5-aminolevulinic acid synthase
  2. Delta-aminolevulinate synthase
  3. Delta-ALA synthetase
  4. ALAS-H
Enzyme 5 Gene Name ALAS1
Enzyme 5 Protein Sequence >5-aminolevulinate synthase, nonspecific, mitochondrial precursor
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
Enzyme 5 Number of Residues 640
Enzyme 5 Molecular Weight 70582
Enzyme 5 Theoretical pI 8.57
Enzyme 5 GO Classification
Function
  • 5-aminolevulinate synthase activity
  • N-acyltransferase activity
  • N-succinyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2)
Enzyme 5 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 5 Reactions
  • succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 28583 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P13196 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name HEM1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1923 bp
ATGGAGAGTGTTGTTCGCCGCTGCCCATTCTTATCCCGAGTCCCCCAGGCCTTTCTGCAG
AAAGCAGGCAAATCTCTGTTGTTCTATGCCCAAAACTGCCCCAAGATGATGGAAGTTGGG
GCCAAGCCAGCCCCTCGGGCATTGTCCACTGCAGCAGTACACTACCAACAGATCAAAGAA
ACCCCTCCGGCCAGTGAGAAAGACAAAACTGCTAAGGCCAAGGTCCAACAGACTCCTGAT
GGATCCCAGCAGAGTCCAGATGGCACACAGCTTCCGTCTGGACACCCCTTGCCTGCCACA
AGCCAGGGCACTGCAAGCAAATGCCCTTTCCTGGCAGCACAGATGAATCAGAGAGGCAGC
AGTGTCTTCTGCAAAGCCAGTCTTGAGCTTCAGGAGGATGTGCAGGAAATGAATGCCGTG
AGGAAAGAGGTTGCTGAAACCTCAGCAGGCCCCAGTGTGGTTAGTGTGAAAACCGATGGA
GGGGATCCCAGTGGACTGCTGAAGAACTTCCAGGACATTATGCAAAAGCAAAGACCAGAA
AGAGTGTCTCATCTTCTTCAAGATAACTTGCCAAAATCTGTTTCCACTTTTCAGTATGAT
CGTTTCTTTGAGAAAAAAATTGATGAGAAAAAGAATGACCACACCTATCGAGTTTTTAAA
ACTGTGAACCGGCGAGCACACATCTTCCCCATGGCAGATGACTATTCAGACTCCCTCATC
ACCAAAAAGCAAGTGTCAGTCTGGTGCAGTAATGACTACCTAGGAATGAGTCGCCACCCA
CGGGTGTGTGGGGCAGTTATGGACACTTTGAAACAACATGGTGCTGGGGCAGGTGGTACT
AGAAATATTTCTGGAACTAGTAAATTCCATGTGGACTTAGAGCGGGAGCTGGCAGACCTC
CATGGGAAAGATGCCGCACTCTTGTTTTCCTCGTGCTTTGTGGCCAATGACTCAACCCTC
TTCACCCTGGCTAAGATGATGCCAGGCTGTGAGATTTACTCTGATTCTGGGAACCATGCC
TCCATGATCCAAGGGATTCGAAACAGCCGAGTGCCAAAGTACATCTTCCGCCACAATGAT
GTCAGCCACCTCAGAGAACTGCTGCAAAGATCTGACCCCTCAGTCCCCAAGATTGTGGCA
TTTGAAACTGTCCATTCAATGGATGGGGCGGTGTGCCCACTGGAAGAGCTGTGTGATGTG
GCCCATGAGTTTGGAGCAATCACCTTCGTGGATGAGGTCCACGCAGTGGGGCTTTATGGG
GCTCGAGGCGGAGGGATTGGGGATCGGGATGGAGTCATGCCAAAAATGGACATCATTTCT
GGAACACTTGGCAAAGCCTTTGGTTGTGTTGGAGGGTACATCGCCAGCACGAGTTCTCTG
ATTGACACCGTACGGTCCTATGCTGCTGGCTTCATCTTCACCACCTCTCTGCCACCCATG
CTGCTGGCTGGAGCCCTGGAGTCTGTGCGGATCCTGAAGAGCGCTGAGGGACGGGTGCTT
CGCCGCCAGCACCAGCGCAACGTCAAACTCATGAGACAGATGCTAATGGATGCCGGCCTC
CCTGTTGTCCACTGCCCCAGCCACATCATCCCTGTGCGGGTTGCAGATGCTGCTAAAAAC
ACAGAAGTCTGTGATGAACTAATGAGCAGACATAACATCTACGTGCAAGCAATCAATTAC
CCTACGGTGCCCCGGGGAGAAGAGCTCCTACGGATTGCCCCCACCCCTCACCACACACCC
CAGATGATGAACTACTTCCTTGAGAATCTGCTAGTCACATGGAAGCAAGTGGGGCTGGAA
CTGAAGCCTCATTCCTCAGCTGAGTGCAACTTCTGCAGGAGGCCACTGCATTTTGAAGTG
ATGAGTGAAAGAGAGAAGTCCTATTTCTCAGGCTTGAGCAAGTTGGTATCTGCTCAGGCC
TGA
Enzyme 5 GenBank Gene ID X56351 Link Image
Enzyme 5 GeneCard ID ALAS1 Link Image
Enzyme 5 GenAtlas ID ALAS1 Link Image
Enzyme 5 HGNC ID HGNC:396 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed Link Image]
  2. Bawden MJ, Borthwick IA, Healy HM, Morris CP, May BK, Elliott WH: Sequence of human 5-aminolevulinate synthase cDNA. Nucleic Acids Res. 1987 Oct 26;15(20):8563. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5252
Enzyme 6 Name General transcription factor 3C polypeptide 4
Enzyme 6 Synonyms
  1. Transcription factor IIIC subunit delta
  2. TF3C-delta
  3. TFIIIC 90 kDa subunit
  4. TFIIIC 90
Enzyme 6 Gene Name GTF3C4
Enzyme 6 Protein Sequence >General transcription factor 3C polypeptide 4
MNTADQARVGPADDGPAPSGEEEGEGGGEAGGKEPAADAAPGPSAAFRLMVTRREPAVKL
QYAVSGLEPLAWSEDHRVSVSTARSIAVLELICDVHNPGQDLVIHRTSVPAPLNSCLLKV
GSKTEVAECKEKFAASKDPTVSQTFMLDRVFNPEGKALPPMRGFKYTSWSPMGCDANGRC
LLAALTMDNRLTIQANLNRLQWVQLVDLTEIYGERLYETSYRLSKNEAPEGNLGDFAEFQ
RRHSMQTPVRMEWSGICTTQQVKHNNESRDVGSVLLAVLFENGNIAVWQFQLPFVGKESI
SSCNTIESGITSPSVLFWWEYEHNNRKMSGLIVGSAFGPIKILPVNLKAVKGYFTLRQPV
ILWKEMDQLPVHSIKCVPLYHPYQKCSCSLVVAARGSYVFWRLLLISKAGLNLHNSHVTG
LHSLPIVSMTADKQNGTVYTCSSDGKVRQVIPIFTDVALKFEHQLIKLSDVFGSVRTHGI
AVKPCGAYLAIITTEGMINGLHPVNKNYQVQFVTLKTFEEAAAQLLESSVQNLFKQVDLI
DLVRWKILKDKHIPQFLQEALEKKIESSGVTYFWRFKLFLLRILYQSMQKTPSEALWKPT
HEDSKILLVDSPGMGNADDEQQEEGTSSKQVVKQGLQERSKEGDVEEPTDDSLPTTGDAG
GREPMEEKLLEIQGKIEAVEMHLTREHMKPVLGEVYLHTWITENTSIPTRGLCNFLMSDE
EYDDRTARVLIGHISKKMNKQTFPEHCSLCKEILPFTDRKQAVCSNGHIWLRCFLTYQSC
QSLIYRRCLLHDSIARHPAPEDPDWIKRLLQSPCPFCDSPVF
Enzyme 6 Number of Residues 822
Enzyme 6 Molecular Weight 92002
Enzyme 6 Theoretical pI 6.71
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 6175593 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9UKN8 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name TF3C4_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2469 bp
ATGAACACGGCCGACCAGGCCAGGGTGGGGCCCGCGGACGACGGGCCTGCGCCGTCTGGG
GAGGAGGAGGGAGAGGGGGGCGGCGAGGCGGGCGGGAAGGAGCCAGCAGCGGACGCGGCC
CCGGGGCCCAGCGCTGCATTCCGCCTCATGGTGACTCGGCGGGAGCCGGCCGTGAAGCTG
CAGTATGCGGTGAGCGGCCTGGAACCGCTGGCTTGGTCCGAGGACCACCGCGTGTCTGTG
TCCACGGCCCGCAGCATCGCTGTGCTGGAGCTCATCTGCGACGTGCACAACCCGGGCCAG
GACCTGGTTATCCACCGCACCTCGGTGCCCGCACCGCTCAACAGCTGTCTCCTCAAAGTT
GGCTCAAAAACAGAAGTTGCTGAGTGCAAGGAGAAATTCGCCGCCTCCAAGGACCCCACG
GTCAGTCAGACTTTCATGTTGGATAGGGTGTTCAACCCTGAGGGGAAGGCTTTACCACCA
ATGAGAGGATTCAAGTACACCAGCTGGTCTCCCATGGGTTGCGATGCTAATGGCAGGTGC
CTCTTGGCAGCACTGACCATGGACAATCGCCTGACCATCCAGGCAAATCTCAACAGACTG
CAGTGGGTCCAGCTGGTTGACCTGACTGAGATCTATGGAGAACGTCTTTATGAGACCAGT
TACAGGCTCTCTAAAAATGAGGCCCCGGAAGGAAATCTCGGGGATTTTGCTGAGTTTCAG
AGGAGACACAGCATGCAGACCCCAGTCAGAATGGAGTGGTCGGGCATCTGTACCACCCAG
CAGGTCAAGCATAACAACGAAAGCCGGGACGTTGGCAGTGTGCTCCTGGCTGTCCTCTTT
GAAAACGGTAATATCGCCGTGTGGCAGTTTCAGCTGCCGTTTGTAGGAAAAGAATCCATC
TCTTCATGCAACACAATTGAGTCAGGAATCACCTCTCCCAGTGTATTGTTTTGGTGGGAA
TATGAGCACAATAATCGAAAAATGAGTGGCCTTATTGTGGGGAGTGCTTTTGGACCCATA
AAAATTCTTCCTGTCAATCTCAAAGCAGTCAAAGGCTATTTCACTTTAAGGCAGCCTGTT
ATCTTGTGGAAAGAAATGGACCAGTTACCTGTGCACAGTATCAAATGTGTGCCACTTTAT
CATCCTTACCAGAAGTGTAGTTGCAGCTTAGTAGTGGCTGCAAGAGGCTCTTATGTATTT
TGGCGTCTTCTTCTGATCTCCAAAGCAGGGCTGAATCTTCACAATTCCCATGTCACAGGC
CTTCACTCACTGCCAATTGTCTCCATGACTGCAGACAAACAGAATGGAACAGTCTATACT
TGCTCCAGTGACGGAAAGGTGAGGCAGGTGATTCCGATTTTCACAGATGTTGCATTGAAG
TTTGAACACCAGTTGATTAAACTCTCAGATGTGTTTGGCTCAGTGAGGACTCACGGGATA
GCAGTGAAGCCCTGCGGTGCATACCTGGCCATCATCACCACTGAGGGCATGATCAACGGC
CTCCACCCTGTTAACAAAAACTACCAGGTCCAATTTGTTACTCTCAAAACCTTTGAAGAA
GCAGCTGCTCAGCTCCTGGAATCTTCAGTTCAAAACCTTTTTAAGCAGGTAGATTTAATA
GACCTAGTACGCTGGAAGATTTTAAAAGATAAACATATCCCTCAATTTTTACAAGAAGCT
TTGGAAAAAAAGATTGAAAGCAGTGGAGTCACCTATTTTTGGCGTTTTAAGCTTTTCCTC
CTGAGGATTTTATATCAGTCAATGCAGAAAACCCCTTCAGAAGCCTTGTGGAAACCCACC
CATGAGGACTCAAAAATCTTACTAGTGGATTCGCCTGGGATGGGCAATGCTGACGATGAA
CAGCAGGAAGAAGGCACTTCTTCCAAACAGGTGGTGAAGCAAGGCCTGCAGGAGAGGAGC
AAGGAAGGAGATGTAGAGGAGCCCACTGATGACTCGCTCCCCACGACTGGAGATGCTGGA
GGCCGTGAGCCAATGGAAGAGAAACTCCTGGAAATCCAAGGGAAAATCGAAGCTGTGGAG
ATGCACTTGACCAGGGAACACATGAAGCCAGTCTTAGGAGAAGTGTATCTGCACACCTGG
ATCACAGAAAACACTAGCATCCCCACCCGCGGACTCTGTAACTTTTTAATGTCTGATGAA
GAGTATGATGACAGAACTGCACGGGTGCTGATTGGACATATCTCAAAGAAGATGAACAAA
CAGACTTTCCCTGAGCACTGTAGTTTGTGTAAAGAGATCTTGCCATTCACAGATCGCAAA
CAGGCAGTCTGTTCCAATGGCCACATTTGGCTCCGGTGCTTCTTAACCTACCAGTCCTGC
CAGAGTTTGATATATAGAAGGTGTTTGCTCCATGACAGCATTGCCCGGCATCCAGCTCCA
GAAGATCCCGACTGGATTAAGAGGTTACTGCAAAGCCCCTGCCCTTTCTGTGATTCTCCT
GTCTTCTAA
Enzyme 6 GenBank Gene ID AF142328 Link Image
Enzyme 6 GeneCard ID GTF3C4 Link Image
Enzyme 6 GenAtlas ID GTF3C4 Link Image
Enzyme 6 HGNC ID HGNC:4667 Link Image
Enzyme 6 Chromosome Location 9
Enzyme 6 Locus 9q34.13
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Hsieh YJ, Kundu TK, Wang Z, Kovelman R, Roeder RG: The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity. Mol Cell Biol. 1999 Nov;19(11):7697-704. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5254
Enzyme 7 Name Choline O-acetyltransferase
Enzyme 7 Synonyms
  1. CHOACTase
  2. Choline acetylase
  3. ChAT
Enzyme 7 Gene Name CHAT
Enzyme 7 Protein Sequence >Choline O-acetyltransferase
MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPH
PRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMA
AKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQ
QKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLIS
GVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPE
PEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSE
WAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANR
WYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMTQSSRKLIRADSVSELPAP
RRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQ
LAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLL
KDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQV
PTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRD
LCSLLPPTESKPLATKEKATRPSQGHQP
Enzyme 7 Number of Residues 748
Enzyme 7 Molecular Weight 82569
Enzyme 7 Theoretical pI 8.69
Enzyme 7 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses
Enzyme 7 Pathways
Enzyme 7 Reactions
  • acetyl-CoA + choline = CoA + O-acetylcholine
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 301096 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P28329 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name CLAT_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2247 bp
ATGGGGCTGAGGACAGCGAAGAAGAGGGGGCTTGGGGGAGGGGGGAAATGGAAGAGAGAG
GAGGGAGGAGGTACAAGAGGAAGGAGAGAAGTGCGGCCAGCTTGCTTTCTCCAGTCGGGT
GGCCGCGGGGACCCGGGCGACGTCGGAGGCCCTGCCGGGAACCCAGGCTGCAGCCCCCAC
CCCCGCGCTGCGACACGCCCCCCACCCCTTCCGGCTCACACCCCCGCCCACACTCCTGAG
TGGTGCGGTGCAGCGTCGGCCGAGGCAGCAGAGCCGAGGAGAGCAGGTCCACACCTCTGC
ATCCCTGCACCAGGACTCACCAAGACGCCCATCCTGGAAAAGGTCCCCCGTAAGATGGCA
GCAAAAACTCCCAGCAGTGAGGAGTCTGGGCTGCCCAAACTGCCCGTGCCCCCGCTGCAG
CAGACCCTGGCCACGTACCTGCAGTGCATGCGACACTTGGTGTCTGAGGAGCAGTTCAGG
AAGAGCCAGGCCATTGTGCAGCAGTTTGGGGCCCCTGGTGGCCTCGGCGAGACCCTGCAG
CAGAAACTCCTGGAGCGGCAGGAGAAGACAGCCAACTGGGTGTCTGAGTACTGGCTGAAT
GACATGTATCTCAACAACCGCCTGGCCCTGCCTGTCAACTCCAGCCCTGCCGTGATCTTT
GCTCGGCAGCACTTCCCTGGCACCGATGACCAGCTGAGGTTTGCAGCCAGCCTCATCTCT
GGTGTACTCAGCTACAAGGCCCTGCTGGACAGCCACTCCATTCCCACTGACTGTGCCAAA
CCGGAGCTGTCAGGGCAGCCCCTTTGCATGAAGCAATACTATGGGCTCTTCTCCTCCTAC
CGGCTCCCCGGCCATACCCAGGACACGCTGGTGGCTCAGAACAGCAGCATCATGCCGGAG
CCTGAGCACGTCATCGTAGCCTGCTGCAATCAGTTCTTTGTCTTGGATGTTGTCATTAAT
TTCCGCCGTCTCAGTGAGGGGGATCTGTTCACTCAGTTGAGAAAGATAGTCAAAATGGCT
TCCAACGAGGACGAGCGTTTGCCTCCAATTGGCCTGCTGACGTCTGACGGGAGGAGCGAG
TGGGCCGAGGCCAGGACGGTCCTCGTGAAAGACTCCACCAACCGGGACTCGCTGGACATG
ATTGAGCGCTGCATCTGCCTTGTATGCCTGGACGGCCCAGGAGGCGTGGAGCTCAGCGAC
ACCCACAGGGCACTCCAGCTCCTTCACGGCGGAGGCTACAGCAAGAACGGGGCCAATCGC
TGGTACGACAAGTCCCTGCAGTTTGTGGTGGGCCGAGACGCGACCTGCGGTGTGGTGTGC
GAACACTCCCCATTCGATGGCATCGTCCTGGTGCAGTGCACTGAGCATCTGCTCAAGCAC
ATGACGCAGAGCAGCAGGAAGCTGATCCGAGCAGACTCCGTCAGCGAGCTCCCCGCCCCC
CGGAGGCTGCGGTGGAAATGCTCCCCGGAAATTCAAGGCCACTTAGCCTCCTCGGCAGAA
AAACTTCAACGAATAGTAAAGAACCTTGACTTCATTGTCTATAAGTTTGACAACTATGGG
AAAACATTCATTAAGAAGCAGAAATGCAGCCCTGATGCCTTCATCCAGGTGGCCCTCCAG
CTGGCCTTCTACAGGCTCCACCGAAGACTGGTGCCCACCTACGAGAGCGCGTCCATCCGC
CGATTCCAGGAGGGACGCGTGGACAACATCAGATCGGCCACTCCAGAGGCACTGGCTTTT
GTGAGAGCCGTGACTGACCACAAGGCTGCTGTGCCAGCTTCTGAGAAGCTTCTGCTCCTG
AAGGATGCCATCCGTGCCCAGACTGCATACACAGTCATGGCCATAACAGGGATGGCCATT
GACAACCACCTGCTGGCACTGCGGGAGCTGGCCCGGGCCATGTGCAAGGAGCTGCCCGAG
ATGTTCATGGATGAAACCTACCTGATGAGCAACCGGTTTGTCCTCTCCACTAGCCAGGTG
CCCACAACCACGGAGATGTTCTGCTGCTATGGTCCTGTGGTCCCAAATGGGTATGGTGCC
TGCTACAACCCCCAGCCAGAGACCATCCTTTTCTGCATCTCTAGCTTTCACAGCTGCAAA
GAGACTTCTTCTAGCAAGTTTGCAAAAGCTGTGGAAGAAAGCCTCATTGACATGAGAGAC
CTCTGCAGTCTGCTGCCGCCTACTGAGAGCAAGCCATTGGCAACAAAGGAAAAAGCCACG
AGGCCCAGCCAGGGACACCAACCTTGA
Enzyme 7 GenBank Gene ID S56138 Link Image
Enzyme 7 GeneCard ID CHAT Link Image
Enzyme 7 GenAtlas ID CHAT Link Image
Enzyme 7 HGNC ID HGNC:1912 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Oda Y, Nakanishi I, Deguchi T: A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells. Brain Res Mol Brain Res. 1992 Dec;16(3-4):287-94. [PubMed Link Image]
  2. Ohno K, Tsujino A, Brengman JM, Harper CM, Bajzer Z, Udd B, Beyring R, Robb S, Kirkham FJ, Engel AG: Choline acetyltransferase mutations cause myasthenic syndrome associated with episodic apnea in humans. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):2017-22. [PubMed Link Image]
  3. Lorenzi MV, Trinidad AC, Zhang R, Strauss WL: Two mRNAs are transcribed from the human gene for choline acetyltransferase. DNA Cell Biol. 1992 Oct;11(8):593-603. [PubMed Link Image]
  4. Toussaint JL, Geoffroy V, Schmitt M, Werner A, Garnier JM, Simoni P, Kempf J: Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions. Genomics. 1992 Feb;12(2):412-6. [PubMed Link Image]
  5. Cervini R, Rocchi M, DiDonato S, Finocchiaro G: Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene. Neurosci Lett. 1991 Nov 11;132(2):191-4. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5256
Enzyme 8 Name Histone acetyltransferase PCAF
Enzyme 8 Synonyms
  1. P300/CBP-associated factor
  2. P/CAF
  3. Histone acetylase PCAF
Enzyme 8 Gene Name PCAF
Enzyme 8 Protein Sequence >Histone acetyltransferase PCAF
MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAA
AGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTP
PRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEED
ADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKE
RQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPR
YETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQ
NSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSG
LEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSA
RDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFD
PKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKH
DILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFS
VIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSK
EPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNR
YYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
Enzyme 8 Number of Residues 832
Enzyme 8 Molecular Weight 93014
Enzyme 8 Theoretical pI 9.37
Enzyme 8 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 5468533 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q92831 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PCAF_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2499 bp
ATGTCCGAGGCTGGCGGGGCCGGGCCGGGCGGCTGCGGGGCAGGAGCCGGGGCAGGGGCC
GGGCCCGGGGCGCTGCCCCCGCAGCCTGCGGCGCTTCCGCCCGCGCCCCCGCAGGGCTCC
CCCTGCGCCGCTGCCGCCGGGGGCTCGGGCGCCTGCGGTCCGGCGACGGCAGTGGCTGCA
GCGGGCACGGCCGAAGGACCGGGAGGCGGTGGCTCGGCCCGAATCGCCGTGAAGAAAGCG
CAACTACGCTCCGCTCCGCGGGCCAAGAAACTGGAGAAACTCGGAGTGTACTCCGCCTGC
AAGGCCGAGGAGTCTTGTAAATGTAATGGCTGGAAAAACCCTAACCCCTCACCCACTCCC
CCCAGAGCCGACCTGCAGCAAATAATTGTCAGTCTAACAGAATCCTGTCGGAGTTGTAGC
CATGCCCTAGCTGCTCATGTTTCCCACCTGGAGAATGTGTCAGAGGAAGAAATGAACAGA
CTCCTGGGAATAGTATTGGATGTGGAATATCTCTTTACCTGTGTCCACAAGGAAGAAGAT
GCAGATACCAAACAAGTTTATTTCTATCTATTTAAGCTCTTGAGAAAGTCTATTTTACAA
AGAGGAAAACCTGTGGTTGAAGGCTCTTTGGAAAAGAAACCCCCATTTGAAAAACCTAGC
ATTGAACAGGGTGTGAATAACTTTGTGCAGTACAAATTTAGTCACCTGCCAGCAAAAGAA
AGGCAAACAATAGTTGAGTTGGCAAAAATGTTCCTAAACCGCATCAACTATTGGCATCTG
GAGGCACCATCTCAACGAAGACTGCGATCTCCCAATGATGATATTTCTGGATACAAAGAG
AACTACACAAGGTGGCTGTGTTACTGCAACGTGCCACAGTTCTGCGACAGTCTACCTCGG
TACGAAACCACACAGGTGTTTGGGAGAACATTGCTTCGCTCGGTCTTCACTGTTATGAGG
CGACAACTCCTGGAACAAGCAAGACAGGAAAAAGATAAACTGCCTCTTGAAAAACGAACT
CTAATCCTCACTCATTTCCCAAAATTTCTGTCCATGCTAGAAGAAGAAGTATATAGTCAA
AACTCTCCCATCTGGGATCAGGATTTTCTCTCAGCCTCTTCCAGAACCAGCCAGCTAGGC
ATCCAAACAGTTATCAATCCACCTCCTGTGGCTGGGACAATTTCATACAATTCAACCTCA
TCTTCCCTTGAGCAGCCAAACGCAGGGAGCAGCAGTCCTGCCTGCAAAGCCTCTTCTGGA
CTTGAGGCAAACCCAGGAGAAAAGAGGAAAATGACTGATTCTCATGTTCTGGAGGAGGCC
AAGAAACCCCGAGTTATGGGGGATATTCCGATGGAATTAATCAACGAGGTTATGTCTACC
ATCACGGACCCTGCAGCAATGCTTGGACCAGAGACCAATTTTCTGTCAGCACACTCGGCC
AGGGATGAGGCGGCAAGGTTGGAAGAGCGCAGGGGTGTAATTGAATTTCACGTGGTTGGC
AATTCCCTCAACCAGAAACCAAACAAGAAGATCCTGATGTGGCTGGTTGGCCTACAGAAC
GTTTTCTCCCACCAGCTGCCCCGAATGCCAAAAGAATACATCACACGGCTCGTCTTTGAC
CCGAAACACAAAACCCTTGCTTTAATTAAAGATGGCCGTGTTATTGGTGGTATCTGTTTC
CGTATGTTCCCATCTCAAGGATTCACAGAGATTGTCTTCTGTGCTGTAACCTCAAATGAG
CAAGTCAAGGGCTATGGAACACACCTGATGAATCATTTGAAAGAATATCACATAAAGCAT
GACATCCTGAACTTCCTCACATATGCAGATGAATATGCAATTGGATACTTTAAGAAACAG
GGTTTCTCCAAAGAAATTAAAATACCTAAAACCAAATATGTTGGCTATATCAAGGATTAT
GAAGGAGCCACTTTAATGGGATGTGAGCTAAATCCACGGATCCCGTACACAGAATTTTCT
GTCATCATTAAAAAGCAGAAGGAGATAATTAAAAAACTGATTGAAAGAAAACAGGCACAA
ATTCGAAAAGTTTACCCTGGACTTTCATGTTTTAAAGATGGAGTTCGACAGATTCCTATA
GAAAGCATTCCTGGAATTAGAGAGACAGGCTGGAAACCGAGTGGAAAAGAGAAAAGTAAA
GAGCCCAGAGACCCTGACCAGCTTTACAGCACGCTCAAGAGCATCCTCCAGCAGGTGAAG
AGCCATCAAAGCGCTTGGCCCTTCATGGAACCTGTGAAGAGAACAGAAGCTCCAGGATAT
TATGAAGTTATAAGGTTCCCCATGGATCTGAAAACCATGAGTGAACGCCTCAAGAATAGG
TACTACGTGTCTAAGAAATTATTCATGGCAGACTTACAGCGAGTCTTTACCAATTGCAAA
GAGTACAACGCCGCTGAGAGTGAATACTACAAATGTGCCAATATCCTGGAGAAATTCTTC
TTCAGTAAAATTAAGGAAGCTGGATTAATTGACAAGTGA
Enzyme 8 GenBank Gene ID U57317 Link Image
Enzyme 8 GeneCard ID PCAF Link Image
Enzyme 8 GenAtlas ID PCAF Link Image
Enzyme 8 HGNC ID HGNC:8638 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed Link Image]
  2. Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [PubMed Link Image]
  3. Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW: TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem. 1997 Oct 31;272(44):27629-34. [PubMed Link Image]
  4. Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM: Structure and ligand of a histone acetyltransferase bromodomain. Nature. 1999 Jun 3;399(6735):491-6. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5257
Enzyme 9 Name Carnitine O-acetyltransferase
Enzyme 9 Synonyms
  1. Carnitine acetylase
  2. CAT
  3. Carnitine acetyltransferase
  4. CrAT
Enzyme 9 Gene Name CRAT
Enzyme 9 Protein Sequence >Carnitine O-acetyltransferase
MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSE
EEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSP
GVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSC
RVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSS
LQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVY
RSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGFPIVTLLDYVIE
YTKKPELVRSPMVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKD
FPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVK
AMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMD
TSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNA
ARLAHYLEKALLDMRALLQSHPRAKL
Enzyme 9 Number of Residues 626
Enzyme 9 Molecular Weight 70927
Enzyme 9 Theoretical pI 8.63
Enzyme 9 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • acetyl-CoA + carnitine = CoA + O-acetylcarnitine
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-16
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 927415 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P43155 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name CACP_HUMAN Link Image
Enzyme 9 PDB ID 1S5O Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1876 bp
AGCCTTCGCTGCCAGGACCGTGGTGAAGCCTCTGGGCTTCCTGAAGCCCTTCTCCTTGAT
GAAGGCTTCCAGCCGCTTCAAGGCACACCAGGATGCCCTGCCACGGCTGCCCGTGCCCCC
TCTCCAGCAGTCCCTGGACCACTACCTGAAGGCGCTGCAGCCCATCGTGAGTGAGGAGGA
GTGGGCCCACACCAAGCAGCTGGTGGATGAGTTTCAGGCCTCAGGAGGTGTAGGGGAGCG
CCTGCAGAAGGGGCTGGGGCGTCGGGCCAGGAAGACGGAGAACTGGCTGTCTGAGTGGTG
GCTCAAGACCGCCTACCTCCAGTACCGCCAGCCTGTGGTCATCTACTCGAGCCCAGGCGT
GATGCTACCCAAGCAGGACTTCGTGGACCTGCAGGGTCAGCTCCGATTTGCTGCCAAACT
CATTGAGGGTGTGTTGGATTTCAAGGTCATGATTGACAACGAGACCCTGCCCGTGGAGTA
CCTGGNGGGGAAGCCACTGTGCATGAACCAGTACTATCAGATCTTGTCCTCCTGCCGAGT
GCCGGGCCCCAAGCAGGACACAGTCAGCAACTTCAGCAAGACCAAGAAGCCTCCCACGCA
CATCACCGTGGTACACAACTACCAGTTTTTTGAGCTGGATGTGTACCACAGTGACGGGAC
ACCCCTCACTGCGGATCAGATCTTTGTGCAGCTGGAGAAGATCTGGAACTCATCCCTACA
GACCAACAAGGAGCCTGTGGGCATCCTCACCTCCAACCACCGCAACTCCTGGGCCAAGGC
ATACAACACCCTCATCAAAGACAAGGTGAACCGGGATTCCGTGCGCTCCATCCAGAAGAG
CATCTTCACCGTGTGCCTAGATGCAACCATGCCCAGGGTCTCAGAAGACGTGTACCGCAG
CCACGTGGCAGGCCAGATGCTGCATGGGGGCGGCAGCAGGCTCAACAGCGGCAACCGCTG
GTTTGACAAGACGCTGCAGTTCATCGTGGCAGAAGATGGCTCCTGTGGGCTTGTGTACGA
GCATGCTGCAGCNGAGGGTTTCCCTATTGTCACCCTTCTGGACTATGTCATCGAGTACAC
GAAGAAACCCGAGCTTGTGCNGTCTCCCATGGTGCCCCTGCCCATGCCCAAGAAGCTGCG
GTTCAACATCACCCCCGAGATCAAGAGCGACATCGAGAAGGCCAAGCAGAACCTCAGCAT
CATGATCCANNACCTGGATATCACCGTGATGGTGTTCCACCATTTTGGAAAAGACTTCCC
CAAGTCGGAGAAGCTAAGCCCAGATGCCTTCATCCAGATGGCTTTGCAGCTGGCCTACTA
CAGGATCTACGGACAGGCATGTGCCACCTATGAAAGTNCNTCCCTGCGCATGTTTCACCT
GGGCCGCACCGACACCATCCGCTCGGCTTCCATGGACTCACTCACCTTTGTCAAGGCCAT
GGATGACTCCAGCGTCACGGAGCACCAGAAGGTGGAGCTGCTGCGGAAGGCCGTGCAGGC
CCACCGGGGCTACACCGACCGGGCCATCCGCGGGGAGGCCTTTGGTCGACACCTGCTGGG
CCTGAAGCTGCAGGCCATCGAGGACCTGGTGAGCACGCCCGACATCTTCATGGACACCTC
CTACGCCATCGCCATGCACTTCCACCTCTCCACCAGCCAGGTCCCTGCCAAGACAGACTG
TGTCATGTTCTTCGGGCCCGTGGTCCCCGACGGCTACGGTGTCTGCTATAACCCCATGGA
GGCCCACATCAACTTCTCCCTGTCGGCCTACAACAGCTGCGCGGAGACCAACGCCGCCCG
CCTGGCGCATTACCTGGAGAAGGCGCTCCTGGACATGCGTGCCCTGCTGCAGAGCCACCC
CCGGGCCAAGCTCTGA
Enzyme 9 GenBank Gene ID X78706 Link Image
Enzyme 9 GeneCard ID CRAT Link Image
Enzyme 9 GenAtlas ID CRAT Link Image
Enzyme 9 HGNC ID HGNC:2342 Link Image
Enzyme 9 Chromosome Location 9
Enzyme 9 Locus 9q34.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Corti O, Finocchiaro G, Rossi E, Zuffardi O, DiDonato S: Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1. Genomics. 1994 Sep 1;23(1):94-9. [PubMed Link Image]
  2. Corti O, DiDonato S, Finocchiaro G: Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations. Biochem J. 1994 Oct 1;303 ( Pt 1):37-41. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5258
Enzyme 10 Name Diamine acetyltransferase 1
Enzyme 10 Synonyms
  1. Spermidine/spermine N(1- acetyltransferase 1
  2. SSAT
  3. SSAT-1
  4. Putrescine acetyltransferase
  5. Polyamine N-acetyltransferase 1
Enzyme 10 Gene Name SAT1
Enzyme 10 Protein Sequence >Diamine acetyltransferase 1
MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVILTEKDLLEDGFGEHPFYHCLVAEVP
KEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMRC
RCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMATEE
Enzyme 10 Number of Residues 171
Enzyme 10 Molecular Weight 20024
Enzyme 10 Theoretical pI 4.82
Enzyme 10 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 10 General Function Transcription
Enzyme 10 Specific Function Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine = spermidine >> spermine > 1- N-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells
Enzyme 10 Pathways
Enzyme 10 Reactions
  • acetyl-CoA + an alkane-alpha,omega -diamine = CoA + an N-acetyldiamine
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 338392 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P21673 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name SAT1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >516 bp
ATGGCTAAATTCGTGATCCGCCCAGCCACTGCCGCCGACTGCAGTGACATACTGCGGCTG
ATCAAGGAGCTGGCTAAATATGAATACATGGAAGAACAAGTAATCTTAACTGAAAAAGAT
CTGCTAGAAGATGGTTTTGGAGAGCACCCCTTTTACCACTGCCTGGTTGCAGAAGTGCCG
AAAGAGCACTGGACTCCGGAAGGACACAGCATTGTTGGTTTTGCCATGTACTATTTTACC
TATGACCCGTGGATTGGCAAGTTATTGTATCTTGAGGACTTCTTCGTGATGAGTGATTAT
AGAGGCTTTGGCATAGGATCAGAAATTCTGAAGAATCTAAGCCAGGTTGCAATGAGGTGT
CGCTGCAGCAGCATGCACTTCTTGGTAGCAGAATGGAATGAACCATCCATCAACTTCTAT
AAAAGAAGAGGTGCTTCTGATCTGTCCAGTGAAGAGGGTTGGAGACTGTTCAAGATCGAC
AAGGAGTACTTGCTAAAAATGGCAACAGAGGAGTGA
Enzyme 10 GenBank Gene ID M77693 Link Image
Enzyme 10 GeneCard ID SAT1 Link Image
Enzyme 10 GenAtlas ID SAT1 Link Image
Enzyme 10 HGNC ID HGNC:10540 Link Image
Enzyme 10 Chromosome Location X
Enzyme 10 Locus Xp22.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Casero RA Jr, Celano P, Ervin SJ, Applegren NB, Wiest L, Pegg AE: Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase. J Biol Chem. 1991 Jan 15;266(2):810-4. [PubMed Link Image]
  2. Xiao L, Celano P, Mank AR, Pegg AE, Casero RA Jr: Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase. Biochem Biophys Res Commun. 1991 Aug 30;179(1):407-15. [PubMed Link Image]
  3. Xiao L, Celano P, Mank AR, Griffin C, Jabs EW, Hawkins AL, Casero RA Jr: Structure of the human spermidine/spermine N1-acetyltransferase gene (exon/intron gene organization and localization to Xp22.1). Biochem Biophys Res Commun. 1992 Sep 30;187(3):1493-502. [PubMed Link Image]
  4. Casero RA Jr, Celano P, Ervin SJ, Wiest L, Pegg AE: High specific induction of spermidine/spermine N1-acetyltransferase in a human large cell lung carcinoma. Biochem J. 1990 Sep 15;270(3):615-20. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5259
Enzyme 11 Name Serotonin N-acetyltransferase
Enzyme 11 Synonyms
  1. Aralkylamine N- acetyltransferase
  2. AA-NAT
  3. Serotonin acetylase
Enzyme 11 Gene Name AANAT
Enzyme 11 Protein Sequence >Serotonin N-acetyltransferase
MSTQSTHPLKPEAPRLPPGIPESPSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVL
GVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLMQESLTLHRSGGHIAH
LHVLAVHRAFRQQGRGPILLWRYLHHLGSQPAVRRAALMCEDALVPFYERFSFHAVGPCA
ITVGSLTFMELHCSLRGHPFLRRNSGC
Enzyme 11 Number of Residues 207
Enzyme 11 Molecular Weight 23344
Enzyme 11 Theoretical pI 7.57
Enzyme 11 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Catalyzes the N-acetylation of serotonin into N- acetylserotonin
Enzyme 11 Pathways
Enzyme 11 Reactions
  • acetyl-CoA + an aralkylamine = CoA + an N-acetylaralkylamine
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 1389594 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q16613 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SNAT_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >624 bp
ATGTCCACGCAGAGCACCCACCCCCTGAAACCTGAGGCCCCACGTCTGCCACCTGGGATC
CCCGAGTCCCCGAGCTGTCAGCGGCGCCACACACTCCCTGCCAGTGAGTTTCGCTGCCTC
ACCCCGGAGGACGCTGTCAGCGCCTTTGAGATCGAGCGTGAAGCCTTCATCTCCGTCTTG
GGCGTCTGCCCCCTGTACCTGGATGAGATCCGGCACTTCCTGACCCTATGTCCAGAGCTG
TCCCTGGGCTGGTTCGAGGAGGGCTGCCTTGTGGCCTTCATCATCGGCTCGCTCTGGGAC
AAGGAGAGACTCATGCAGGAGTCACTGACGCTGCACAGGTCTGGGGGCCACATAGCCCAC
CTGCATGTGCTGGCCGTGCACCGCGCCTTCCGGCAGCAGGGCAGGGGCCCCATCCTGCTG
TGGCGCTACCTGCACCACCTGGGCAGCCAGCCGGCCGTGCGCCGGGCCGCGCTCATGTGC
GAGGACGCGCTGGTACCCTTCTATGAGAGGTTCAGCTTCCACGCCGTGGGCCCCTGCGCC
ATCACCGTGGGCTCCCTCACCTTCATGGAGCTCCACTGCTCCCTGCGGGGCCACCCCTTC
CTGCGCAGGAACAGCGGCTGCTGA
Enzyme 11 GenBank Gene ID U40391 Link Image
Enzyme 11 GeneCard ID AANAT Link Image
Enzyme 11 GenAtlas ID AANAT Link Image
Enzyme 11 HGNC ID HGNC:19 Link Image
Enzyme 11 Chromosome Location 17
Enzyme 11 Locus 17q25
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR: The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression. Genomics. 1996 May 15;34(1):76-84. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5260
Enzyme 12 Name 3-ketoacyl-CoA thiolase, mitochondrial
Enzyme 12 Synonyms
  1. Beta- ketothiolase
  2. Acetyl-CoA acyltransferase
  3. Mitochondrial 3-oxoacyl- CoA thiolase
  4. T1
Enzyme 12 Gene Name ACAA2
Enzyme 12 Protein Sequence >3-ketoacyl-CoA thiolase, mitochondrial
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Enzyme 12 Number of Residues 397
Enzyme 12 Molecular Weight 41925
Enzyme 12 Theoretical pI 8.21
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Lipid transport and metabolism
Enzyme 12 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 12 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 12 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-12
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 509676 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P42765 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name THIM_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1194 bp
ATGCGTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTACTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGTGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
Enzyme 12 GenBank Gene ID D16294 Link Image
Enzyme 12 GeneCard ID ACAA2 Link Image
Enzyme 12 GenAtlas ID ACAA2 Link Image
Enzyme 12 HGNC ID HGNC:83 Link Image
Enzyme 12 Chromosome Location 18
Enzyme 12 Locus 18q21.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, Suzuki Y, Mori M, et al.: Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase. Biochim Biophys Acta. 1993 Nov 16;1216(2):304-6. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5262
Enzyme 13 Name Testis-specific chromodomain protein Y 1
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name CDY1
Enzyme 13 Protein Sequence >Testis-specific chromodomain protein Y 1
MASQEFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQTE
KQKKLTWTTTSRIFSNNARRRTSRSTKANYSKNSPKTPVTDKHHRSKNRKLFAASKNVRR
KAASILSDTKNMEIINSTIETLAPDSPFDHKTVSGFQKLEKLDPIAADQQDTVVFKVTEG
KLLRDPLSRPGAEQTGIQNKTQIHPLMSQMSGSVTASMATGSATRKGIVVLIDPLAANGT
TDMHTSVPRVKGGQRNITDDSRDQPFIKKMHFTIRLTESASTYRDIVVKKEDGFTQIVLS
TRSTEKNALNTEVIKEIVNALNSAAADDSKLVLFSAAGSVFCCGLDFGYFVKHLRNNRNT
ASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTF
GQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIK
ELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESMLKYVENKIDEF
Enzyme 13 Number of Residues 540
Enzyme 13 Molecular Weight 60474
Enzyme 13 Theoretical pI 9.61
Enzyme 13 GO Classification
Function
  • binding
  • chromatin binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin assembly or disassembly
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • chromatin
  • chromosome
  • intracellular membrane-bound organelle
  • intracellular non-membrane-bound organelle
  • membrane-bound organelle
  • non-membrane-bound organelle
  • nucleus
  • organelle
Enzyme 13 General Function Lipid transport and metabolism
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3342716 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9Y6F8 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name CDY1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1665 bp
ATGGCTTCCCAGGAGTTTGAGGTTGAAGCTATTGTTGACAAAAGACAGGATAAAAATGGG
AATACACAGTATTTGGTTCGGTGGAAAGGTTATGACAAACAGGATGACACTTGGGAACCA
GAGCAGCACCTCATGAACTGTGAAAAATGTGTACATGATTTTAATAGACGACAGACTGAA
AAACAGAAAAAACTGACATGGACTACAACCAGTAGAATTTTTTCAAACAATGCCAGAAGA
AGAACTTCCAGATCTACAAAAGCAAACTATTCTAAGAACTCTCCTAAAACGCCAGTGACT
GATAAACACCACAGGTCCAAAAACCGCAAGTTATTTGCTGCCAGCAAGAACGTTAGGAGA
AAGGCAGCTTCAATTCTCTCCGACACAAAGAATATGGAGATAATAAATTCAACTATTGAG
ACCCTTGCACCTGACAGCCCCTTTGACCACAAAACTGTGAGTGGCTTTCAGAAACTTGAG
AAACTGGACCCTATTGCAGCAGATCAGCAGGACACGGTGGTCTTCAAGGTGACAGAAGGG
AAACTCCTCCGGGACCCTTTGTCACGTCCTGGTGCAGAACAGACTGGAATACAGAACAAG
ACTCAGATACACCCACTAATGTCGCAGATGTCTGGCTCAGTTACTGCTTCTATGGCCACA
GGTTCAGCTACCCGAAAGGGTATAGTGGTATTAATAGACCCATTAGCAGCCAATGGGACA
ACAGACATGCATACCTCAGTTCCAAGAGTGAAAGGTGGGCAAAGAAATATTACTGATGAC
AGCAGAGACCAGCCTTTTATCAAGAAGATGCACTTCACCATAAGGCTAACAGAAAGTGCC
AGCACATACAGAGACATTGTAGTGAAGAAAGAGGATGGATTCACCCAGATAGTGCTATCA
ACTAGATCGACAGAAAAAAATGCACTGAATACAGAAGTAATTAAAGAAATAGTTAATGCT
CTGAATAGCGCTGCTGCAGATGACAGCAAGCTCGTGCTGTTCAGTGCAGCTGGAAGTGTC
TTTTGCTGCGGTCTTGATTTTGGGTACTTTGTGAAGCACTTAAGGAATAACAGAAACACA
GCAAGCCTTGAAATGGTGGACACCATCAAGAACTTTGTGAATACTTTTATTCAATTTAAA
AAGCCTATTGTTGTATCAGTCAATGGCCCTGCGATTGGACTAGGTGCATCCATCCTGCCT
CTTTGTGATCTCGTGTGGGCTAATGAAAAGGCTTGGTTCCAAACCCCTTATACGACCTTT
GGACAGAGTCCAGATGGCTGTTCTTCTATTACATTCCCCAAAATGATGGGTAAAGCATCT
GCCAATGAAATGTTAATTGCTGGGCGAAAGCTGACAGCAAGGGAGGCATGCGCCAAAGGC
CTGGTCTCTCAGGTATTTTTGACTGGAACTTTCACCCAAGAGGTTATGATTCAAATTAAG
GAGCTTGCCTCATACAATCCAATTGTACTGGAAGAATGTAAGGCCCTCGTTCGCTGTAAT
ATTAAGTTGGAGTTGGAACAGGCCAATGAGAGAGAGTGTGAGGTGCTGAGGAAGATCTGG
AGCTCAGCCCAAGGGATAGAATCCATGTTAAAAATACCTCTGTTGGGATATAAAGCAGCC
TTCCCTCCCAGAAAGACACAGAATGATCAGAGATGGTGCCCTTGA
Enzyme 13 GenBank Gene ID AF000981 Link Image
Enzyme 13 GeneCard ID CDY1 Link Image
Enzyme 13 GenAtlas ID CDY1 Link Image
Enzyme 13 HGNC ID HGNC:1809 Link Image
Enzyme 13 Chromosome Location Y
Enzyme 13 Locus Yq11.23
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Lahn BT, Page DC: Functional coherence of the human Y chromosome. Science. 1997 Oct 24;278(5338):675-80. [PubMed Link Image]
  2. Lahn BT, Page DC: Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome. Nat Genet. 1999 Apr;21(4):429-33. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5264
Enzyme 14 Name Fatty acid synthase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name FASN
Enzyme 14 Protein Sequence >Fatty acid synthase
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTTVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
Enzyme 14 Number of Residues 2511
Enzyme 14 Molecular Weight 273403
Enzyme 14 Theoretical pI 6.39
Enzyme 14 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • oxidoreductase activity
  • phosphopantetheine binding
  • transferase activity
  • vitamin binding
Process
  • biosynthesis
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
Enzyme 14 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 14 Specific Function Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein
Enzyme 14 Pathways
Enzyme 14 Reactions
  • (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = 2-hexadecenoyl-[acyl-carrier protein] + H2O
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 1049053 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P49327 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name FAS_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >7515 bp
ATGGAGGAGGTGGTGATTGCCGGCATGTTCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCTGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGCTACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAACGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCTGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
AAGGTCTACACCACCATCCTGAACAAAGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCTCAGGATATCCAGGAGCAGCCTATCCGCTCGTTGTACCAGTCGGCCGGA
GTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGACCAGGCACCAAGGTGGGCGAC
CCCCAGGAGCGTAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTGCTC
ATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTCGACGCCCTG
GCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCATAGC
CCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCCCTG
CCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACATGCAC
ATCATCCTGAGGCCCAACACGCAGTCCGCCCCCGCACCCGCCCCACATGCCACCCTGCCC
CGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAGGGC
CTCCGGCACAGCCAGGGCCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTCCCC
GCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGACGCGGTGGCCCAGA
GTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGCACA
CAGTGGCGTGGAATGGGGCTGAGCCTTATGCGCCTGGACCGCTTCCGAGATTCCATCCTA
CGCTCCGATGAGGCTGTGAACCGATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGCACA
GACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAGATA
GGCCTCATAGACCTGCTGAGCTGCATGGGACCTGAGGCAGATGGCATCGTCGGCCACTCC
CTGGGGGAGTGGCTGTCGGTACGCGACGGCTGCCTGTCCCAGGAGGAGGCCGTCCTCGCT
GCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCCACTTCCCGCCGGCGCCATGGCAGCC
GTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCTGCGGTGGTGCCCGCCTGC
CACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAGTTCGTG
GAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATGGCCTTC
CACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAGGTGATC
CGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCCCAGTGG
CACAGCAGCCTGGCACGCACGTCTTCCGCCGAGTACAATGTCAACAACCTGGTGAGCCCT
GTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAGATCGCC
CCGACCCCGTGCCCTCAGGCTGTCCTGAAGCGGGTCCGTAAGCCGAGCTGCACCATCATC
CCCCGTATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATCGGCAGG
CTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAGTCCCCA
GCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTGGCCTGG
GACGCGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCACCATCTAC
ACATGCACACCAAGCTCCGAGTCTCCTGACCGCTACCTGGTGGACCACACCATCGACGGT
CGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCCCGCGCC
TGGGCTGGGCTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCAGCACCAGGCCACC
ATCCTGCCCAAGACTGGGACAGTGTCCTTGGAGGTACGGCTCCTGGAGGCCACCGGTGCC
TTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAGTGGGATGAC
CCTGACCCCAGGCTCTTCGACCACCCGGAAAGTCCCCACCCCAATTCCCCACGGAGTCCC
CTCTTCCTGGCCCAGGCAGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGACTACGGC
CCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTGCTGTGG
AAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGCTCGGCC
AAGCACGGCCTGTACCTACCCACCCGTGTCACCGCCATCCACATCGACCCTGCCACCCAC
AGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTGAGCAGG
TGGCCGAGGGTCACAGTGGCGGGAGGCGTCCACATCTCCGGGCTCCACACTGAGTCGGCC
CCGCGGCGGCACGAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACTCCCCAC
ACGGAGGAGGGGTGCCTGTCTGAGCACGCTGCCCTCGAGGAGGAGCTGCAACTGTGCAAG
GGGCTGGTCGAGGCACTCGAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTGGTGCCG
GACTGGACGGGGCCCAGATCCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGGCTGTTG
TCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAGGTGCTG
GCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGACTCCCCG
GCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATGAAGGTG
GTGGAGGTGCTGGCCGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTCAGCCCC
CATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTGGAGGCT
GCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCAGACCCT
GCCCCCAGCGCCCTGGGCAGCGCGGACCTCCTGGTGTGCAACTGTGCTGTGGCTGCCCTC
GGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGCTTTCTG
CTCCTGCACACACTGCTCCGGGGGCACCCTCGGGACATCGTGGCCTTCCTCACCTCCACT
GAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTCTTCTCCAGG
GTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCGCCACGCTCTTCCTGTGC
CGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACCAGCTTCCGC
TGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCTGTGTGGCTG
AAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTCCGCCGAGAG
CCCGGCGGAACCGTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACCTCCCACGTCCCG
GAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGACCTGGTGATGAAC
GTCTACCGCGACGGGGCCTGGGGGGTTTTCCGCCACTTCCTGCTGGAGGACAAGCCTGAG
GAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGACCTGTCCTCCATCCGC
TGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGCGCCCAGCTCTGCACG
GTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACTGGCAAGCTGTCCCCT
GATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGTATGGAGTTCTCGGGC
CGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAGGGCCTGGCCACCTCT
GTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGGACGCTGGAGGAGGCG
GCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTGGTGCGTGGGCGGGTG
CGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTGGGCCAGGCCGCCATC
GCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGGTCGGCTGAGAAGCGG
GCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTCGCCAACTCCCGGGAC
ACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGCGTTGACCTGGTCTTG
AACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTCGGTACGCACGGTCGC
TTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTCGGCATGGCTATCTTC
CTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTCAACGAGAGCAGTGCT
GACTGGCGGGAGGTGTGGGCGCTTGTCGAGGCCGCCATCCGGGATGGGGTGGTACGGCCC
CTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTCCGCTACATGGCCCAA
GGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAGCCGGCAGTGCTGAAG
GGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTCTGCCCGGCCCACAAGAGC
TACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTGGCGCAGTGGCTGATACAG
CGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATCCGGACAGGCTACCAGGCC
AAGCAGGTCCGCCGGTGGAGGCGCCAGGGGCTACAGGTGCAGGTGTCCACCAGCAACATC
AGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCGCAGCTTGGGCCCGTGGGG
GGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTGGAGAACCAGACCCCAGAG
TTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTGAACCTGGACAGGGTGACC
CGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCCTCTGTGAGCTGCGGGCGT
GGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCCATGGAGCGTATCTGTGAG
AAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGGGGCGCCATCGGCACCGTG
GGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTCAGTGGCACGCTGCCCACG
CGCATTGGCGTCCTTGGCCTGGAGGTGCTGGACCTCTTCCTGAACCAGCCCCACATGGTC
CTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGACAGGGACAGCCAGCGG
GACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTGGCTGCTGTCAACCTG
GGCGGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGCGCCGGTGCGCCAGACG
CTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGGCAACTCACGCTCCGG
AAACTGCAGGAGCTGTCCTCAAAGGCGGATGAAGCCAGCGAGCTGGCATGCCCCACGCCC
AAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGCTCCCTGCTGGTGAAA
CCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCGGAGCGGCCCCTGTTC
CTGGTGCACCCAATCGAGGCTACCACCGTGTTCCACAGCCTCGGTCCCGGTCTCAGCATC
CCCACCTATGGCCTGCAGTGCACCCCGGCTGCGCCCCTTGACAGCATCCACAGCCTGGCT
GCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGCCCCTACCGCGTGGCCGGC
TACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAGCTGCAGGCCCAGCAGAGC
CCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCGCCCACCTACGTACTGGCC
TACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTAAGGCTGAGGCTGAGACGGAG
GCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCACAACAGGGTGCTGGAGGCG
CTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCCGTGGACCTGATCATCAAG
AGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCCCGGTCCTTCTACTACAGG
CTGCGTGCCGCTGACCAGTATACACCCAAGGCCAAGTACAGTGGCAACGTGATGCTACTG
CGGGCCAAGACGGGTGGCCGCTACGGCGAGGACCTGGGCGCGGACTACAACCTCTCCCAG
GTATGCGACGGGAAAGTATCCGTCCATATCATCGAGGGTGACCACCGCACGCTGCTGGAG
GGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCCCTGGCTGAGCCACGTGTG
AGTCGGGAGGGCTAG
Enzyme 14 GenBank Gene ID U26644 Link Image
Enzyme 14 GeneCard ID FASN Link Image
Enzyme 14 GenAtlas ID FASN Link Image
Enzyme 14 HGNC ID HGNC:3594 Link Image
Enzyme 14 Chromosome Location 17
Enzyme 14 Locus 17q25
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed Link Image]
  2. Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed Link Image]
  3. Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5265
Enzyme 15 Name Histone acetyltransferase HTATIP
Enzyme 15 Synonyms
  1. 60 kDa Tat interactive protein
  2. Tip60
  3. HIV-1 Tat interactive protein
  4. cPLA(2-interacting protein
Enzyme 15 Gene Name HTATIP
Enzyme 15 Protein Sequence >Histone acetyltransferase HTATIP
MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTH
ERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPK
EREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAV
AAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRH
RLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTIS
FFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKE
STEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQ
TILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDI
VDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
Enzyme 15 Number of Residues 513
Enzyme 15 Molecular Weight 58583
Enzyme 15 Theoretical pI 8.64
Enzyme 15 GO Classification
Function
  • binding
  • chromatin binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin assembly or disassembly
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • chromatin
  • chromosome
  • intracellular membrane-bound organelle
  • intracellular non-membrane-bound organelle
  • membrane-bound organelle
  • non-membrane-bound organelle
  • nucleus
  • organelle
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. In case of HIV-1 infection, interaction with the viral Tat protein leads to HTATIP polyubiquitination and targets it to degradation
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 1657982 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q92993 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name TIP60_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1542 bp
ATGGCGGAGGTGGGGGAGATAATCGAGGGCTGCCGCCTACCCGTGCTGCGGCGGAACCAG
GACAACGAAGATGAGTGGCCCCTGGCCGAGATCCTGAGCGTGAAGGACATCAGTGGCCGG
AAGCTTTTCTACGTCCATTACATTGACTTCAACAAACGTCTGGATGAATGGGTGACGCAT
GAGCGGCTGGACCTAAAGAAGATCCAGTTCCCCAAGAAAGAGGCCAAGACCCCCACTAAG
AACGGACTTCCTGGGTCCCGTCCTGGCTCTCCAGAGAGAGAGGTGCCGGCCTCGGCGCAG
GCCAGCGGGAAGACCTTGCCAATCCCGGTCCAGATCACACTCCGCTTCAACCTGCCCAAG
GAGCGGGAGGCCATTCCCGGTGGCGAGCCTGACCAGCCGCTCTCCTCCAGCTCCTGCCTG
CAGCCCAACCACCGCTCAACGAAACGGAAGGTGGAGGTGGTTTCACCAGCAACTCCAGTG
CCCAGCGAGACAGCCCCGGCCTCGGTTTTTCCCCAGAATGGAGCCGCCCGTAGGGCAGTG
GCAGCCCAGCCAGGACGGAAGCGAAAATCGAATTGTTTGGGCACTGATGAGGACTCCCAG
GACAGCTCTGATGGAATACCGTCAGCACCACGCATGACTGGCAGCCTGGTGTCTGATCGA
AGCCACGACGACATCGTCACCCGGATGAAGAACATTGAGTGCATTGAGCTGGGCCGGCAC
CGCCTCAAGCCGTGGTACTTCTCCCCGTACCCACAGGAACTCACCACATTGCCTGTCCTC
TACCTGTGCGAGTTCTGCCTCAAGTACGGCCGTAGTCTCAAGTGTCTTCAGCGTCATTTG
ACCAAGTGTGACCTACGACATCCTCCAGGCAATGAGATTTACCGCAAGGGCACCATCTCC
TTCTTTGAGATTGATGGACGTAAGAACAAGAGTTATTCCCAGAACCTGTGTCTTTTGGCC
AAGTGTTTCCTTGACCATAAGACACTGTACTATGACACAGACCCTTTCCTCTTCTACGTC
ATGACAGAGTATGACTGTAAGGGCTTCCACATCGTGGGCTACTTCTCCAAGGAGAAAGAA
TCAACGGAAGACTACAATGTGGCCTGCATCCTAACCCTGCCTCCCTACCAGCGCCGGGGC
TACCGGAAGCTGCTGATCGAGTTCAGCTATGAACTCTCCAAAGTGGAAGGGAAAACAGGG
ACCCCTGAGAAGCCCCTCTCAGACCTTGGCCTCCTATCCTATCGAAGCTACTGGTCCCAG
ACCATCCTGGAGATCCTGATGGGGCTGAAGTCGGAGAGCGGGGAGAGGCCACAGATCACC
ATCAATGAGATTAGTGAAATCACCAGCATCAAGAAGGAGGATGTCATCTCCACTCTGCAG
TACCTCAATCTCATCAACTACTACAAGGGCCAGTACATCCTCACACTGTCAGAGGACATC
GTGGATGGCCATGAGCGGGCCATGCTCAAGCGGCTCCTGCGGATCGACTCCAAGTGTCTG
CACTTCACTCCCAAGGACTGGAGCAAGAGGGGGAAGTGGTGA
Enzyme 15 GenBank Gene ID U74667 Link Image
Enzyme 15 GeneCard ID HTATIP Link Image
Enzyme 15 GenAtlas ID HTATIP Link Image
Enzyme 15 HGNC ID HGNC:5275 Link Image
Enzyme 15 Chromosome Location 11
Enzyme 15 Locus 11q13
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G: Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology. 1996 Feb 15;216(2):357-66. [PubMed Link Image]
  2. Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed Link Image]
  3. Kimura A, Horikoshi M: Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells. 1998 Dec;3(12):789-800. [PubMed Link Image]
  4. Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, Scully R, Qin J, Nakatani Y: Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell. 2000 Aug 18;102(4):463-73. [PubMed Link Image]
  5. Lee HJ, Chun M, Kandror KV: Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling. J Biol Chem. 2001 May 18;276(20):16597-600. Epub 2001 Mar 21. [PubMed Link Image]
  6. Xiao H, Chung J, Kao HY, Yang YC: Tip60 is a co-repressor for STAT3. J Biol Chem. 2003 Mar 28;278(13):11197-204. Epub 2003 Jan 27. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5268
Enzyme 16 Name Nuclear receptor coactivator 1
Enzyme 16 Synonyms
  1. NCoA-1
  2. Steroid receptor coactivator 1
  3. SRC-1
  4. RIP160
  5. Protein Hin-2
  6. Renal carcinoma antigen NY-REN-52
Enzyme 16 Gene Name NCOA1
Enzyme 16 Protein Sequence >Nuclear receptor coactivator 1
MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSL
SVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEAL
DGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNG
VPWPQEATRRNSHTFNCRMLIHPPDEPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQ
SCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFF
QPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMG
IHIIDREHSGLSPQDDTNSGMSIPRVNPSVNPSISPAHGVARSSTLPPSNSNMVSTRINR
QQSSDLHSSSHSNSSNSQGSFGCSPGSQIVANVALNKGQASSQSSKPSLNLNNPPMEGTG
ISLAQFMSPRRQVTSGLATRPRMPNNSFPPNISTLSSPVGMTSSACNNNNRSYSNIPVTS
LQGMNEGPNNSVGFSASSPVLRQMSSQNSPSRLNIQPAKAESKDNKEIASTLNEMIQSDN
SSSDGKPLDSGLLHNNDRLSDGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSC
TGTSNSASANSSGGSCPSSHSSLTARHKILHRLLQEGSPSDITTLSVEPDKKDSASTSVS
VTGQVQGNSSIKLELDASKKKESKDHQLLRYLLDKDEKDLRSTPNLSLDDVKVKVEKKEQ
MDPCNTNPTPMTKPTPEEIKLEAQSQFTADLDQFDQLLPTLEKAAQLPGLCETDRMDGAV
TSVTIKSEILPASLQSATARPTSRLNRLPELELEAIDNQFGQPGTGDQIPWTNNTVTAIN
QSKSEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKL
VQGGGLDVLSERFPPQQATPPLIMEERPNLYSQPYSSPFPTANLPSPFQGMVRQKPSLGT
MPVQVTPPRGAFSPGMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLIHQNRQAILNQF
AATAPVGINMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQLIQQQRAMLMRQQSF
GNNLPPSSGLPVQTGNPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLAN
RNSMVSRGMTGNIGGQFGTGINPQMQQNVFQYPGAGMVPQGEANFAPSLSPGSSMVPMPI
PPPQSSLLQQTPPASGYQSPDMKAWQQGAIGNNNVFSQAVQNQPTPAQPGVYNNMSITVS
MAGGNTNVQNMNPMMAQMQMSSLQMPGMNTVCPEQINDPALRHTGLYCNQLSSTDLLKTE
ADGTQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLT
E
Enzyme 16 Number of Residues 1441
Enzyme 16 Molecular Weight 156742
Enzyme 16 Theoretical pI 6.33
Enzyme 16 GO Classification
Function
  • binding
  • protein binding
  • signal transducer activity
  • transcription coactivator activity
  • transcription cofactor activity
  • transcription factor binding
  • transcription regulator activity
Process
  • cell communication
  • cellular process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • signal transduction
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 1480646 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q15788 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name NCOA1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >4323 bp
ATGAGTGGCCTCGGGGACAGTTCATCCGACCCTGCTAACCCAGACTCACATAAGAGGAAA
GGATCGCCATGTGACACACTGGCATCAAGCACGGAAAAGAGGCGCAGGGAGCAAGAAAAT
AAATATTTAGAAGAACTAGCTGAGTTACTGTCTGCCAACATTAGTGACATTGACAGCTTG
AGTGTAAAACCAGACAAATGCAAGATTTTGAAGAAAACAGTCGATCAGATACAGCTAATG
AAGAGAATGGAACAAGAGAAATCAACAACTGATGACGATGTACAGAAATCAGACATCTCA
TCAAGTAGTCAAGGAGTGATAGAAAAGGAATCCTTGGGACCCCTTCTTTTGGAGGCTTTG
GATGGATTTTTCTTTGTTGTGAACTGTGAAGGGAGAATTGTATTTGTGTCAGAGAATGTA
ACCAGCTACTTAGGTTACAATCAGGAGGAATTAATGAATACCAGCGTCTACAGCATACTG
CACGTGGGGGATCATGCAGAATTTGTGAAGAATCTGCTACCAAAATCACTAGTAAATGGA
GTTCCTTGGCCTCAAGAGGCAACACGACGAAATAGCCATACCTTTAACTGCAGGATGCTA
ATTCACCCTCCAGATGAGCCAGGGACCGAGAACCAAGAAGCTTGCCAGCGTTATGAAGTA
ATGCAGTGTTTCACTGTGTCACAGCCAAAATCAATTCAAGAGGATGGAGAAGATTTCCAG
TCATGTCTGATTTGTATTGCACGGCGATTACCTCGGCCTCCAGCTATTACGGGTGTAGAA
TCCTTTATGACCAAGCAAGATACTACAGGTAAAATCATCTCTATTGATACTAGTTCCCTG
AGAGCTGCTGGCAGAACTGGTTGGGAAGATTTAGTGAGGAAGTGCATTTATGCTTTTTTC
CAACCTCAGGGCAGAGAACCATCTTATGCCAGACAGCTGTTCCAAGAAGTGATGACTCGT
GGCACTGCCTCCAGCCCCTCCTATAGATTCATATTGAATGATGGGACAATGCTTAGCGCC
CACACCAAGTGTAAACTTTGCTACCCTCAAAGTCCAGACATGCAACCTTTCATCATGGGA
ATTCATATCATCGACAGGGAGCACAGTGGGCTTTCTCCTCAAGATGACACTAATTCTGGA
ATGTCAATTCCCCGAGTAAATCCCTCGGTCAATCCTAGTATCTCTCCAGCTCATGGTGTG
GCTCGTTCATCCACATTGCCACCATCCAACAGCAACATGGTATCCACCAGAATAAACCGC
CAGCAGAGCTCAGACCTTCATAGCAGCAGTCATAGTAATTCTAGCAACAGCCAAGGAAGT
TTCGGATGCTCACCCGGAAGTCAGATTGTAGCCAATGTTGCCTTAAACCAAGGACAGGCC
AGTTCACAGAGCAGTAATCCCTCTTTAAACCTCAATAATTCTCCTATGGAAGGTACAGGA
ATATCCCTAGCACAGTTCATGTCTCCAAGGAGACAGGTTACTTCTGGATTGGCAACAAGG
CCCAGGATGCCAAACAATTCCTTTCCTCCTAATATTTCGACATTAAGCTCTCCCGTTGGC
ATGACAAGTAGTGCCTGTAATAATAATAACCGATCTTATTCAAACATCCCAGTAACATCT
TTACAGGGTATGAATGAAGGACCCAATAACTCCGTTGGCTTCTCTGCCAGTTCTCCAGTC
CTCAGGCAGATGAGCTCACAGAATTCACCTAGCAGATTAAATATACAACCAGCAAAAGCT
GAGTCCAAAGATAACAAAGAGATTGCCTCAATTTTAAATGAAATGATTCAATCTGACAAC
AGCTCTAGTGATGGCAAACCTCTGGATTCAGGGCTTCTGCATAACAATGACAGACTTTCA
GATGGAGACAGTAAATACTCTCAAACCAGTCACAAACTAGTGCAGCTTTTGACAACAACT
GCCGAACAGCAGTTACGGCATGCTGATATAGACACAAGCTGCAAAGATGTCCTGTCTTGC
ACAGGCACTTCCAACTCTGCCTCTGCTAACTCTTCAGGAGGTTCTTGTCCCTCTTCTCAT
AGCTCATTGACAGAACGGCATAAAATTCTACACCGGCTCTTACAGGAGGGTAGCCCCTCA
GATATCACCACTTTGTCTGTCGAGCCTGATAAAAAGGACAGTGCATCTACTTCTGTGTCA
GTGACTGGACAGGTACAAGGAAACTCCAGTATAAAACTAGAACTGGATGCTTCAAAGAAA
AAAGAATCAAAAGACCATCAGCTCCTACGCTATCTTTTAGATAAAGATGAGAAAGATTTA
AGATCAACTCCAAACCTGAGCCTGGATGATGTAAAGGTGAAAGTGGAAAAGAAAGAACAG
ATGGATCCATGTAATACAAACCCAACCCCAATGACCAAACCCACTCCTGAGGAAATAAAA
CTGGAGGCCCAGAGCCAGTTTACAGCTGACCTTGACCAGTTTGATCAGTTACTGCCCACG
CTGGAGAAGGCAGCACAGTTGCCAGGCTTATGTGAGACAGACAGGATGGATGGTGCGGTC
ACCAGTGTAACCATCAAATCGGAGATCCTGCCAGCTTCACTTCAGTCCGCCACTGCCAGA
CCCACTTCCAGGCTAAATAGATTACCTGAGCTGGAATTGGAAGCAATTGATAACCAATTT
GGACAACCAGGAACAGGCGATCAGATTCCATGGACAAATAATACAGTGACAGCTATAAAT
CAGAGTAAATCAGAAGACCAGTGTATTAGCTCACAATTAGATGAGCTTCTCTGTCCACCC
ACAACAGTAGAAGGGAGAAATGATGAGAAGGCTCTTCTTGAACAGCTGGTATCCTTCCTT
AGTGGCAAAGATGAAACTGAGCTAGCTGAACTAGACAGAGCTCTGGGAATTGACAAACTT
GTTCAGGGGGGTGGATTAGATGTATTATCAGAGAGATTTCCACCACAACAAGCAACGCCA
CCTTTGATCATGGAAGAAAGACCCAACCTTTATTCCCAGCCTTACTCTTCTCCTTCTCCT
ACTGCCAATCTCCCTAGCCCTTTCCAAGGCATGGTCAGGCAAAAACCTTCACTGGGGACG
ATGCCTGTTCAAGTAACACCTCCCCGAGGTGCTTTTTCACCTGGCATGGGCATGCAGCCC
AGGCAAACTCTAAACAGACCTCCGGCTGCACCTAACCAGCTTCGACTTCAACTACAGCAG
CGATTACAGGGACAACAGCAGTTGATACACCAAAATCGGCAAGCTATCTTAAACCAGTTT
GCAGCAACTGCTCCTGTTGGCATCAATATGAGATCAGGCATGCAACAGCAAATTACACCT
CAGCCACCCCTGAATGCTCAAATGTTGGCACAACGTCAGCGGGAACTGTACAGTCAACAG
CACCGACAGAGGCAGCTAATACAGCAGCAAAGAGCCATGCTTATGAGGCAGCAAAGCTTT
GGGAACAACCTCCCTCCCTCATCTGGACTACCAGTTCAAATGGGGAACCCCCGTCTTCCT
CAGGGTGCTCCACAGCAATTCCCCTATCCACCAAACTATGGTACAAATCCAGGAACCCCA
CCTGCTTCTACCAGCCCGTTTTCACAACTAGCAGCAAATCCTGAAGCATCCTTGGCCAAC
CGCAACAGCATGGTGAGCAGAGGCATGACAGGAAACATAGGAGGACAGTTTGGCACTGGA
ATCAATCCTCAGATGCAGCAGAATGTCTTCCAGTATCCAGGAGCAGGAATGGTTCCCCAA
GGTGAGGCCAACTTTGCTCCATCTCTAAGCCCTGGGAGCTCCATGGTGCCGATGCCAATC
CCTCCTCCTCAGAGTTCTCTGCTCCAGCAAACTCCACCTGCCTCCGGGTATCAGTCACCA
GACATGAAGGCCTGGCAGCAAGGAGCGATAGGAAACAACAATGTGTTCAGTCAAGCTGTC
CAGAACCAGCCCACGCCTGCACAGCCAGGAGTATACAACAACATGAGCATCACCGTTTCC
ATGGCAGGTGGAAATACGAATGTTCAGAACATGAACCCAATGATGGCCCAGATGCAGATG
AGCTCTTTGCAGATGCCAGGAATGAACACTGTGTGCCCTGAGCAGATAAATGATCCCGCA
CTGAGACACACAGGCCTCTACTGCAACCAGCTCTCATCCACTGACCTTCTCAAAACAGAA
GCAGATGGAACCCAGGTGCAACAGGTTCAGGTGTTTGCTGACGTCCAGTGTACAGTGAAT
CTGGTAGGCGGGGACCCTTACCTGAACCAGCCTGGTCCACTGGGAACTCAAAAGCCCACG
TCAGGACCACAGACCCCCCAGGCCCAGCAGAAGAGCCTCCTTCAGCAGCTACTGACTGAA
TAA
Enzyme 16 GenBank Gene ID U59302 Link Image
Enzyme 16 GeneCard ID NCOA1 Link Image
Enzyme 16 GenAtlas ID NCOA1 Link Image
Enzyme 16 HGNC ID HGNC:7668 Link Image
Enzyme 16 Chromosome Location 2
Enzyme 16 Locus 2p23
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Takeshita A, Yen PM, Misiti S, Cardona GR, Liu Y, Chin WW: Molecular cloning and properties of a full-length putative thyroid hormone receptor coactivator. Endocrinology. 1996 Aug;137(8):3594-7. [PubMed Link Image]
  2. Kalkhoven E, Valentine JE, Heery DM, Parker MG: Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 1998 Jan 2;17(1):232-43. [PubMed Link Image]
  3. Onate SA, Tsai SY, Tsai MJ, O'Malley BW: Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science. 1995 Nov 24;270(5240):1354-7. [PubMed Link Image]
  4. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  5. Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed Link Image]
  6. Carrero P, Okamoto K, Coumailleau P, O'Brien S, Tanaka H, Poellinger L: Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol Cell Biol. 2000 Jan;20(1):402-15. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5269
Enzyme 17 Name Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
Enzyme 17 Synonyms
  1. HMG-CoA synthase
  2. 3-hydroxy-3-methylglutaryl coenzyme A synthase
Enzyme 17 Gene Name HMGCS2
Enzyme 17 Protein Sequence >Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALE
VYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLP
WDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWM
ESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYD
FYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIF
HTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKAS
QDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASF
FSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPG
DTNSLFPGTWYLERVDEQHRRKYARRPV
Enzyme 17 Number of Residues 508
Enzyme 17 Molecular Weight 56636
Enzyme 17 Theoretical pI 8.28
Enzyme 17 GO Classification
Function
  • catalytic activity
  • hydroxymethylglutaryl-CoA synthase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • acetyl-CoA metabolism
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
Enzyme 17 General Function Lipid transport and metabolism
Enzyme 17 Specific Function This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase
Enzyme 17 Pathways
  • Butyrate Metabolism (map00650 Link Image)
  • Synthesis and Degradation of Ketone Bodies (map00072 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 17 Reactions
  • acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-17
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 619877 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P54868 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name HMCS2_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1527 bp
ATGCAGCGTCTGTTGACTCCAGTGAAGCGCATTCTGCAACTGACAAGAGCGGTGCAGGAA
ACCTCCCTCACACCTGCTCGCCTGCTCCCAGTAGCCCACCAAAGGTTTTCTACAGCCTCT
GCTGTCCCCCTGGCCAAAACAGATACTTGGCCAAAGGACGTGGGCATCCTGGCCCTGGAG
GTCTACTTCCCAGCCCAATATGTGGACCAAACTGACCTGGAGAAGTATAACAATGTGGAA
GCAGGAAAGTATACAGTGGGCTTGGGCCAGACCCGTATGGGCTTCTGCTCAGTCCAAGAG
GACATCAACTCCCTGTGCCTGACGGTGGTGCAACGGCTGATGGAGCGCATACAGCTCCCA
TGGGACTCTGTGGGCAGGCTGGAAGTAGGCACTGAGACCATCATTGACAAGTCCAAAGCT
GTCAAAACAGTGCTCATGGAACTCTTCCAGGATTCAGGCAATACTGATATTGAGGGCATA
GATACCACCAATGCCTGCTACGGTGGTACTGCCTCCCTCTTCAATGCTGCCAACTGGATG
GAGTCCAGTTCCTGGGATGGTCGTTATGCCATGGTGGTCTGTGGAGACATTGCCGTCTAT
CCCAGTGGTAATGCTCGTCCCACAGGTGGGGCCGGAGCTGTGGCTATGCTGATTGGCCCA
AAGGCCCCTCTGGCCCTGGAGCGAGGGCTGAGGGGAACCCATATGGAGAATGTGTATGAC
TTCTACAAACCAAATTTGGCCTCGGAGTACCCAATAGTGGATGGGAAGCTTTCCATCCAG
TGCTACTTGCGGGCCTTGGATCGATGTTACACATCATACCGTAAAAAAATCCAGAATCAG
TGGAAGCAAGCTGGCAGCGATCGACCCTTCACCCTTGACGATTTACAGTATATGATCTTT
CATACACCCTTTTGCAAGATGGTCCAGAAGTCTCTGGCTCGCCTGATGTTCAATGACTTC
CTGTCAGCCAGCAGTGACACACAAACCAGCTTATATAAGGGGCTGGAGGCTTTCGGGGGG
CTAAAGCTGGAAGACACCTACACCAACAAGGACCTGGATAAAGCACTTCTAAAGGCCTCT
CAGGACATGTTCGACAAGAAAACCAAGGCTTCCCTTTACCTCTCCACTCACAATGGGAAC
ATGTACACCTCATCCCTGTACGGGTGCCTGGCCTCGCTTCTGTCCCACCACTCTGCCCAA
GAACTGGCTGGCTCCAGGATTGGTGCCTTCTCTTATGGCTCTGGTTTAGCAGCAAGTTTC
TTTTCATTTCGAGTATCCCAGGATGCTGCTCCAGGCTCTCCCCTGGACAAGTTGGTGTCC
AGCACATCAGACCTGCCAAAACGCCTAGCCTCCCGAAAGTGTGTGTCTCCTGAGGAGTTC
ACAGAAATAATGAACCAAAGAGAGCAATTCTACCATAAGGTGAATTTCTCCCCACCTGGT
GACACAAACAGCCTTTTCCCAGGTACTTGGTACCTGGAGCGAGTGGACGAGCAGCATCGC
CGAAAGTATGCCCGGCGTCCCGTCTAA
Enzyme 17 GenBank Gene ID X83618 Link Image
Enzyme 17 GeneCard ID HMGCS2 Link Image
Enzyme 17 GenAtlas ID HMGCS2 Link Image
Enzyme 17 HGNC ID HGNC:5008 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 1p13-p12
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Mascaro C, Buesa C, Ortiz JA, Haro D, Hegardt FG: Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase. Arch Biochem Biophys. 1995 Mar 10;317(2):385-90. [PubMed Link Image]
  2. Boukaftane Y, Mitchell GA: Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene. Gene. 1997 Aug 22;195(2):121-6. [PubMed Link Image]
  3. Boukaftane Y, Duncan A, Wang S, Labuda D, Robert MF, Sarrazin J, Schappert K, Mitchell GA: Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution. Genomics. 1994 Oct;23(3):552-9. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5271
Enzyme 18 Name Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
Enzyme 18 Synonyms
  1. Acetate--CoA ligase 2
  2. Acetyl-CoA synthetase 2
  3. Acyl- CoA synthetase short-chain family member 1
Enzyme 18 Gene Name ACSS1
Enzyme 18 Protein Sequence >Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK
Enzyme 18 Number of Residues 689
Enzyme 18 Molecular Weight 74857
Enzyme 18 Theoretical pI 7.11
Enzyme 18 GO Classification
Function
  • AMP binding
  • CoA-ligase activity
  • acetate-CoA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-sulfur bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • metabolism
  • physiological process
Component
Enzyme 18 General Function Lipid transport and metabolism
Enzyme 18 Specific Function Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2)
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-22
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 56203089 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9NUB1 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name ACS2L_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1439 bp
CCAAGTGCAAGGTGGTTATCACCTTCAACCAAGGACTCCGGGGTGGGCGCGTGGTGGAGC
TGAAGAAAATAGTGGATGAGGCTGTGAAGCACTGCCCCACCGTGCAGCATGTCCTGGTGG
CTCACAGGACAGACAACAAGGTCCACATGGGGGATCTGGACGTCCCGCTGGAGCAGGAAA
TGGCCAAGGAGGACCCTGTTTGCGCCCCAGAGAGCATGGGCAGTGAGGACATGCTCTTCA
TGCTGTACACCTCAGGGAGCACCGGAATGCCCAAGGGCATCGTCCATACCCAGGCAGGCT
ACCTGCTCTATGCCGCCCTGACTCACAAGCTTGTGTTTGACCACCAGCCAGGTGACATCT
TTGGCTGTGTGGCCGACATCGGTTGGATTACAGGACACAGCTACGTGGTGTATGGGCCTC
TCTGCAATGGTGCCACCAGCGTCCTTTTTGAGAGCACCCCAGTTTATCCCAATGCTGGTC
GGTACTGGGAGACAGTAGAGAGGTTGAAGATCAATCAGTTCTATGGCGCCCCAACGGCTG
TCCGGCTGTTGCTGAAATACGGTGATGCCTGGGTGAAGAAGTATGATCGCTCCTCCCTGC
GGACCCTGGGGTCAGTGGGAGAGCCCATCAACTGTGAGGCCTGGGAGTGGCTTCACAGGG
TGGTGGGGGACAGCAGGTGCACGCTGGTGGACACCTGGTGGCAGACAGAAACAGGTGGCA
TCTGCATCGCACCACGGCCCTCGGAAGAAGGGGCGGAAATCCTCCCTGCCATGGCGATGA
GGCCCTTCTTTGGCATCGTCCCCGTCCTCATGGATGAGAAGGGCAGCGTCGTGGAGGGCA
GCAACGTCTCCGGGGCCCTGTGCATCTCCCAGGCCTGGCCGGGCATGGCCAGGACCATCT
ATGGCGACCACCAGCGATTTGTGGACGCCTACTTCAAGGCCTACCCAGGCTATTACTTCA
CTGGAGACGGGGCTTACCGAACTGAGGGCGGCTATTACCAGATCACAGGGCGGATGGATG
ATGTCATCAACATCAGTGGCCACCGGCTGGGGACCGCAGAGATTGAGGACGCCATCGCCG
ACCACCCTGCAGTACCAGAAAGTGCTGTCATTGGCTACCCCCACGACATCAAAGGAGAAG
CTGCCTTTGCCTTCATTGTGGTGAAAGATAGTGCGGGTGACTCAGATGTGGTGGTGCAGG
AGCTCAAGTCCATGGTGGCCACCAAGATCGCCAAATATGCTGTGCCTGATGAGATCCTGG
TGGTGAAACGTCTTCCAAAAACCAGGTCTGGGAAGGTCATGCGGCGGCTCCTGAGGAAGA
TCATCACTAGTGAGGCCCAGGAGCTGGGAGACACTACCACCTTGGAGGACCCCAGCATCA
TCGCAGAGATCCTGAGTGTCTACCAGAAGTGCAAGGACAAGCAGGCTGCTGCTAAGTGA
Enzyme 18 GenBank Gene ID AL035661 Link Image
Enzyme 18 GeneCard ID ACSS1 Link Image
Enzyme 18 GenAtlas ID ACSS1 Link Image
Enzyme 18 HGNC ID HGNC:16091 Link Image
Enzyme 18 Chromosome Location 20
Enzyme 18 Locus 20p11.23-p11.21
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5272
Enzyme 19 Name Citrate synthase, mitochondrial precursor
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name CS
Enzyme 19 Protein Sequence >Citrate synthase, mitochondrial precursor
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVV
GQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLF
WLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESN
FARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNF
TNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPL
HGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQ
REFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYY
TVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
Enzyme 19 Number of Residues 466
Enzyme 19 Molecular Weight 51713
Enzyme 19 Theoretical pI 8.53
Enzyme 19 GO Classification
Function
  • catalytic activity
  • citrate (Si)-synthase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
  • tricarboxylic acid cycle
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 19 General Function Energy production and conversion
Enzyme 19 Specific Function Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Enzyme 19 Pathways
Enzyme 19 Reactions
  • acetyl-CoA + H2O + oxaloacetate = citrate + CoA
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-16
Enzyme 19 Transmembrane Regions Not Available
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 3288815 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O75390 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name CISY_HUMAN Link Image
Enzyme 19 PDB ID 4CTS Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1401 bp
ATGGCTTTACTTACTGCGGCCGCCCGGCTCTTGGGAACCAAGAATGCATCTTGTCTTGTT
CTTGCAGCCCGGCATGCTAGTGCTTCCTCCACGAATTTGAAAGACATATTGGCTGACCTG
ATACCTAAGGAGCAGGCCAGAATTAAGACTTTCAGGCAGCAACATGGCAAGACGGTGGTG
GGCCAAATCACTGTGGACATGATGTATGGTGGCATGAGAGGCATGAAGGGATTGGTGTAT
GAAACATCAGTTCTTGATCCTGATGAGGGCATCCGTTTCCGAGGCTTTAGTATCCCTGAA
TGCCAGAAACTGCTACCCAAGGCTAAGGGTGGGGAAGAACCCCTGCCTGAGGGCTTATTT
TGGCTGCTGGTAACTGGATGTATCCCAACAGAGGAACAGGTATCTTGGCTCTCAAAAGAG
TGGGCAAAGAGGGCAGCTCTGCCTTCCCATGTGGTCACCATGCTGGACAACTTTCCCACC
AATCTACACCCCATGTCTCAGCTGAGTGCAGCTGTTACAGCCCTCAACAGTGAAAGTAAC
TTTGCCCAAGCATATGCACGGGGTATCAGCCGAACCAAGTACTGGGAGTTGATTTATGAA
GATTCTGTGGATCTAATAGCAAAGCTACCTTGTGTTGCAGCAAAGATCTACCGAAATCTC
TACTGGGAAGGCAGCGGTATTGGGGCCATTGACTCTAACCTGGACTGGTCTCACAATTTC
ACCAACATGTTAGGCTATACTGATCATCAGTTCACTGAGCTCATGCGCCTGTACCTCACC
ATCCACAGTGACCATGAGGGTGGCAATGTAAGTGCCCATACCAGCCACTTGGTGGGCAGT
GCCCTTTCCGACCCTTACCTGTCCTTTGCAGCAGCCATGAACGGGCTGGCAGGGCCTCTC
CATGGACTGGCAAATCAGGAAGTGCTTGTCTGGCTAACACAGCTGCAGAAGGAAGTTGGC
AAAGATGTGTCAGATGAGAAGTTACGAGACTACATCTGGAACACACTCAACTCAGGACGG
GTTGTTCCAGGCTATGGCCATGCAGTACTAAGGAAGACTGATCCGCGATATACCTGTCAG
CGAGAGTTTGCTCTGAAACACCTGCCTAATGACCCCATGTTTAAGTTGGTTGCTCAGCTG
TACAAGATTGTGCCCAATGTCCTCTTAGAGCAGGGTAAAGCCAAGAATCCTTGGCCCAAT
GTAGATGCTCACAGTGGGGTGCTGCTCCAGTATTATGGCATGACGGAGATGAATTACTAC
ACGGTCCTGTTTGGGGTGTCACGAGCATTGGGTGTACTGGCACAGCTCATCTGGAGCCGA
GCCTTAGGCTTCCCTCTAGAAAGGCCCAAGTCCATGAGCACAGAGGGTCTGATGAAGTTT
GTGGACTCTAAGTCAGGGTAA
Enzyme 19 GenBank Gene ID AF047042 Link Image
Enzyme 19 GeneCard ID CS Link Image
Enzyme 19 GenAtlas ID CS Link Image
Enzyme 19 HGNC ID HGNC:2422 Link Image
Enzyme 19 Chromosome Location 12
Enzyme 19 Locus 12q13.2-q13.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Goldenthal MJ, Marin-Garcia J, Ananthakrishnan R: Cloning and molecular analysis of the human citrate synthase gene. Genome. 1998 Oct;41(5):733-8. [PubMed Link Image]
  2. Liu Q, Yu L, Han XF, Fu Q, Zhang JX, Tang H, Zhao SY: [Cloning and tissue expression pattern analysis of the human citrate synthase cDNA] Shi Yan Sheng Wu Xue Bao. 2000 Sep;33(3):207-14. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5273
Enzyme 20 Name Testis-specific chromodomain protein Y 2
Enzyme 20 Synonyms Not Available
Enzyme 20 Gene Name CDY2A
Enzyme 20 Protein Sequence >Testis-specific chromodomain protein Y 2
MASQEFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQTE
KQKKLTWTTTSRIFSNNARRRTSRSTKANYSKNSPKTPVTDKHHRSKNCKLFAASKNVRR
KAASTLSDTKNMEIINSTIETLAPDSPFDHKKTVSGFQKLEKLDPIAADQQDTVVFKVTE
GKLLRDPLSHPGAEQTGIQNKTQMHPLMSQMSGSVTASMATGSATRKGIVVLIDPLAANG
TTDMHTSVPRVKGGQRNITDDSRGQPFIKKMHFTIRLTESAITYRDIVVKKEDGFTQIVL
STRSTEKNALNTEVIKEMVNALNSAAADDSKLVLFSAAGSVFCCGLDFGYFVRHLRNDRN
TASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTT
FGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQI
KELASYNAIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESMLKYVENKIDE
F
Enzyme 20 Number of Residues 541
Enzyme 20 Molecular Weight 60525
Enzyme 20 Theoretical pI 9.42
Enzyme 20 GO Classification
Function
  • binding
  • chromatin binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin assembly or disassembly
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • chromatin
  • chromosome
  • intracellular membrane-bound organelle
  • intracellular non-membrane-bound organelle
  • membrane-bound organelle
  • non-membrane-bound organelle
  • nucleus
  • organelle
Enzyme 20 General Function Lipid transport and metabolism
Enzyme 20 Specific Function Not Available
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 4558754 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9Y6F7 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name CDY2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1626 bp
ATGGCTTCCCAGGAGTTTGAGGTTGAAGCTATTGTTGACAAAAGACAGGATAAAAATGGG
AATACACAGTATTTGGTTCGGTGGAAAGGTTATGACAAACAGGATGACACTTGGGAACCA
GAGCAGCACCTCATGAACTGTGAAAAATGTGTACATGATTTTAATAGACGACAGACTGAA
AAACAGAAAAAACTGACATGGACTACAACCAGTAGAATTTTTTCAAACAATGCCAGAAGA
AGAACTTCCAGATCTACAAAAGCAAACTATTCTAAGAACTCTCCTAAAACTCCAGTGACT
GATAAACACCACAGGTCCAAAAACTGCAAGTTATTTGCTGCCAGCAAGAACGTTAGGAGA
AAGGCAGCTTCAACTCTCTCCGACACAAAGAATATGGAGATAATAAATTCAACTATTGAG
ACCCTTGCACCTGACAGCCCCTTTGACCACAAGAAAACTGTGAGTGGCTTTCAGAAACTT
GAGAAACTGGACCCTATTGCAGCAGATCAGCAGGACACGGTGGTCTTCAAGGTGACAGAA
GGGAAACTCCTCCGGGACCCTTTGTCACATCCTGGTGCAGAACAGACTGGAATACAGAAC
AAGACTCAGATGCACCCACTAATGTCGCAGATGTCTGGCTCAGTTACTGCTTCTATGGCC
ACAGGTTCAGCTACCCGAAAGGGTATAGTGGTATTAATAGACCCATTAGCAGCCAATGGG
ACAACAGACATGCATACCTCAGTTCCAAGAGTGAAAGGTGGGCAAAGAAATATTACTGAT
GACAGCAGAGGCCAGCCTTTTATCAAGAAGATGCACTTCACCATAAGGCTAACAGAAAGT
GCCATCACATACAGAGACATTGTAGTGAAGAAAGAGGATGGATTCACCCAGATAGTGCTA
TCAACTAGATCGACAGAAAAAAATGCACTGAATACAGAAGTAATTAAAGAAATGGTTAAT
GCTCTGAATAGCGCTGCTGCAGATGACAGCAAGCTCGTGCTGTTCAGTGCAGCTGGAAGT
GTCTTTTGCTGCGGTCTTGATTTTGGGTACTTTGTGAGGCACTTAAGGAATGACAGAAAC
ACAGCAAGCCTTGAAATGGTGGACACCATCAAGAACTTTGTGAATACTTTTATTCAATTT
AAAAAGCCTATTGTTGTATCAGTCAATGGCCCTGCCATTGGACTAGGTGCATCCATCCTG
CCTCTTTGTGATCTCGTGTGGGCTAATGAAAAGGCTTGGTTCCAAACCCCTTATACGACC
TTTGGACAGAGTCCAGATGGCTGTTCTTCTATTACATTCCCCAAAATGATGGGTAAAGCA
TCTGCCAATGAAATGTTAATTGCTGGGCGAAAGCTGACAGCACGGGAGGCATGCGCCAAA
GGCCTGGTCTCTCAGGTATTTTTGACTGGAACTTTCACCCAAGAGGTTATGATTCAAATT
AAGGAGCTTGCCTCATACAATGCAATTGTACTGGAAGAATGTAAGGCCCTCGTTCGCTGT
AATATTAAGTTGGAGTTGGAACAGGCCAATGAGAGAGAGTGTGAGGTGCTGAGGAAGATC
TGGAGCTCAGCCCAAGGGATAGAATCCATGTTAAAGTATGTTGAAAATAAAATTGATGAG
TTTTAA
Enzyme 20 GenBank Gene ID AF080598 Link Image
Enzyme 20 GeneCard ID CDY2A Link Image
Enzyme 20 GenAtlas ID CDY2A Link Image
Enzyme 20 HGNC ID HGNC:1810 Link Image
Enzyme 20 Chromosome Location Y
Enzyme 20 Locus Yq11.221
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Lahn BT, Page DC: Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome. Nat Genet. 1999 Apr;21(4):429-33. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5275
Enzyme 21 Name Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
Enzyme 21 Synonyms
  1. PDHE1-A type I
Enzyme 21 Gene Name PDHA1
Enzyme 21 Protein Sequence >Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTRED
GLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRA
HGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALA
CKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAAST
DYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVS
YRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPP
LEELGYHIYSSDPPFEVRGANQWIKFKSVS
Enzyme 21 Number of Residues 390
Enzyme 21 Molecular Weight 43296
Enzyme 21 Theoretical pI 8.14
Enzyme 21 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
  • metabolism
  • physiological process
Component
Enzyme 21 General Function Energy production and conversion
Enzyme 21 Specific Function The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 21 Pathways
Enzyme 21 Reactions
  • pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-16
Enzyme 21 Transmembrane Regions Not Available
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 387009 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P08559 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name ODPA_HUMAN Link Image
Enzyme 21 PDB ID 1NI4 Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1173 bp
ATGAGGAAGATGCTCGCCGCCGTCTCCCGCGTGCTGTCTGGCGCTTCTCAGAAGCCGGCA
AGCAGAGTGCTGGTAGCATCCCGTAATTTTGCAAATGATGCTACATTTGAAATTAAGAAA
TGTGACCTTCACCGGCTGGAAGAAGGCCCTCCTGTCACAACAGTGCTCACCAGGGAGGAT
GGGCTCAAATACTACAGGATGATGCAGACTGTACGCCGAATGGAGTTGAAAGCAGATCAG
CTGTATAAACAGAAAATTATTCGTGGTTTCTGTCACTTGTGTGATGGTCAGGAAGCTTGC
TGTGTGGGCCTGGAGGCCGGCATCAACCCCACAGACCATCTCATCACAGCCTACCGGGCT
CACGGCTTTACTTTCACCCGGGGCCTTTCCGTCCGAGAAATTCTCGCAGAGCTTACAGGA
CGAAAAGGAGGTTGTGCTAAAGGGAAAGGAGGATCGATGCACATGTATGCCAAGAACTTC
TACGGGGGCAATGGCATCGTGGGAGCGCAGGTGCCCCTGGGCGCTGGGATTGCTCTAGCC
TGTAAGTATAATGGAAAAGATGAGGTCTGCCTGACTTTATATGGCGATGGTGCTGCTAAC
CAGGGCCAGATATTCGAAGCTTACAACATGGCAGCTTTGTGGAAATTACCTTGTATTTTC
ATCTGTGAGAATAATCGCTATGGAATGGGAACGTCTGTTGAGAGAGCGGCAGCCAGCACT
GATTACTACAAGAGAGGCGATTTCATTCCTGGGCTGAGAGTGGATGGAATGGATATCCTG
TGCGTCCGAGAGGCAACAAGGTTTGCTGCTGCCTATTGTAGATCTGGGAAGGGGCCCATC
CTGATGGAGCTGCAGACTTACCGTTACCACGGACACAGTATGAGTGACCCTGGAGTCAGT
TACCGTACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGTGACCCTATTATGCTTCTC
AAGGACAGGATGGTGAACAGCAATCTTGCCAGTGTGGAAGAACTAAAGGAAATTGATGTG
GAAGTGAGGAAGGAGATTGAGGATGCTGCCCAGTTTGCCACGGCCGATCCTGAGCCACCT
TTGGAAGAGCTGGGCTACCACATCTACTCCAGCGACCCACCTTTTGAAGTTCGTGGTGCC
AATCAGTGGATCAAGTTTAAGTCAGTCAGTTAA
Enzyme 21 GenBank Gene ID M27257 Link Image
Enzyme 21 GeneCard ID PDHA1 Link Image
Enzyme 21 GenAtlas ID PDHA1 Link Image
Enzyme 21 HGNC ID HGNC:8806 Link Image
Enzyme 21 Chromosome Location X
Enzyme 21 Locus Xp22.2-p22.1
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Koike K, Urata Y, Matsuo S, Koike M: Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit. Gene. 1990 Sep 14;93(2):307-11. [PubMed Link Image]
  2. Ho L, Wexler ID, Liu TC, Thekkumkara TJ, Patel MS: Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5330-4. [PubMed Link Image]
  3. Dahl HH, Hunt SM, Hutchison WM, Brown GK: The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA. J Biol Chem. 1987 May 25;262(15):7398-403. [PubMed Link Image]
  4. Maragos C, Hutchison WM, Hayasaka K, Brown GK, Dahl HH: Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex. J Biol Chem. 1989 Jul 25;264(21):12294-8. [PubMed Link Image]
  5. De Meirleir L, MacKay N, Lam Hon Wah AM, Robinson BH: Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex. J Biol Chem. 1988 Feb 5;263(4):1991-5. [PubMed Link Image]
  6. Koike K, Ohta S, Urata Y, Kagawa Y, Koike M: Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):41-5. [PubMed Link Image]
  7. Harris EE, Hey J: X chromosome evidence for ancient human histories. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3320-4. [PubMed Link Image]
  8. Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS: Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. [PubMed Link Image]
  9. Dahl HH, Brown GK, Brown RM, Hansen LL, Kerr DS, Wexler ID, Patel MS, De Meirleir L, Lissens W, Chun K, et al.: Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene. Hum Mutat. 1992;1(2):97-102. [PubMed Link Image]
  10. Hansen LL, Brown GK, Kirby DM, Dahl HH: Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency. J Inherit Metab Dis. 1991;14(2):140-51. [PubMed Link Image]
  11. De Meirleir L, Lissens W, Vamos E, Liebaers I: Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit. Hum Genet. 1992 Mar;88(6):649-52. [PubMed Link Image]
  12. Dahl HH, Hansen LL, Brown RM, Danks DM, Rogers JG, Brown GK: X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation. J Inherit Metab Dis. 1992;15(6):835-47. [PubMed Link Image]
  13. Matthews PM, Marchington DR, Squier M, Land J, Brown RM, Brown GK: Molecular genetic characterization of an X-linked form of Leigh's syndrome. Ann Neurol. 1993 Jun;33(6):652-5. [PubMed Link Image]
  14. Chun K, MacKay N, Petrova-Benedict R, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex. Hum Mol Genet. 1993 Apr;2(4):449-54. [PubMed Link Image]
  15. Matthews PM, Brown RM, Otero LJ, Marchington DR, LeGris M, Howes R, Meadows LS, Shevell M, Scriver CR, Brown GK: Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients. Brain. 1994 Jun;117 ( Pt 3):435-43. [PubMed Link Image]
  16. Hansen LL, Horn N, Dahl HH, Kruse TA: Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit. Hum Mol Genet. 1994 Jun;3(6):1021-2. [PubMed Link Image]
  17. Dahl HH, Brown GK: Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit. Hum Mutat. 1994;3(2):152-5. [PubMed Link Image]
  18. Awata H, Endo F, Tanoue A, Kitano A, Matsuda I: Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia. J Inherit Metab Dis. 1994;17(2):189-95. [PubMed Link Image]
  19. Chun K, MacKay N, Petrova-Benedict R, Federico A, Fois A, Cole DE, Robertson E, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex. Am J Hum Genet. 1995 Mar;56(3):558-69. [PubMed Link Image]
  20. Takakubo F, Cartwright P, Hoogenraad N, Thorburn DR, Collins F, Lithgow T, Dahl HH: An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein. Am J Hum Genet. 1995 Oct;57(4):772-80. [PubMed Link Image]
  21. Hemalatha SG, Kerr DS, Wexler ID, Lusk MM, Kaung M, Du Y, Kolli M, Schelper RL, Patel MS: Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit. Hum Mol Genet. 1995 Feb;4(2):315-8. [PubMed Link Image]
  22. Lissens W, De Meirleir L, Seneca S, Benelli C, Marsac C, Poll-The BT, Briones P, Ruitenbeek W, van Diggelen O, Chaigne D, Ramaekers V, Liebaers I: Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency. Hum Mutat. 1996;7(1):46-51. [PubMed Link Image]
  23. Tripatara A, Kerr DS, Lusk MM, Kolli M, Tan J, Patel MS: Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS). Hum Mutat. 1996;8(2):180-2. [PubMed Link Image]
  24. Otero LJ, Brown RM, Brown GK: Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity. Hum Mutat. 1998;12(2):114-21. [PubMed Link Image]
  25. Ito M, Huq AH, Naito E, Saijo T, Takeda E, Kuroda Y: Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein. J Inherit Metab Dis. 1992;15(6):848-56. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5277
Enzyme 22 Name Trifunctional enzyme subunit beta, mitochondrial precursor
Enzyme 22 Synonyms
  1. TP-beta[Includes: 3-ketoacyl-CoA thiolase
  2. Acetyl-CoA acyltransferase
  3. Beta-ketothiolase]
Enzyme 22 Gene Name HADHB
Enzyme 22 Protein Sequence >Trifunctional enzyme subunit beta, mitochondrial precursor
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
Enzyme 22 Number of Residues 474
Enzyme 22 Molecular Weight 51295
Enzyme 22 Theoretical pI 9.94
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Lipid transport and metabolism
Enzyme 22 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 22 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 22 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 862458 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P55084 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name ECHB_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1425 bp
ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA
Enzyme 22 GenBank Gene ID D16481 Link Image
Enzyme 22 GeneCard ID HADHB Link Image
Enzyme 22 GenAtlas ID HADHB Link Image
Enzyme 22 HGNC ID HGNC:4803 Link Image
Enzyme 22 Chromosome Location 2
Enzyme 22 Locus 2p23
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed Link Image]
  2. Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5278
Enzyme 23 Name 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial precursor
Enzyme 23 Synonyms
  1. AKB ligase
  2. Glycine acetyltransferase
  3. Aminoacetone synthetase
Enzyme 23 Gene Name GCAT
Enzyme 23 Protein Sequence >2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial precursor
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRV
DGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIA
RFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLD
MADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLG
PTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPP
AVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLAS
RMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
Enzyme 23 Number of Residues 419
Enzyme 23 Molecular Weight 45286
Enzyme 23 Theoretical pI 8.11
Enzyme 23 GO Classification
Function
  • C-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycine C-acetyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 23 General Function Coenzyme transport and metabolism
Enzyme 23 Specific Function Acetyl-CoA + glycine = CoA + 2-amino-3- oxobutanoate
Enzyme 23 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 23 Reactions
  • acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-20
Enzyme 23 Transmembrane Regions Not Available
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 3342906 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O75600 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name KBL_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1260 bp
ATGTGGCCTGGGAACGCCTGGCGCGCCGCACTCTTCTGGGTGCCCCGCGGCCGCCGCGCA
CAGTCAGCGCTGGCCCAGCTGCGTGGCATTCTGGAGGGGGAGCTGGAAGGCATCCGCGGA
GCTGGCACTTGGAAGAGTGAGCGGGTCATCACGTCCCGTCAGGGGCCGCACATCCGCGTG
GACGGCGTCTCCGGAGGAATCCTCAACTTCTGTGCCAACAACTACCTGGGCCTGAGCAGC
CACCCTGAGGTGATTCAGGCAGGTCTGCAGGCTCTGGAGGAGTTTGGAGCTGGCCTTAGC
TCGGTCCGCTTCATCTGTGGAACCCAGAGCATCCACAAGAATCTAGAAGCAAAAATAGCC
CGCTTCCACCAGCGGGAGGATGCCATCCTCTATCCCAGCTGTTATGACGCCAACGCCGGC
CTCTTTGAGGCCCTGCTGACCCCAGAGGACGCAGTCCTGTCGGACGAGCTGAACCATGCC
TCCATCATCGACGGCATCCGGCTGTGCAAGGCCCACAAGTACCGCTATCGCCACCTGGAC
ATGGCCGACCTAGAAGCCAAGCTGCAGGAGGCCCAGAAGCATCGGCTGCGCCTGGTGGCC
ACCGATGGGGCCTTTTCCATGGATGGCGACATCGCACCCCTGCAGGAGATCTGCTGCCTC
GCCTCTAGATATGGTGCCCTGGTCTTCATGGATGAATGCCATGCCACTGGTTTCCTGGGG
CCCACAGGACGGGGCACAGATGAGCTGCTGGGTGTGATGGACCAGGTCACCATCATCAAC
TCCACCCTGGGGAAGGCCCTGGGTGGAGCATCAGGGGGCTACACGACAGGGCCTGGGCCC
CTGGTGTCACTGCTGCGGCAGCGCGCCCGGCCATACCTCTTCTCCAACAGTCTGCCACCT
GCTGTCGTTGGCTGCGCCTCCAAGGCCCTAGATCTGCTGATGGGGAGTAACACCATTGTC
CAGTCTATGGCTGCCAAGACCCAGAGGTTCCGTAGTAAGATGGAAGCTGCTGGCTTCACT
ATCTCAGGAGCCAGTCACCCCATCTGCCCTGTGATGCTGGGTGATGCCCGGCTGGCCTCT
CGCATGGCGGATGACATGCTGAAGAGAGGCATCTTTGTCATCGGGTTCAGCTACCCCGTG
GTCCCCAAGGGCAAGGCCCGGATCCGGGTACAGATCTCAGCAGTGCATAGCGAGGAAGAC
ATTGACCGCTGCGTGGAGGCCTTCGTGGAAGTGGGGCGACTGCACGGGGCACTGCCCTGA
Enzyme 23 GenBank Gene ID AF077740 Link Image
Enzyme 23 GeneCard ID GCAT Link Image
Enzyme 23 GenAtlas ID GCAT Link Image
Enzyme 23 HGNC ID HGNC:4188 Link Image
Enzyme 23 Chromosome Location 22
Enzyme 23 Locus 22q13.1
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Edgar AJ, Polak JM: Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. Eur J Biochem. 2000 Mar;267(6):1805-12. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5279
Enzyme 24 Name Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor
Enzyme 24 Synonyms
  1. PDHE1-A type II
Enzyme 24 Gene Name PDHA2
Enzyme 24 Protein Sequence >Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor
MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGL
KYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG
VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACK
YKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDY
YKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYR
TREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE
ELGHHIYSSDSSFEVRGANPWIKFKSVS
Enzyme 24 Number of Residues 388
Enzyme 24 Molecular Weight 42934
Enzyme 24 Theoretical pI 8.56
Enzyme 24 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Energy production and conversion
Enzyme 24 Specific Function The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 24 Pathways
Enzyme 24 Reactions
  • pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-15
Enzyme 24 Transmembrane Regions Not Available
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 190790 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P29803 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name ODPAT_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1167 bp
ATGCTGGCCGCCTTCATCTCCCGCGTGTTGAGGCGAGTTGCCCAGAAATCAGCTCGCAGA
GTGCTGGTGGCATCCCGTAACTCCTCAAATGACGCTACATTTGAAATTAAGAAATGTGAT
CTTTATCTGTTGGAAGAGGGTCCCCCTGTCACTACAGTGCTCACTAGGGCGGAGGGGCTT
AAATACTACAGGATGATGCTGACTGTTCGCCGCATGGAATTGAAGGCAGATCAGCTGTAC
AAACAGAAATTCATTCGCGGTTTCTGTCACCTGTGCGATGGTCAGGAAGCTTGTTGCGTG
GGCCTTGAGGCCGGCATAAACCCCTCGGATCACGTCATTACATCCTATAGGGCTCATGGT
GTGTGCTATACTCGGGGACTTTCTGTCCGATCCATTCTCGCAGAGCTGACGGGAAGAAGA
GGAGGTTGTGCTAAAGGAAAAGGAGGATCGATGCATATGTATACCAAGAACTTCTATGGG
GGCAATGGCATCGTCGGTGCACAGGGCCCCCTGGGCGCTGGCATTGCTCTGGCCTGTAAA
TATAAAGGAAACGATGAGATCTGTTTGACTTTATATGGGGATGGCGCTGCGAATCAGGGG
CAGATAGCCGAAGCTTTCAATATGGCAGCTTTATGGAAATTACCTTGTGTTTTCATCTGT
GAGAATAACCTATATGGAATGGGAACATCTACTGAGAGAGCAGCAGCCAGCCCTGATTAC
TACAAGAGGGGCAATTTTATCCCTGGGCTAAAGGTCGATGGAATGGATGTTCTGTGTGTT
CGTGAGGCAACAAAATTTGCAGCTAACTACTGTAGATCTGGAAAGGGGCCCATACTGATG
GAGCTGCAAACCTACCGTTATCATGGACACAGTATGAGTGATCCTGGAGTCAGTTATCGT
ACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGGGATCCTATAATAATTCTCCAAGAT
AGAATGGTAAACAGCAAGCTCGCCACTGTGGAAGAATTAAAGGAAATTGGGGCTGAGGTG
AGGAAAGAAATTGATGATGCTGCCCAGTTTGCTACCACTGATCCTGAGCCACATTTGGAA
GAATTAGGCCATCACATCTACAGCAGTGATTCATCTTTTGAAGTTCGTGGTGCAAATCCA
TGGATCAAGTTTAAGTCCGTCAGTTAA
Enzyme 24 GenBank Gene ID M86808 Link Image
Enzyme 24 GeneCard ID PDHA2 Link Image
Enzyme 24 GenAtlas ID PDHA2 Link Image
Enzyme 24 HGNC ID HGNC:8807 Link Image
Enzyme 24 Chromosome Location 4
Enzyme 24 Locus 4q22-q23
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Dahl HH, Brown RM, Hutchison WM, Maragos C, Brown GK: A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4. Genomics. 1990 Oct;8(2):225-32. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5281
Enzyme 25 Name Glucosamine 6-phosphate N-acetyltransferase
Enzyme 25 Synonyms
  1. Phosphoglucosamine transacetylase
  2. Phosphoglucosamine acetylase
Enzyme 25 Gene Name GNPNAT1
Enzyme 25 Protein Sequence >Glucosamine 6-phosphate N-acetyltransferase
MKPDETPMFDPSLLKEVDWSQNTATFSPAISPTHPGEGLVLRPLCTADLNRGFFKVLGQL
TETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVE
DVVVSDECRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFGYTVSEENYMCR
RFLK
Enzyme 25 Number of Residues 184
Enzyme 25 Molecular Weight 20749
Enzyme 25 Theoretical pI 8.12
Enzyme 25 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 25 General Function Transcription
Enzyme 25 Specific Function Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
Enzyme 25 Pathways
Enzyme 25 Reactions
  • acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 21748766 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q96EK6 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name GNA1_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >555 bp
ATGAAACCTGATGAAACTCCTATGTTTGACCCAAGTCTACTCAAAGAAGTGGACTGGAGT
CAGAATACAGCTACATTTTCTCCAGCCATTTCCCCAACACATCCTGGAGAAGGCTTGGTT
TTGAGGCCTCTTTGTACTGCTGACTTAAATAGAGGTTTTTTTAAGGTATTGGGTCAGCTA
ACAGAGACTGGAGTTGTCAGCCCTGAACAATTTATGAAATCTTTTGAGCATATGAAGAAA
TCTGGGGATTATTATGTTACAGTTGTAGAAGATGTGACTCTAGGACAGATTGTTGCTACG
GCAACTCTGATTATAGAACATAAATTCATCCATTCCTGTGCTAAGAGAGGAAGAGTAGAA
GATGTTGTTGTTAGTGATGAATGCAGAGGAAAGCAGCTTGGCAAATTGTTATTATCAACC
CTTACTTTGCTAAGCAAGAAACTGAACTGTTACAAGATTACCCTTGAATGTCTACCACAA
AATGTTGGTTTCTATAAAAAGTTTGGATATACTGTATCTGAAGAAAACTACATGTGTCGG
AGGTTTCTAAAGTAA
Enzyme 25 GenBank Gene ID AK090577 Link Image
Enzyme 25 GeneCard ID GNPNAT1 Link Image
Enzyme 25 GenAtlas ID GNPNAT1 Link Image
Enzyme 25 HGNC ID HGNC:19980 Link Image
Enzyme 25 Chromosome Location 14
Enzyme 25 Locus 14q22.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5284
Enzyme 26 Name Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor
Enzyme 26 Synonyms
  1. Pyruvate dehydrogenase complex E2 subunit
  2. PDCE2
  3. E2
  4. Dihydrolipoamide S- acetyltransferase component of pyruvate dehydrogenase complex
  5. PDC- E2
  6. 70 kDa mitochondrial autoantigen of primary biliary cirrhosis
  7. PBC
  8. M2 antigen complex 70 kDa subunit
Enzyme 26 Gene Name DLAT
Enzyme 26 Protein Sequence >Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor
MSPHCSTTYLRTLGRTTMFWKTTEGRDGKMAVQEFSEFGLLLQLLGSPGRRYYSLPPHQK
VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEG
TRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGS
SYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLA
KILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTP
QPLAPTPSTPCPATPAGPKGRVFVDPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV
PSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN
MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSV
AVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGI
KNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLA
EFRKYLEKPITMLL
Enzyme 26 Number of Residues 614
Enzyme 26 Molecular Weight 65782
Enzyme 26 Theoretical pI 5.95
Enzyme 26 GO Classification
Function
  • S-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • dihydrolipoyllysine-residue acetyltransferase activity
  • protein binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • protein complex
  • pyruvate dehydrogenase complex
Enzyme 26 General Function Energy production and conversion
Enzyme 26 Specific Function The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 26 Pathways
Enzyme 26 Reactions
  • acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 35360 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P10515 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name ODP2_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1848 bp
CGAGTGACCTCGCGATCTGGCCCGGCTCCCGCTCGTCGCAACAGCGTGACTACAGGGTAT
GGCGGGGTCCGGGCACTGTGCGGCTGGACCCCCAGTTCTGGGGCCACGCCGCGGAACCGC
TTACTGCTGCAGCTTTTGGGGTCGCCCGGCCGCCGCTATTACAGTCTTCCCCCGCATCAG
AAGGTTCCATTGCCTTCTCTTTCCCCCACAATGCAGGCAGGCACCATAGCCCGTTGGAAA
AAAAAAGAGGGGGACAAAATCAATGAAGGTGACCTAATTGCAGAGGTTGAAACTGATAAA
GCCACTGTTGGATTTGAGAGCCTGGAGGAGTGTTATATGGCAAAGATACTTGTTGCTGAA
GGTACCAGGGATGTTCCCATCGGAGCGATCATCTGTATCACAGTTGGCAAGCCTGAGGAT
ATTGAGGCCTTTAAAAATTATACACTGGATTCCTCAGCAGCACCTACCCCACAAGCGGCC
CCAGCACCAACCCCTGCTGCCACTGCTTCGCCACCTACACCTTCTGCTCAGGCTCCTGGT
AGCTCATATCCCCCTCACATGCAGGTACTTCTTCCTGCCCTCTCTCCCACCATGACCATG
GGCACAGTTCAGAGATGGGAAAAAAAAGTGGGTGAGAAGCTAAGTGAAGGAGACTTACTG
GCAGAGATAGAAACTGACAAAGCCACTATAGGTTTTGAAGTACAGGAAGAAGGTTATCTG
GCAAAAATCCTGGTCCCTGAAGGCACAAGAGATGTCCCTCTAGGAACCCCACTCTGTATC
ATTGTAGAAAAAGAGGCAGATATATCAGCATTTGCTGACTATAGGCCAACCGAAGTAACA
GATTTAAAACCACAAGTGCCACCACCTACCCCACCCCCGGTGGCCGCTGTTCCTCCAACT
CCCCAGCCTTTAGCTCCTACACCTTCAGCACCCTGCCCAGCTACTCCTGCTGGACCAAAG
GGAAGGGTGTTTGTTAGCCCTCTTGCAAAGAAGTTGGCAGTAGAGAAAGGGATTGATCTT
ACACAAGTAAAAGGGACAGGACCAGATGGTAGAATCACCAAGAAGGATATCGACTCTTTT
GTGCCTAGTAAAGTTGCTCCTGCTCCGGCAGCTGTTGTGCCTCCCACAGGTCCTGGAATG
GCACCAGTTCCTACAGGTGTCTTCACAGATATCCCAATCAGCAACATTCGTCGGGTTATT
GCACAGCGATTAATGCAATCAAAGCAAACCATACCTCATTATTACCTTTCTATCGATGTA
AATATGGGAGAAGTTTTGTTGGTACGGAAAGAACTTAATAAGATATTAGAAGGGAGAAGC
AAAATTTCTGTCAATGACTTCATCATAAAAGCTTCAGCTTTGGCATGTTTAAAAGTTCCC
GAAGCAAATTCTTCTTGGATGGACACAGTTATAAGACAAAATCATGTTGTTGATGTCAGT
GTTGCGGTCAGTACTCCTGCAGGACTCATCACACCTATTGTGTTTAATGCACATATAAAA
GGAGTGGAAACCATTGCTAATGATGTTGTTTCTTTAGCAACCAAAGCAAGAGAGGGTAAA
CTACAGCCACATGAATTCCAGGGTGGCACTTTTACGATCTCCAATTTAGGAATGTTTGGA
ATTAAGAATTTCTCTGCTATTATTAACCCACCTCAAGCATGTATTTTGGCAATTGGTGCT
TCAGAGGATAAACTGGTCCCTGCAGATAATGAAAAAGGGTTTGATGTGGCTAGCATGATG
TCTGTTACACTCAGTTGTGATCACCGGGTGGTGGATGGAGCAGTTGGAGCCCAGTGGCTT
GCTGAGTTTAGAAAGTACCTTGAAAAACCTATCACTATGTTGTTGTAA
Enzyme 26 GenBank Gene ID Y00978 Link Image
Enzyme 26 GeneCard ID DLAT Link Image
Enzyme 26 GenAtlas ID DLAT Link Image
Enzyme 26 HGNC ID HGNC:2896 Link Image
Enzyme 26 Chromosome Location 11
Enzyme 26 Locus 11q23.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Coppel RL, McNeilage LJ, Surh CD, Van de Water J, Spithill TW, Whittingham S, Gershwin ME: Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7317-21. [PubMed Link Image]
  2. Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS: Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 1988 Nov 21;240(1-2):45-8. [PubMed Link Image]
  3. Howard MJ, Fuller C, Broadhurst RW, Perham RN, Tang JG, Quinn J, Diamond AG, Yeaman SJ: Three-dimensional structure of the major autoantigen in primary biliary cirrhosis. Gastroenterology. 1998 Jul;115(1):139-46. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5542
Enzyme 27 Name Peroxisomal carnitine O-octanoyltransferase
Enzyme 27 Synonyms
  1. COT
Enzyme 27 Gene Name CROT
Enzyme 27 Protein Sequence >Peroxisomal carnitine O-octanoyltransferase
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS
GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT
QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF
RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL
TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG
DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR
DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI
QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ
QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV
LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF
HDMIQLMNSTHL
Enzyme 27 Number of Residues 612
Enzyme 27 Molecular Weight 70179
Enzyme 27 Theoretical pI 7.09
Enzyme 27 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl- CoA, to its corresponding carnitine ester
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions
  • octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 6066280 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q9UKG9 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name OCTC_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1839 bp
ATGGAAAATCAATTGGCTAAATCAACTGAAGAACGAACATTTCAGTACCAGGATTCTCTT
CCATCACTGCCTGTTCCTTCACTTGAAGAATCATTAAAAAAATACCTTGAATCAGTGAAA
CCATTTGCAAATCAAGAAGAATATAAGAAAACTGAAGAAATAGTTCAAAAATTTCAAAGT
GGGATTGGAGAAAAATTGCACCAGAAATTGCTTGAAAGAGCAAAAGGAAAAAGAAATTGG
CTGGAAGAGTGGTGGCTGAATGTTGCCTATCTGGATGTTCGTATACCATCACAATTGAAT
GTCAACTTTGCGGGTCCTGCAGCTCATTTTGAACACTACTGGCCTCCAAAGGAAGGGACT
CAATTAGAAAGAGGAAGTATAACTCTTTGGCATAACTTGAACTACTGGCAGCTATTAAGA
AAAGAAAAGTTGCCTGTTCATAAAGTTGGAAATACTCCTCTAGATATGAATCAATTCCGA
ATGCTATTTTCTACCTGCAAGGTTCCAGGAATTACTAGAGACTCCATTATGAATTATTTT
AGGACTGAGAGTGAAGGGCGTTCCCCAAACCACATTGTAGTGCTGTGTCGAGGCCGAGCT
TTTGTCTTTGATGTAATACATGAAGGATGTTTGGTCACCCCGCCAGAGCTTCTCAGACAA
CTGACATATATCCACAAGAAGTGCCATAGTGAACCTGATGGACCTGGGATTGCAGCATTA
ACTAGTGAGGAGCGAACTCGATGGGCTAAGGCACGAGAATATCTGATTGGTCTTGATCCA
GAGAACTTGGCTTTGTTAGAAAAAATTCAGAGTAGTTTACTGGTATATTCCATGGAGGAT
AGCAGTCCACATGTAACACCAGAGGATTATTCTGAGATTATTGCAGCCATCCTTATTGGA
GATCCAACAGTACGCTGGGGTGACAAATCCTATAACTTGATTTCCTTTTCTAATGGAGTA
TTTGGCTGTAATTGTGATCATGCTCCTTTTGATGCAATGATTATGGTGAACATCAGTTAT
TATGTGGATGAGAAAATTTTTCAGAATGAAGGAAGATGGAAGGGTTCAGAGAAGGTACGA
GATATACCACTTCCAGAAGAGCTCATTTTCATTGTGGATGAGAAAGTTTTAAATGACATC
AACCAAGCTAAAGCCCAGTATCTCAGGGAGGCATCTGATCTACAGATTGCGGCTTATGCC
TTTACATCTTTTGGCAAAAAGCTAACCAAGAACAAGATGCTTCACCCGGATACGTTTATT
CAGCTTGCACTTCAGCTGGCCTATTACAGACTTCATGGACACCCTGGTTGTTGCTATGAA
ACAGCTATGACAAGACATTTTTATCATGGCCGTACAGAGACTATGCGATCATGCACAGTT
GAAGCAGTGAGGTGGTGCCAGTCCATGCAGGATCCTTCTGTCAATCTTCGTGAGCGGCAG
CAAAAGATGTTACAAGCTTTTGCAAAGCATAATAAAATGATGAAAGATTGTTCAGCTGGA
AAAGGATTTGATCGTCACCTTTTAGGTCTCTTACTCATAGCAAAAGAGGAAGGTCTTCCT
GTTCCAGAACTCTTTACGGACCCACTTTTTTCCAAAAGCGGAGGAGGTGGAAATTTTGTT
CTCTCAACAAGTCTGGTTGGCTATTTACGAGTCCAGGGAGTGGTAGTTCCCATGGTACAC
AATGGTTATGGATTTTTCTACCATATCAGAGATGACAGGTTTGTTGTGGCCTGTTCAGCC
TGGAAATCCTGTCCCGAGACTGATGCGGAAAAGCTAGTTCAGCTGACTTTTTGTGCTTTT
CATGATATGATACAGCTGATGAACTCTACTCATCTTTAG
Enzyme 27 GenBank Gene ID AF168793 Link Image
Enzyme 27 GeneCard ID CROT Link Image
Enzyme 27 GenAtlas ID CROT Link Image
Enzyme 27 HGNC ID HGNC:2366 Link Image
Enzyme 27 Chromosome Location 7
Enzyme 27 Locus 7q21.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Ferdinandusse S, Mulders J, IJlst L, Denis S, Dacremont G, Waterham HR, Wanders RJ: Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids. Biochem Biophys Res Commun. 1999 Sep 16;263(1):213-8. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5543
Enzyme 28 Name Carnitine O-palmitoyltransferase I, muscle isoform
Enzyme 28 Synonyms
  1. CPT I
  2. CPTI-M
  3. Carnitine palmitoyltransferase 1B
  4. Carnitine palmitoyltransferase I-like protein
Enzyme 28 Gene Name CPT1B
Enzyme 28 Protein Sequence >Carnitine O-palmitoyltransferase I, muscle isoform
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPT
SWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTG
IFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPR
VSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEE
YIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALG
IVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDL
EMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVA
LDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPI
IGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKAL
ADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREG
RTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCL
YLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGY
GVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
Enzyme 28 Number of Residues 772
Enzyme 28 Molecular Weight 87802
Enzyme 28 Theoretical pI 8.77
Enzyme 28 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 28 Pathways
Enzyme 28 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • 48-73 103-122
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 1621202 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q92523 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name CPT1B_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >2319 bp
ATGGCGGAAGCTCACCAGGCCGTGGCCTTCCAGTTCACGGTGACCCCAGACGGGGTCGAC
TTCCGGCTCAGTCGGGAGGCCCTGAAACACGTCTACCTGTCTGGGATCAACTCCTGGAAG
AAACGCCTGATCCGCATCAAGAATGGCATCCTCAGGGGCGTGTACCCTGGCAGCCCCACC
AGCTGGCTGGTCGTCATCATGGCAACAGTGGGTTCCTCCTTCTGCAACGTGGACATCTCC
TTGGGGCTGGTCAGTTGCATCCAGAGATGCCTCCCTCAGGGGTGTGGCCCCTACCAGACC
CCGCAGACCCGGGCACTTCTCAGCATGGCCATCTTCTCCACGGGCGTCTGGGTGACGGGC
ATCTTCTTCTTCCGCCAAACCCTGAAGCTGCTTCTCTGCTACCATGGGTGGATGTTTGAG
ATGCATGGCAAGACCAGCAACTTGACCAGGATCTGGGCTATGTGTATCCGCCTTCTATCC
AGCCGGCACCCTATGCTCTACAGCTTCCAGACATCTCTGCCCAAGCTTCCTGTGCCCAGG
GTGTCAGCCACAATTCAGCGGTACCTAGAGTCTGTGCGCCCCTTGTTGGATGATGAGGAA
TATTACCGCATGGAGTTGCTGGCCAAAGAATTCCAGGACAAGACTGCCCCCAGGCTGCAG
AAATACCTGGTGCTCAAGTCATGGTGGGCAAGTAACTATGTGAGTGACTGGTGGGAAGAG
TACATCTACCTTCGAGGCAGGAGCCCTCTCATGGTGAACAGCAACTATTATGTCATGGAC
CTTGTGCTCATCAAGAATACAGACGTGCAGGCAGCCCGCCTGGGAAACATCATCCACGCC
ATGATCATGTATCGCCGTAAACTGGACCGTGAAGAAATCAAGCCTGTGATGGCACTGGGC
ATAGTGCCTATGTGCTCCTACCAGATGGAGAGGATGTTCAACACCACTCGGATCCCGGGC
AAGGACACAGATGTGCTACAGCACCTCTCAGACAGCCGGCACGTGGCTGTCTACCACAAG
GGACGCTTCTTCAAGCTGTGGCTCTATGAGGGCGCCCGTCTGCTCAAGCCTCAGGATCTG
GAGATGCAGTTCCAGAGGATCCTGGACGACCCCTCCCCACCTCAGCCTGGGGAGGAGAAG
CTGGCAGCCCTCACTGCAGGAGGAAGGGTGGAGTGGGCGCAGGCACGCCAGGCCTTCTTT
AGCTCTGGAAAGAATAAGGCTGCCTTGGAGGCCATCGAGCGTGCCGCTTTCTTCGTGGCC
CTGGATGAGGAATCCTACTCCTATGACCCCGAAGATGAGGCCAGCCTCAGCCTCTATGGC
AAGGCCCTGCTACATGGCAACTGCTACAACAGGTGGTTTGACAAATCCTTCACTCTCATT
TCCTTCAAGAATGGCCAGTTGGGTCTCAATGCAGAGCATGCGTGGGCAGATGCTCCCATC
ATTGGGCACCTCTGGGAGTTTGTCCTGGGCACAGACAGCTTCCACCTGGGCTACACGGAG
ACCGGGCACTGCCTGGGCAAACCGAACCCTGCGCTCGCACCTCCTACACGGCTGCAGTGG
GACATTCCAAAACAGTGCCAGGCGGTCATCGAGAGTTCCTACCAGGTGGCCAAGGCGTTG
GCAGACGACGTGGAGTTGTACTGCTTCCAGTTCCTGCCCTTTGGCAAAGGCCTCATCAAG
AAGTGCCGGACCAGCCCTGATGCCTTTGTGCAGATCGCGCTGCAGCTGGCTCACTTCCGG
GACAGGGGTAAGTTCTGCCTGACCTATGAGGCCTCAATGACCAGAATGTTCCGGGAGGGA
CGGACTGAGACTGTGCGTTCCTGTACCAGCGAGTCCACAGCCTTTGTGCAGGCCATGATG
GAGGGGTCCCACACAAAAGCAGACCTGCGAGATCTCTTCCAGAAGGCTGCTAAGAAGCAC
CAGAATATGTACCGCCTGGCCATGACCGGGGCAGGGATCGACAGGCACCTCTTCTGCCTT
TACTTGGTCTCCAAGTACCTAGGAGTCAGCTCTCCTTTCCTTGCTGAGGTGCTCTCGGAA
CCCTGGCGTCTCTCCACCAGCCAGATCCCCCAATCCCAGATCCGCATGTTCGACCCAGAG
CAGCACCCCAATCACCTGGGCGCTGGAGGTGGCTTTGGCCCTGTAGCAGATGATGGCTAT
GGAGTTTCCTACATGATTGCAGGCGAGAACACGATCTTCTTCCACATCTCCAGCAAGTTC
TCAAGCTCAGAGACGAACGCCCAGCGCTTTGGAAACCACATCCGCAAAGCCCTGCTGGAC
ATTGCTGATCTTTTCCAAGTTCCCAAGGCCTACAGCTGA
Enzyme 28 GenBank Gene ID D87812 Link Image
Enzyme 28 GeneCard ID CPT1B Link Image
Enzyme 28 GenAtlas ID CPT1B Link Image
Enzyme 28 HGNC ID HGNC:2329 Link Image
Enzyme 28 Chromosome Location 22
Enzyme 28 Locus 22q13.33
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Yamazaki N, Shinohara Y, Shima A, Yamanaka Y, Terada H: Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I. Biochim Biophys Acta. 1996 Jun 7;1307(2):157-61. [PubMed Link Image]
  2. Zhu H, Shi J, de Vries Y, Arvidson DN, Cregg JM, Woldegiorgis G: Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I. Arch Biochem Biophys. 1997 Nov 1;347(1):53-61. [PubMed Link Image]
  3. Britton CH, Mackey DW, Esser V, Foster DW, Burns DK, Yarnall DP, Froguel P, McGarry JD: Fine chromosome mapping of the genes for human liver and muscle carnitine palmitoyltransferase I (CPT1A and CPT1B). Genomics. 1997 Feb 15;40(1):209-11. [PubMed Link Image]
  4. van der Leij FR, Takens J, van der Veen AY, Terpstra P, Kuipers JR: Localization and intron usage analysis of the human CPT1B gene for muscle type carnitine palmitoyltransferase I. Biochim Biophys Acta. 1997 May 30;1352(2):123-8. [PubMed Link Image]
  5. Yamazaki N, Yamanaka Y, Hashimoto Y, Shinohara Y, Shima A, Terada H: Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I. FEBS Lett. 1997 Jun 16;409(3):401-6. [PubMed Link Image]
  6. Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O: Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. DNA Res. 2001 Feb 28;8(1):1-9. [PubMed Link Image]
  7. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5544
Enzyme 29 Name Carnitine O-palmitoyltransferase I, liver isoform
Enzyme 29 Synonyms
  1. CPT I
  2. CPTI-L
  3. Carnitine palmitoyltransferase 1A
Enzyme 29 Gene Name CPT1A
Enzyme 29 Protein Sequence >Carnitine O-palmitoyltransferase I, liver isoform
MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKKFIRFKNGIITGVYPASPS
SWLIVVVGVMTTMYAKIDPSLGIIAKINRTLETANCMSSQTKNVVSGVLFGTGLWVALIV
TMRYSLKVLLSYHGWMFTEHGKMSRATKIWMGMVKIFSGRKPMLYSFQTSLPRLPVPAVK
DTVNRYLQSVRPLMKEEDFKRMTALAQDFAVGLGPRLQWYLKLKSWWATNYVSDWWEEYI
YLRGRGPLMVNSNYYAMDLLYILPTHIQAARAGNAIHAILLYRRKLDREEIKPIRLLGST
IPLCSAQWERMFNTSRIPGEETDTIQHMRDSKHIVVYHRGRYFKVWLYHDGRLLKPREME
QQMQRILDNTSEPQPGEARLAALTAGDRVPWARCRQAYFGRGKNKQSLDAVEKAAFFVTL
DETEEGYRSEDPDTSMDSYAKSLLHGRCYDRWFDKSFTFVVFKNGKMGLNAEHSWADAPI
VAHLWEYVMSIDSLQLGYAEDGHCKGDINPNIPYPTRLQWDIPGECQEVIETSLNTANLL
ANDVDFHSFPFVAFGKGIIKKCRTSPDAFVQLALQLAHYKDMGKFCLTYEASMTRLFREG
RTETVRSCTTESCDFVRAMVDPAQTVEQRLKLFKLASEKHQHMYRLAMTGSGIDRHLFCL
YVVSKYLAVESPFLKEVLSEPWRLSTSQTPQQQVELFDLENNPEYVSSGGGFGPVADDGY
GVSYILVGENLINFHISSKFSCPETDSHRFGRHLKEAMTDIITLFGLSSNSKK
Enzyme 29 Number of Residues 773
Enzyme 29 Molecular Weight 88369
Enzyme 29 Theoretical pI 8.84
Enzyme 29 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 29 Pathways
Enzyme 29 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 48-73 103-122
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 755646 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P50416 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name CPT1A_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >2322 bp
ATGGCAGAAGCTCACCAAGCTGTGGCCTTTCAGTTCACGGTCACTCCGGACGGGATTGAC
CTGCGGCTGAGCCATGAAGCTCTTAGACAAATCTATCTCTCTGGACTTCATTCCTGGAAA
AAGAAGTTCATCAGATTCAAGAACGGCATCATCACTGGCGTGTACCCGGCAAGCCCCTCC
AGTTGGCTTATCGTGGTGGTGGGCGTGATGACAACGATGTACGCCAAGATCGACCCCTCG
TTAGGAATAATTGCAAAAATCAATCGGACTCTGGAAACGGCCAACTGCATGTCCAGCCAG
ACGAAGAACGTGGTCAGCGGCGTGCTGTTTGGCACCGGCCTGTGGGTGGCCCTCATCGTC
ACCATGCGCTACTCCCTGAAAGTGCTGCTCTCCTACCACGGGTGGATGTTCACTGAGCAC
GGCAAGATGAGTCGTGCCACCAAGATCTGGATGGGTATGGTCAAGATCTTTTCAGGCCGA
AAACCCATGTTGTACAGCTTCCAGACATCGCTGCCTCGCCTGCCGGTCCCGGCTGTCAAA
GACACTGTGAACAGGTATCTACAGTCGGTGAGGCCTCTTATGAAGGAAGAAGACTTCAAA
CGGATGACAGCACTTGCTCAAGATTTTGCTGTCGGTCTTGGACCAAGATTACAGTGGTAT
TTGAAGTTAAAATCCTGGTGGGCTACAAATTACGTGAGCGACTGGTGGGAGGAGTACATC
TACCTCCGAGGACGAGGGCCGCTCATGGTGAACAGCAACTATTATGCCATGGATCTGCTG
TATATCCTTCCAACTCACATTCAGGCAGCAAGAGCCGGCAACGCCATCCATGCCATCCTG
CTTTACAGGCGCAAACTGGACCGGGAGGAAATCAAACCAATTCGTCTTTTGGGATCCACG
ATTCCACTCTGCTCCGCTCAGTGGGAGCGGATGTTTAATACTTCCCGGATCCCAGGAGAG
GAGACAGACACCATCCAGCACATGAGAGACAGCAAGCACATCGTCGTGTACCATCGAGGA
CGCTACTTCAAGGTCTGGCTCTACCATGATGGGCGGCTGCTGAAGCCCCGGGAGATGGAG
CAGCAGATGCAGAGGATCCTGGACAATACCTCGGAGCCTCAGCCCGGGGAGGCCAGGCTG
GCAGCCCTCACCGCAGGAGACAGAGTTCCCTGGGCCAGGTGTCGTCAGGCCTATTTTGGA
CGTGGGAAAAATAAGCAGTCTCTTGATGCTGTGGAGAAAGCAGCGTTCTTCGTGACGTTA
GATGAAACTGAAGAAGGATACAGAAGTGAAGACCCGGATACGTCAATGGACAGCTACGCC
AAATCTCTACTACACGGCCGATGTTACGACAGGTGGTTTGACAAGTCGTTCACGTTTGTT
GTCTTCAAAAACGGGAAGATGGGCCTCAACGCTGAACACTCCTGGGCAGATGCGCAGATC
GTGGCCCACCTTTGGGAGTACGTCATGTCCATTGACAGCCTCCAGCTGGGCTATGCGGAG
GATGGGCACTGCAAAGGCGACATCAATCCGAACATTCCGTACCCCACCAGGCTGCAGTGG
GACATCCCGGGGGAATGTCAAGAGGTTATAGAGACCTCCCTGAACACCGCAAATCTTCTG
GCAAACGACGTGGATTTCCATTCCTTCCCATTCGTAGCCTTTGGTAAAGGAATCATCAAG
AAATGTCGCACGAGCCCAGACACCTTTGTGCAGCTGGCCCTCCAGCTGGCGCACTACAAG
GACATGGGCAAGTTTTGCCTCACATACGAGGCCTCCATGACCCGGCTCTTCCGAGAGGGG
AGGACGGAGACCGTGCGCTCCTGCACCACTGAGTCATGCGACTTCGTGCGGGCCATGGTG
GACCCGGCCCAGACGGTGGAACAGAGGCTGAAGTTGTTCAAGTTGGCGTCTGAGAAGCAT
CAGCATATGTATCGCCTCGCCATGACCGGCTCTGGGATCGATCGTCACCTCTTCTGCCTT
TACGTGGTGTCTAAATATCTCGCTGTGGAGTCCCCTTTCCTTAAGGAAGTTTTATCTGAG
CCTTGGAGATTATCAACAAGCCAGACCCCTCAGCAGCAAGTGGAGCTGTTTGACTTGGAG
AATAACCCAGAGTACGTGTCCAGCGGAGGGGGCTTTGGACCGGTTGCTGATGACGGCTAT
GGTGTGTCGTACATCCTTGTGGGAGAGAACCTCATCAATTTCCACATTTCTTCCAAGTTC
TCTTGCCCTGAGACGGATTCTCATCGCTTTGGAAGGCACCTGAAAGAAGCAATGACTGAC
ATCATCACTTTGTTTGGTCTCAGTTCTAATTCCAAAAAGTAA
Enzyme 29 GenBank Gene ID L39211 Link Image
Enzyme 29 GeneCard ID CPT1A Link Image
Enzyme 29 GenAtlas ID CPT1A Link Image
Enzyme 29 HGNC ID HGNC:2328 Link Image
Enzyme 29 Chromosome Location 11
Enzyme 29 Locus 11q13.1-q13.2
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Britton CH, Schultz RA, Zhang B, Esser V, Foster DW, McGarry JD: Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene. Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):1984-8. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5677
Enzyme 30 Name 2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
Enzyme 30 Synonyms
  1. Alpha-ketoglutarate dehydrogenase
Enzyme 30 Gene Name OGDH
Enzyme 30 Protein Sequence >2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEE
MYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNV
DKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDES
DLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFET
PGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSEN
GVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINR
VTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIV
YETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDP
EAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKY
AELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPR
SMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMA
FGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSL
SEYGVLGFEAGLRMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLP
HGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFH
VLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKR
LLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEH
KNQGYYDYVKPRLRTTISRAKPVWYAGRNPAAAPATGNKKTH
Enzyme 30 Number of Residues 1002
Enzyme 30 Molecular Weight 113477
Enzyme 30 Theoretical pI 7.08
Enzyme 30 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
  • oxoglutarate dehydrogenase (succinyl-transferring) activity
  • thiamin pyrophosphate binding
  • vitamin binding
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 30 General Function Energy production and conversion
Enzyme 30 Specific Function The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components:2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 30 Pathways
Enzyme 30 Reactions
  • 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 531241 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q02218 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ODO1_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >3009 bp
ATGTTTCATTTAAGGACTTGTGCTGCTAAGTTGAGGCCATTGACGGCTTCCCAGACTGTT
AAGACATTTTCACAAAACAGACCAGCAGCAGCTAGGACATTTCAACAGATTCGGTGCTAT
TCTGCACCTGTTGCTGCTGAGCCCTTTCTCAGTGGGACTAGTTCGAACTATGTGGAGGAG
ATGTACTGTGCTTGGCTGGAAAACCCCAAAAGTGTACATAAGTCATGGGACATTTTTTTT
CGCAACACGAATGCCGGAGCCCCACCGGGCACTGCCTACCAGAGTCCCCTTCCCCTGAGC
CGAGGCTCCCTGGCTGCTGTGGCCCATGCACAGTCCCTGGTAGAAGCACAGCCCAACGTG
GACAAGCTCGTGGAGGACCACCTGGCAGTGCAGTCACTCATCAGGGCATATCAGATACGA
GGGCACCATGTAGCACAGCTGGACCCCCTGGGGATTTTGGATGCTGATCTGGACTCCTCC
GTGCCCGCTGACATTATCTCATCCACAGACAAACTTGGGTTCTATGGCCTGGATGAGTCT
GACCTCGACAAGGTCTTCCACTTGCCCACCACCACTTTCATCGGGGGACAGGAATCAGCA
CTTCCTCTGCGGGAGATCATCCGTCGGCTGGAGATGGCCTACTGCCAGCATATTGGGGTG
GAGTTCATGTTCATCAATGACCTGGAGCAGTGCCAGTGGATCCGGCAGAAGTTTGAGACC
CCTGGGATCATGCAGTTCACAAATGAGGAGAAACGGACCCTGCTGGCCAGGCTTGTGCGG
TCCACCAGGTTTGAGGAGTTCCTACAGCGGAAGTGGTCCTCTGAGAAGCGCTTTGGTCTA
GAAGGCTGCGAGGTACTGATCCCTGCCCTCAAGACCATCATTGACAAGTCTAGTGAGAAT
GGCGTGGACTACGTGATCATGGGCATGCCACACAGAGGGCGGCTGAACGTGCTTGCAAAT
GTCATCAGGAAGGAGCTGGAACAGATCTTCTGTCAATTCGATTCAAAGCTGGAGGCAGCT
GATGAGGGCTCCGGAGATGTGAAGTACCACCTGGGCATGTATCACCGCAGGATCAATCGT
GTCACCGACAGGAACATTACCTTGTCCTTGGTGGCCAACCCTTCCCACCTTGAGGCCGCT
GACCCCGTGGTGATGGGCAAGACCAAAGCCGAACAGTTTTACTGTGGCGACACTGAAGGG
AAAAAGGTCATGTCCATCCTGTTGCATGGGGATGCTGCATTTGCTGGCCAGGGCATTGTG
TACGAGACCTTCCACCTCAGCGACCTGCCATCCTACACAACTCATGGCACCGTGCACGTG
GTCGTCAACAACCAGATCGGCTTCACCACCGACCCTCGGATGGCCCGCTCCTCCCCCTAC
CCCACTGACGTGGCCCGAGTGGTGAATGCCCCCATTTTCCACGTGAACTCAGATGACCCC
GAGGCTGTCATGTACGTGTGCAAAGTGGCGGCCGAGTGGAGGAGCACCTTCCACAAGGAC
GTGGTTGTCGATTTGGTGTGTTACCGGCGCAACGGCCACAACGAGATGGATGAGCCCATG
TTCACGCAGCCGCTCATGTACAAGCAGATCCGCAAGCAGAAGCCTGTGTTACAGAAGTAC
GCTGAGCTGCTGGTGTCGCAGGGTGTGGTCAACCAGCCTGAGTATGAGGAGGAAATTTCC
AAGTATGATAAGATCTGTGAGGAAGCTTTTGCCAGATCTAAAGATGAGAAGATCTTGCAC
ATTAAGCACTGGCTGGACTCTCCCTGGCCTGGCTTCTTCACCCTGGACGGGCAGCCCAGG
AGCATGTCCTGCCCCTCCACGGGTCTGACGGAGGATATTCTGACACACATCGGGAATGTG
GCTAGTTCTGTGCCTGTGGAAAACTTTACTATTCATGGAGGGCTGAGCCGGATCTTGAAG
ACTCGTGGGGAAATGGTGAAGAACCGGACTGTGGACTGGGCTCTAGCGGAGTACATGGCG
TTTGGCTCGCTCCTGAAGGAGGGCATCCACATTCGGCTGAGCGGCCAGGACGTGGAGCGG
GGCACATTCAGCCACCGCCACCATGTGCTCCATGACCAGAATGTGGACAAGAGAACCTGC
ATCCCCATGAACCATCTCTGGCCCAATCAGGCCCCCTATACTGTGTGCAACAGCTCACTG
TCTGAGTACGGCGTGCTGGGCTTTGAAGCTGGGCTTCGCATGGCCAGTCCTAATGCCCTG
GTCCTCTGGGAAGCCCAATTTGGTGACTTCCACAACACGGCCCAGTGTATCATCGACCAG
TTCATCTGCCCGGGACAAGCCAAGTGGGTGCGGCAGAATGGCATCGTGTTGCTGCTGCCC
CATGGCATGGAGGGCATGGGTCCAGAACATTCCTCCGCCCGCCCAGAGCGGTTCTTGCAG
ATGTGCAACGATGACCCAGATGTCCTGCCAGACCTTAAAGAAGCCAACTTCGACATCAAT
CAGCTATATGACTGCAATTGGGTTGTTGTCAACTGCTCCACTCCTGGCAACTTCTTCCAC
GTGCTACGACGCCAGATCCTGCTGCCATTCCGGAAGCCGTTAATTATCTTCACCCCCAAA
TCCCTGTTGCGCCACCCCGAGGCCAGATCCAGCTTTGATGAGATGCTTCCAGGAACCCAC
TTCCAGCGGGTGATCCCAGAAGATGGCCCTGCAGCTCAGAACCCAGAAAATGTCAAAAGG
CTTCTCTTCTGCACCGGCAAAGTGTATTATGACCTCACCCGGGAGCGCAAAGCACGCGAC
ATGGTGGGGCAGGTGGCCATCACAAGGATTGAGCAGCTGTCGCCATTCCCCTTTGACCTC
CTGCTGAAGGAGGTGCAGAAGTACCCCAATGCTGAGCTGGCCTGGTGCCAGGAGGAGCAC
AAGAACCAAGGCTACTATGACTACGTGAAGCCAAGACTTCGGACCACCATCAGCCGCGCC
AAGCCCGTCTGGTATGCCGGCCGGAACCCAGCGGCTGCTCCAGCCACCGGCAACAAGAAG
ACCCACTGA
Enzyme 30 GenBank Gene ID D10523 Link Image
Enzyme 30 GeneCard ID OGDH Link Image
Enzyme 30 GenAtlas ID OGDH Link Image
Enzyme 30 HGNC ID HGNC:8124 Link Image
Enzyme 30 Chromosome Location 7
Enzyme 30 Locus 7p14-p13
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Koike K, Urata Y, Goto S: Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1963-7. [PubMed Link Image]
  2. Koike K: The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14. Gene. 1995 Jul 4;159(2):261-6. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5746
Enzyme 31 Name Sterol O-acyltransferase 2
Enzyme 31 Synonyms
  1. Cholesterol acyltransferase 2
  2. Acyl coenzyme A:cholesterol acyltransferase 2
  3. ACAT-2
Enzyme 31 Gene Name SOAT2
Enzyme 31 Protein Sequence >Sterol O-acyltransferase 2
MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQL
RELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHF
RTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLA
PYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFL
MKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKN
FAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLH
CWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARG
VAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTM
LFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT
Enzyme 31 Number of Residues 522
Enzyme 31 Molecular Weight 59897
Enzyme 31 Theoretical pI 8.71
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa
Enzyme 31 Pathways
Enzyme 31 Reactions
  • acyl-CoA + cholesterol = CoA + cholesterol ester
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 124-144 155-175 200-220 262-282 304-324 344-366 437-457 472-492
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 3746535 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID O75908 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name SOAT2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1569 bp
ATGGAGCCAGGCGGGGCCCGTCTGCGTCTGCAGAGGACAGAAGGGCTGGGAGGGGAGCGG
GAGCGCCAACCCTGTGGAGATGGAAACACTGAGACGCACAGAGCCCCGGACTTGGTACAA
TGGACCCGACACATGGAGGCTGTGAAGGCACAATTGCTGGAGCAAGCGCAGGGACAACTG
AGGGAGCTGCTGGATCGGGCCATGCGGGAGGCTATACAATCCTACCCATCACAAGACAAA
CCTCTGCCCCCACCTCCCCCAGGTTCCTTGAGCAGGACCCAGGAGCCATCCCTGGGGAAA
CAGAAAGTTTTCATCATCCGCAAGTCCCTGCTTGATGAGCTGATGGAGGTGCAGCATTTC
CGCACCATCTACCACATGTTCATCGCTGGCCTGTGTGTCTTCATCATCAGCACCCTGGCC
ATCGACTTCATTGATGAGGGCAGGCTGCTGCTGGAGTTTGACCTACTGATCTTCAGCTTC
GGACAGCTGCCATTGGCGCTGGTGACCTGGGTGCCCATGTTTCTGTCCACCCTGTTGGCG
CCGTACCAGGCCCTACGGCTGTGGGCCAGGGGCACCTGGACGCAGGCGACGGGCCTGGGC
TGTGCGCTGCTAGCCGCCCACGCCGTGGTGCTCTGCGCGCTGCCGGTCCACGTGGCCGTG
GAGCATCAGCTCCCGCCGGCCTCCCGTTGTGTCCTGGTCTTCGAGCAGGTTAGGTTCCTG
ATGAAAAGCTACTCCTTCCTGAGAGAGGCTGTGCCTGGGACCCTTCGTGCCAGACGAGGT
GAGGGGATCCAGGCCCCCAGTTTCTCCAGCTACCTCTACTTCCTCTTCTGCCCAACACTC
ATCTACAGGGAGACTTACCCTAGGACGCCCTATGTCAGGTGGAATTATGTGGCCAAGAAC
TTTGCCCAGGCCCTGGGATGTGTGCTCTATGCCTGCTTCATCCTGGGCCGCCTCTGTGTT
CCTGTCTTTGCCAACATGAGCCGAGAGCCCTTCAGCACCCGTGCCCTGGTGCTCTCTATC
CTGCATGCCACGTTGCCAGGCATCTTCATGCTGCTGCTCATCTTCTTTGCCTTCCTCCAT
TGCTGGCTCAACGCCTTTGCCGAGATGCTACGATTTGGAGACAGGATGTTCTACCGGGAC
TGGTGGAACTCAACGTCCTTCTCCAACTACTACCGCACTTGGAACGTGGTGGTCCATGAC
TGGCTGTACAGCTACGTGTATCAGGATGGGCTGCGGCTCCTTGGTGCCCGGGCCCGAGGG
GTAGCCATGCTGGGTGTGTTCCTGGTCTCCGCAGTGGCCCATGAGTATATCTTCTGCTTC
GTCCTGGGGTTCTTCTATCCCGTCATGCTGATACTCTTCCTTGTCATTGGAGGAATGTTG
AACTTCATGATGCATGACCAGCGCACCGGCCCGGCATGGAACGTGCTGATGTGGACCATG
CTGTTTCTAGGCCAGGGAATCCAGGTCAGCCTGTACTGCCAGGAGTGGTACGCACGGCGG
CACTGCCCCTTACCCCAGGCAACTTTCTGGGGGCTGGTGACACCTCGATCTTGGTCCTGC
CATACCTAG
Enzyme 31 GenBank Gene ID AF059203 Link Image
Enzyme 31 GeneCard ID SOAT2 Link Image
Enzyme 31 GenAtlas ID SOAT2 Link Image
Enzyme 31 HGNC ID HGNC:11178 Link Image
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [PubMed Link Image]
  2. Chang CC, Sakashita N, Ornvold K, Lee O, Chang ET, Dong R, Lin S, Lee CY, Strom SC, Kashyap R, Fung JJ, Farese RV Jr, Patoiseau JF, Delhon A, Chang TY: Immunological quantitation and localization of ACAT-1 and ACAT-2 in human liver and small intestine. J Biol Chem. 2000 Sep 8;275(36):28083-92. [PubMed Link Image]
  3. Katsuren K, Tamura T, Arashiro R, Takata K, Matsuura T, Niikawa N, Ohta T: Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-2) gene and its relation to dyslipidemia. Biochim Biophys Acta. 2001 Apr 30;1531(3):230-40. [PubMed Link Image]
  4. Song BL, Qi W, Yang XY, Chang CC, Zhu JQ, Chang TY, Li BL: Organization of human ACAT-2 gene and its cell-type-specific promoter activity. Biochem Biophys Res Commun. 2001 Mar 30;282(2):580-8. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5751
Enzyme 32 Name Sterol O-acyltransferase 1
Enzyme 32 Synonyms
  1. Cholesterol acyltransferase 1
  2. Acyl coenzyme A:cholesterol acyltransferase 1
  3. ACAT-1
Enzyme 32 Gene Name SOAT1
Enzyme 32 Protein Sequence >Sterol O-acyltransferase 1
MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEE
LKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGK
IFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGK
FPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPT
YVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYF
LFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSAR
VLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTW
NVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFM
FFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVR
PRSWTCRYVF
Enzyme 32 Number of Residues 550
Enzyme 32 Molecular Weight 64735
Enzyme 32 Theoretical pI 9.18
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase
Enzyme 32 Pathways
Enzyme 32 Reactions
  • acyl-CoA + cholesterol = CoA + cholesterol ester
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 141-159 320-341 361-382 470-490 498-518
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 4878022 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P35610 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name SOAT1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1653 bp
ATGGTGGGTGAAGAGAAGATGTCTCTAAGAAACCGGCTGTCAAAGTCCAGGGAAAATCCT
GAGGAAGATGAAGACCAGAGAAACCCTGCAAAGGAGTCCCTAGAGACACCTAGTAATGGT
CGAATTGACATAAAACAGTTGATAGCAAAGAAGATAAAGTTGACAGCAGAGGCAGAGGAA
TTGAAGCCATTTTTTATGAAGGAAGTTGGCAGTCACTTTGATGATTTTGTGACCAATCTC
ATTGAAAAGTCAGCATCATTAGATAATGGTGGGTGCGCTCTCACAACCTTTTCTGTTCTT
GAAGGAGAGAAAAACAACCATAGAGCGAAGGATTTGAGAGCACCTCCAGAACAAGGAAAG
ATTTTTATTGCAAGGCGCTCTCTCTTAGATGAACTGCTTGAAGTGGACCACATCAGAACA
ATATATCACATGTTTATTGCCCTCCTCATTCTCTTTATCCTCAGCACACTTGTAGTAGAT
TACATTGATGAAGGAAGGCTGGTGCTTGAGTTCAGCCTCCTGTCTTATGCTTTTGGCAAA
TTTCCTACCGTTGTTTGGACCTGGTGGATCATGTTCCTGTCTACATTTTCAGTTCCCTAT
TTTCTGTTTCAACATTGGGCCACTGGCTATAGCAAGAGTTCTCATCCGCTGATCCGTTCT
CTCTTCCATGGCTTTCTTTTCATGATCTTCCAGATTGGAGTTCTAGGTTTTGGACCAACA
TATGTTGTGTTAGCATATACACTGCCACCAGCTTCCCGGTTCATCATTATATTCGAGCAG
ATTCGTTTTGTAATGAAGGCCCACTCATTTGTCAGAGAGAACGTGCCTCGGGTACTAAAT
TCAGCTAAGGAGAAATCAAGCACTGTTCCAATACCTACAGTCAACCAGTATTTGTACTTC
TTATTTGCTCCTACCCTTATCTACCGTGACAGCTATCCCAGGAATCCCACTGTAAGATGG
GGTTATGTCGCTATGAAGTTTGCACAGGTCTTTGGTTGCTTTTTCTATGTGTACTACATC
TTTGAAAGGCTTTGTGCCCCCTTGTTTCGGAATATCAAACAGGAGCCCTTCAGCGCTCGT
GTTCTGGTCCTATGTGTATTTAACTCCATCTTGCCAGGTGTGCTGATTCTCTTCCTTACT
TTTTTTGCCTTTTTGCACTGCTGGCTCAATGCCTTTGCTGAGATGTTACGCTTTGGTGAC
AGGATGTTCTATAAGGATTGGTGGAACTCCACGTCATACTCCAACTATTATAGAACCTGG
AATGTGGTGGTCCATGACTGGCTATATTACTATGCTTACAAGGACTTTCTCTGGTTTTTC
TCCAAGAGATTCAAATCTGCTGCCATGTTAGCTGTCTTTGCTGTATCTGCTGTAGTACAC
GAATATGCCTTGGCTGTTTGCTTGAGCTTTTTCTATCCCGTGCTCTTCGTGCTCTTCATG
TTCTTTGGAATGGCTTTCAACTTCATTGTCAATGATAGTCGGAAAAAGCCGATTTGGAAT
GTTCTGATGTGGACTTCTCTTTTCTTGGGCAATGGAGTCTTACTCTGCTTTTATTCTCAA
GAATGGTATGCACGTCGGCACTGTCCTCTGAAAAATCCCACATTTTTGGATTATGTCCGG
CCACGTTCCTGGACTTGTCGTTACGTGTTTTAG
Enzyme 32 GenBank Gene ID L21934 Link Image
Enzyme 32 GeneCard ID SOAT1 Link Image
Enzyme 32 GenAtlas ID SOAT1 Link Image
Enzyme 32 HGNC ID HGNC:11177 Link Image
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Chang CC, Huh HY, Cadigan KM, Chang TY: Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells. J Biol Chem. 1993 Oct 5;268(28):20747-55. [PubMed Link Image]
  2. Lin S, Cheng D, Liu MS, Chen J, Chang TY: Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains. J Biol Chem. 1999 Aug 13;274(33):23276-85. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5762
Enzyme 33 Name N-acetylglutamate synthase, mitochondrial precursor
Enzyme 33 Synonyms
  1. Amino-acid acetyltransferase[Contains: N-acetylglutamate synthase long form
  2. N-acetylglutamate synthase short form
  3. N-acetylglutamate synthase conserved domain form]
Enzyme 33 Gene Name NAGS
Enzyme 33 Protein Sequence >N-acetylglutamate synthase, mitochondrial precursor
MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPP
EEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEA
RHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAP
TAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVS
VETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLR
DSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTE
LFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYV
SEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNP
INPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS
Enzyme 33 Number of Residues 534
Enzyme 33 Molecular Weight 58157
Enzyme 33 Theoretical pI 9.12
Enzyme 33 GO Classification
Function
  • N-acetyltransferase activity
  • acetylglutamate kinase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
  • transferase activity, transferring phosphorus-containing groups
Process
  • amino acid and derivative metabolism
  • amino acid biosynthesis
  • amino acid metabolism
  • arginine biosynthesis
  • arginine metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • urea cycle intermediate metabolism
Component
Enzyme 33 General Function Amino acid transport and metabolism
Enzyme 33 Specific Function Plays a role in the regulation of ureagenesis by producing variable amounts of N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPSI) activity
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions
  • acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-21
Enzyme 33 Transmembrane Regions Not Available
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 22651769 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q8N159 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name NAGS_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1605 bp
ATGGCGACGGCGCTGATGGCTGTGGTTCTGCGGGCAGCTGCTGTAGCCCCGAGGCTGAGA
GGCCGGGGAGGCACTGGGGGCGCCCGAAGGCTGAGCTGTGGCGCGCGGCGGCGGGCGGCG
AGGGGCACCAGCCCGGGGCGCCGGCTCAGCACCGCCTGGTCGCAGCCCCAGCCCCCGCCC
GAGGAGTACGCGGGCGCGGACGACGTCTCCCAGTCGCCCGTCGCCGAGGAGCCGTCGTGG
GTGCCGAGTCCCAGGCCCCCGGTGCCCCACGAGTCCCCAGAGCCTCCTTCGGGCCGCTCG
CTGGTGCAGCGGGACATCCAGGCCTTCCTGAACCAGTGCGGGGCCAGCCCTGGGGAGGCG
CGCCACTGGCTCACGCAGTTCCAGACCTGCCATCACTCCGCGGACAAGCCCTTCGCCGTC
ATCGAGGTGGACGAGGAGGTGCTCAAGTGCCAGCAGGGCGTATCCAGTCTGGCCTTTGCC
CTGGCCTTCTTGCAGCGCATGGACATGAAGCCGCTGGTGGTCCTGGGGCTGCCGGCCCCT
ACGGCTCCCTCGGGCTGTCTTTCCTTCTGGGAGGCCAAGGCGCAGCTGGCCAAGAGCTGC
AAGGTGCTGGTAGACGCGCTTCGACACAACGCCGCCGCTGCTGTGCCATTTTTTGGCGGC
GGGTCTGTGCTACGCGCTGCCGAGCCGGCTCCCCATGCCAGCTACGGCGGCATCGTCTCG
GTGGAGACAGACCTGCTGCAGTGGTGCCTGGAGTCGGGCAGCATCCCCATCCTGTGCCCC
ATCGGGGAGACGGCCGCGCGCCGCTCCGTGCTTCTCGACTCCCTGGAGGTGACCGCGTCG
CTGGCCAAGGCGCTGCGGCCCACCAAAATCATCTTCCTCAATAACACAGGCGGCCTGCGC
GACAGCAGTCATAAGGTCCTGAGTAACGTGAACCTGCCCGCCGACCTGGACCTGGTGTGC
AACGCCGAGTGGGTGAGCACAAAAGAACGGCAGCAGATGCGGCTCATCGTGGACGTGCTC
AGCCGCCTGCCCCACCACTCCTCGGCCGTCATCACCGCCGCTAGCACGCTGCTCACTGAG
CTCTTTAGCAACAAGGGGTCCGGGACCCTGTTCAAGAACGCCGAGCGAATGCTACGGGTG
CGCAGCCTGGACAAGCTGGACCAGGGCCGTCTAGTGGACCTGGTCAACGCCAGCTTCGGC
AAGAAGCTCAGGGACGACTACCTGGCCTCGCTGCGCCCGCGGCTGCACTCCATCTACGTC
TCCGAGGGGTACAACGCCGCCGCCATTCTGACCATGGAGCCCGTCCTGGGGGGCACCCCG
TACCTGGACAAATTTGTGGTGAGCTCCAGCCGCCAGGGCCAAGGCTCCGGCCAGATGCTG
TGGGAGTGCCTGCGGCGGGACCTTCAGACACTTTTCTGGCGCTCCCGGGTCACCAACCCC
ATCAATCCCTGGTACTTCAAACACAGTGATGGCAGCTTCTCCAACAAGCAGTGGATCTTC
TTCTGGTTTGGCCTGGCTGATATCCGGGACTCCTATGAGTTGGTCAACCACGCCAAGGGA
CTGCCAGACTCCTTTCACAAGCCAGCTTCTGACCCAGGCAGCTGA
Enzyme 33 GenBank Gene ID AY116537 Link Image
Enzyme 33 GeneCard ID NAGS Link Image
Enzyme 33 GenAtlas ID NAGS Link Image
Enzyme 33 HGNC ID HGNC:17996 Link Image
Enzyme 33 Chromosome Location 17
Enzyme 33 Locus 17q21.31
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Haberle J, Schmidt E, Pauli S, Kreuder JG, Plecko B, Galler A, Wermuth B, Harms E, Koch HG: Mutation analysis in patients with N-acetylglutamate synthase deficiency. Hum Mutat. 2003 Jun;21(6):593-7. [PubMed Link Image]
  2. Caldovic L, Morizono H, Gracia Panglao M, Gallegos R, Yu X, Shi D, Malamy MH, Allewell NM, Tuchman M: Cloning and expression of the human N-acetylglutamate synthase gene. Biochem Biophys Res Commun. 2002 Dec 13;299(4):581-6. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5821
Enzyme 34 Name Bile acid CoA:amino acid N-acyltransferase
Enzyme 34 Synonyms
  1. BAT
  2. BACAT
  3. Glycine N-choloyltransferase
  4. Long-chain fatty-acyl-CoA hydrolase
Enzyme 34 Gene Name BAAT
Enzyme 34 Protein Sequence >Bile acid CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
Enzyme 34 Number of Residues 418
Enzyme 34 Molecular Weight 46300
Enzyme 34 Theoretical pI 7.00
Enzyme 34 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs
Enzyme 34 Pathways
Enzyme 34 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 532505 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q14032 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name BAAT_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1257 bp
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
Enzyme 34 GenBank Gene ID L34081 Link Image
Enzyme 34 GeneCard ID BAAT Link Image
Enzyme 34 GenAtlas ID BAAT Link Image
Enzyme 34 HGNC ID HGNC:932 Link Image
Enzyme 34 Chromosome Location 9
Enzyme 34 Locus 9q22.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed Link Image]
  2. Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5842
Enzyme 35 Name Long-chain-fatty-acid--CoA ligase 4
Enzyme 35 Synonyms
  1. Long-chain acyl-CoA synthetase 4
  2. LACS 4
Enzyme 35 Gene Name ACSL4
Enzyme 35 Protein Sequence >Long-chain-fatty-acid--CoA ligase 4
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
Enzyme 35 Number of Residues 711
Enzyme 35 Molecular Weight 79189
Enzyme 35 Theoretical pI 8.51
Enzyme 35 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 35 General Function Lipid transport and metabolism
Enzyme 35 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates
Enzyme 35 Pathways
Enzyme 35 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-23
Enzyme 35 Transmembrane Regions Not Available
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 3158351 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID O60488 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name ACSL4_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2013 bp
ATGGCAAAGAGAATAAAAGCTAAGCCCACTTCAGACAAACCTGGAAGTCCATATCGCTCT
GTCACACACTTCGACTCACTAGCTGTAATAGACATCCCTGGAGCAGATACTCTGGATAAA
TTATTTGACCATGCTGTATCCAAGTTTGGGAAGAAGGACAGCCTTGGGACCAGGGAAATC
CTAAGTGAAGAAAATGAAATGCAGCCAAATGGAAAAGTTTTTAAGAAGTTAATTCTTGGG
AATTATAAATGGATGAACTATCTTGAAGTGAATCGCAGAGTGAATAACTTTGGTAGTGGA
CTCACTGCACTGGGACTAAAACCAAAGAACACCATTGCCATCTTCTGTGAGACCAGGGCC
GAATGGATGATTGCAGCACAGACCTGCTTTAAGTACAACTTTCCTCTTGTGACTTTATAT
GCCACACTTGGCAAAGAAGCAGTAGTTCATGGGCTAAATGAATCTGAGGCTTCCTATCTG
ATTACCAGTGTTGAACTTCTGGAAAGTAAACTTAAGACTGCATTGTTAGATATCAGTTGT
GTTAAACATATCATTTATGTGGACAATAAGGCTATCAATAAAGCAGAGTACCCTGAAGGA
TTTGAGATTCACAGCATGCAATCAGTAGAAGAGTTGGGATCTAACCCAGAAAACTTGGGC
ATTCCTCCAAGTAGACCAACGCCTTCAGACATGGCCATTGTTATGTATACTAGTGGTTCT
ACTGGCCGACCTAAGGGAGTGATGATGCATCATAGCAATTTGATAGCTGGAATGACAGGC
CAGTGTGAAAGAATACCTGGACTGGGACCGAAGGACACATATATTGGCTACTTGCCTTTG
GCTCATGTGCTAGAACTGACAGCAGAGATATCTTGCTTTACCTATGGCTGCAGGATTGGA
TATTCTTCTCCGCTTACACTCTCTGACCAGTCCAGCAAAATTAAAAAAGGAAGCAAAGGA
GACTGTACTGTACTGAAGCCCACACTTATGGCTGCTGTTCCGGAAATCATGGATAGAATT
TATAAGAATGTTATGAGCAAAGTCCAAGAGATGAATTATATTCAGAAAACTCTGTTCAAG
ATAGGGTATGATTACAAATTGGAACAGATCAAAAAGGGATATGATGCACCTCTTTGCAAT
CTGTTACTGTTTAAAAAGGTCAAGGCCCTGCTGGGAGGGAATGTCCGCATGATGCTGTCT
GGAGGGGCCCCGCTATCTCCTCAGACACACCGATTCATGAATGTCTGCTTCTGCTGCCCA
ATTGGCCAGGGTTATGGACTGACAGAATCATGTGGTGCTGGGACAGTTACTGAAGTAACT
GACTATACTACTGGCAGAGTTGGAGCACCTCTTATTTGCTGTGAAATTAAGCTAAAAGAC
TGGCAAGAAGGCGGTTATACAATTAATGACAAGCCAAACCCCAGAGGTGAAATCGTAATT
GGTGGACAGAACATCTCCATGGGATATTTTAAAAATGAAGAGAAAACAGCAGAAGATTAT
TCTGTGGATGAAAATGGACAAAGGTGGTTTTGCACTGGTGATATTGGAGAATTCCATCCC
GATGGATGTTTACAGATTATAGATCGTAAGAAAGATCTAGTGAAGTTACAAGCAGGAGAG
TATGTATCTCTTGGGAAAGTAGAAGCTGCACTGAAGAATTGTCCACTTATTGACAACATC
TGTGCTTTTGCCAAAAGTGATCAGTCCTATGTGATCAGTTTTGTGGTTCCTAACCAGAAA
AGGTTGACACTTTTGGCACAACAGAAAGGGGTAGAAGGAACTTGGGTTGATATCTGCAAT
AATCCTGCTATGGAAGCTGAAATACTGAAAGAAATTCGAGAAGCTGCAAATGCCATGAAA
TTGGAGCGATTTGAAATTCCAATCAAGGTTCGATTAAGCCCAGAGCCATGGACCCCTGAA
ACTGGTTTGGTAACTGATGCTTTCAAACTGAAAAGGAAGGAGCTGAGGAACCATTACCTC
AAAGACATTGAACGAATGTATGGGGGCAAATAA
Enzyme 35 GenBank Gene ID AF030555 Link Image
Enzyme 35 GeneCard ID ACSL4 Link Image
Enzyme 35 GenAtlas ID ACSL4 Link Image
Enzyme 35 HGNC ID HGNC:3571 Link Image
Enzyme 35 Chromosome Location X
Enzyme 35 Locus Xq22.3-q23
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Cao Y, Traer E, Zimmerman GA, McIntyre TM, Prescott SM: Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4). Genomics. 1998 Apr 15;49(2):327-30. [PubMed Link Image]
  2. Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ, Villanova M, Zollo M, Borsani G, Ballabio A, Renieri A: FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics. 1998 Feb 1;47(3):350-8. [PubMed Link Image]
  3. Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A: FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat Genet. 2002 Apr;30(4):436-40. Epub 2002 Mar 11. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5849
Enzyme 36 Name Long-chain-fatty-acid--CoA ligase 1
Enzyme 36 Synonyms
  1. Long-chain acyl-CoA synthetase 1
  2. LACS 1
  3. Palmitoyl-CoA ligase 1
  4. Long-chain fatty acid CoA ligase 2
  5. Long-chain acyl-CoA synthetase 2
  6. LACS 2
  7. Acyl-CoA synthetase 1
  8. ACS1
  9. Palmitoyl-CoA ligase 2
Enzyme 36 Gene Name ACSL1
Enzyme 36 Protein Sequence >Long-chain-fatty-acid--CoA ligase 1
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
Enzyme 36 Number of Residues 698
Enzyme 36 Molecular Weight 77944
Enzyme 36 Theoretical pI 7.16
Enzyme 36 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 36 General Function Lipid transport and metabolism
Enzyme 36 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate
Enzyme 36 Pathways
Enzyme 36 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 25-45
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 219900 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID P33121 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name ACSL1_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2097 bp
ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG
Enzyme 36 GenBank Gene ID D10040 Link Image
Enzyme 36 GeneCard ID ACSL1 Link Image
Enzyme 36 GenAtlas ID ACSL1 Link Image
Enzyme 36 HGNC ID HGNC:3569 Link Image
Enzyme 36 Chromosome Location 4
Enzyme 36 Locus 4q34-q35
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed Link Image]
  2. Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed Link Image]
  3. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5894
Enzyme 37 Name Long-chain-fatty-acid--CoA ligase 6
Enzyme 37 Synonyms
  1. Long-chain acyl-CoA synthetase 6
  2. LACS 6
Enzyme 37 Gene Name ACSL6
Enzyme 37 Protein Sequence >Long-chain-fatty-acid--CoA ligase 6
MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQ
SEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQW
LSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT
LGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQK
CGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF
LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP
TIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI
QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV
GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD
IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGI
VVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS
DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM
Enzyme 37 Number of Residues 697
Enzyme 37 Molecular Weight 77753
Enzyme 37 Theoretical pI 7.46
Enzyme 37 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 37 General Function Lipid transport and metabolism
Enzyme 37 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid
Enzyme 37 Pathways
Enzyme 37 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-37
Enzyme 37 Transmembrane Regions Not Available
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 5702202 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9UKU0 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name ACSL6_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >2094 bp
ATGCAGACACAGGAGATCCTGAGGATACTGCGACTGCCTGAGCTAGGTGACTTGGAACAG
TTTTTCCGCAGCCTCTCGGCCACCACCCTCGTGAGTATGGGTGCCCTGGCTGCCATCCTT
GCCTACTGGTTCACTCAGCGGCCAAAGGCCTTGCAGCCGCCATGCAACCTCCTGATGCAG
TCAGAAGAAGTAGAGGACAGTGGCGGGGCACGGCGATCTGTGATTGGGTCTGGCCCTCAG
CTACTTACCCACTACTATGATGATGCCCGGACCATGTACCAGGTGTTCCGCCGTGGGCTT
AGCATCTCAGGGAATGGGCCCTGTCTTGGTTTCAGGAAGCCTAAGCAGCCTTACCAGTGG
CTGTCCTACCAGGAGGTGGCCGACAGGGCTGAATTTCTGGGGTCCGGACTTCTCCAGCAC
AATTGTAAAGCATGCACTGATCAGTTTATTGGTGTTTTTGCACAAAATCGGCCAGAGTGG
ATCATTGTGGAGCTGGCCTGCTACACATATTCCATGGTGGTGGTCCCGCTCTATGACACC
CTGGGCCCTGGGGCTATCCGCTACATCATCAATACAGCGGACATCAGCACCGTGATTGTG
GACAAACCTCAGAAGGCTGTGCTTCTGCTAGAGCATGTGGAGAGGAAGGAGACTCCAGGC
CTCAAGCTGATCATCCTCATGGACCCATTCGAAGAAGCCCTGAAAGAGAGAGGGCAGAAG
TGCGGGGTGGTCATTAAGTCCATGCAGGCCGTGGAGGACTGTGGCCAAGAGAATCACCAG
GCTCCTGTGCCCCCGCAGCCTGATGACCTCTCCATTGTGTGTTTCACAAGCGGCACGACA
GGGAACCCAAAAGGTGCGATGCTCACCCATGGGAACGTGGTGGCTGATTTCTCAGGCTTT
CTGAAAGTGACAGAGAGTCAGTGGGCTCCCACTTGTGCGGATGTGCACATTTCCTATTTG
CCTTTAGCACACATGTTTGAGCGAATGGTGCAGTCTGTCGTCTATTGCCACGGAGGGCGT
GTTGGCTTCTTCCAGGGAGATATCCGCCTTCTCTCAGATGACATGAAGGCTCTATGCCCC
ACCATCTTCCCTGTGGTCCCACGACTGCTGAACCGGATGTACGACAAGATCTTCAGCCAG
GCAAACACACCATTAAAGCGCTGGCTCCTGGAGTTTGCAGCAAAGCGTAAGCAAGCCGAG
GTCCGGAGTGGAATCATCAGGAATGATAGTATCTGGGATGAACTCTTCTTTAATAAGATT
CAGGCCAGTCTTGGTGGGTGTGTGCGGATGATTGTTACTGGAGCAGCCCCAGCATCACCA
ACAGTTCTGGGATTTCTCCGGGCAGCTCTAGGGTGCCAGGTTTATGAAGGTTATGGCCAA
ACTGAGTGCACAGCTGGATGTACCTTCACCACTCCTGGCGACTGGACCTCAGGGCACGTA
GGGGCGCCACTTCCCTGCAATCATATCAAGCTCGTTGATGTTGAGGAACTGAACTACTGG
GCCTGCAAAGGAGAGGGAGAGATATGTGTGAGAGGACCAAATGTGTTCAAAGGCTACTTG
AAAGATCCAGACAGGACGAAGGAGGCCCTGGACAGCGATGGCTGGCTTCACACTGGAGAC
ATCGGAAAATGGCTGCCGGCAGGAACTCTTAAAATTATTGATCGGAAAAAGCATATATTT
AAACTTGCTCAGGGAGAATATGTTGCACCCGAGAAGATTGAGAACATCTACATCCGGAGC
CAACCTGTGGCGCAAATCTATGTCCATGGGGACAGCTTAAAGGCCTTTTTGGTAGGCATT
GTTGTGCCTGACCCTGAAGTTATGCCCTCCTGGGCCCAGAAGAGAGGAATTGAAGGAACA
TATGCAGATCTCTGCACAAATAAGGATCTGAAGAAAGCCATTTTGGAAGATATGGTGAGG
TTAGGAAAAGAAAGTGGACTCCATTCTTTTGAGCAGGTTAAAGCCATTCACATCCATTCT
GACATGTTCTCAGTTCAAAATGGCTTGCTGACCCCAACACTAAAAGCTAAGAGACCTGAG
CTGAGAGAGTACTTCAAAAAACAAATAGAAGAGCTTTACTCAATCCCCATGTGA
Enzyme 37 GenBank Gene ID AF129166 Link Image
Enzyme 37 GeneCard ID ACSL6 Link Image
Enzyme 37 GenAtlas ID ACSL6 Link Image
Enzyme 37 HGNC ID HGNC:16496 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
  2. Yagasaki F, Jinnai I, Yoshida S, Yokoyama Y, Matsuda A, Kusumoto S, Kobayashi H, Terasaki H, Ohyashiki K, Asou N, Murohashi I, Bessho M, Hirashima K: Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13). Genes Chromosomes Cancer. 1999 Nov;26(3):192-202. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 5916
Enzyme 38 Name Long-chain-fatty-acid--CoA ligase 5
Enzyme 38 Synonyms
  1. Long-chain acyl-CoA synthetase 5
  2. LACS 5
Enzyme 38 Gene Name ACSL5
Enzyme 38 Protein Sequence >Long-chain-fatty-acid--CoA ligase 5
MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVS
QKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGS
CLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADI
AMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLG
KEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDV
AISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYD
KVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGA
APMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVA
DMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR
KKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKL
GVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLK
AKRGELSKYFRTQIDSLYEHIQD
Enzyme 38 Number of Residues 683
Enzyme 38 Molecular Weight 75992
Enzyme 38 Theoretical pI 6.91
Enzyme 38 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 38 General Function Lipid transport and metabolism
Enzyme 38 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids
Enzyme 38 Pathways
Enzyme 38 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • 1-35
Enzyme 38 Transmembrane Regions Not Available
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 6174680 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q9ULC5 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name ACSL5_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >2052 bp
ATGCTTTTTATCTTTAACTTTTTGTTTTCCCCACTTCCGACCCCGGCGTTGATCTGCATC
CTGACATTTGGAGCTGCCATCTTCTTGTGGCTGATCACCAGACCTCAACCCGTCTTACCT
CTTCTTGACCTGAACAATCAGTCTGTGGGAATTGAGGGAGGAGCACGGAAGGGGGTTTCC
CAGAAGAACAATGACCTAACAAGTTGCTGCTTCTCAGATGCCAAGACTATGTATGAGGTT
TTCCAAAGAGGACTCGCTGTGTCTGACAATGGGCCCTGCTTGGGATATAGAAAACCAAAC
CAGCCCTACAGATGGCTATCTTACAAACAGGTGTCTGATAGAGCAGAGTACCTGGGTTCC
TGTCTCTTGCATAAAGGTTATAAATCATCACCAGACCAGTTTGTCGGCATCTTTGCTCAG
AATAGGCCAGAGTGGATCATCTCCGAATTGGCTTGTTACACGTACTCTATGGTAGCTGTA
CCTCTGTATGACACCTTGGGACCAGAAGCCATCGTACATATTGTCAACAAGGCTGATATC
GCCATGGTGATCTGTGACACACCCCAAAAGGCATTGGTGCTGATAGGGAATGTAGAGAAA
GGCTTCACCCCGAGCCTGAAGGTGATCATCCTTATGGACCCCTTTGATGATGACCTGAAG
CAAAGAGGGGAGAAGAGTGGAATTGAGATCTTATCCCTATATGATGCTGAGAACCTAGGC
AAAGAGCACTTCAGAAAACCTGTGCCTCCTAGCCCAGAAGACCTGAGCGTCATCTGCTTC
ACCAGTGGGACCACAGGTGACCCCAAAGGAGCCATGATAACCCATCAAAATATTGTTTCA
AATGCTGCTGCCTTTCTCAAATGTGTGGAGCATGCTTATGAGCCCACTCCTGATGATGTG
GCCATATCCTACCTCCCTCTGGCTCATATGTTTGAGAGGATTGTACAGGCTGTTGTGTAC
AGCTGTGGAGCCAGAGTTGGATTCTTCCAAGGGGATATTCGGTTGCTGGCTGACGACATG
AAGACTTTGAAGCCCACATTGTTTCCCGCGGTGCCTCGACTCCTTAACAGGATCTACGAT
AAGGTACAAAATGAGGCCAAGACACCCTTGAAGAAGTTCTTGTTGAAGCTGGCTGTTTCC
AGTAAATTCAAAGAGCTTCAAAAGGGTATCATCAGGCATGATAGTTTCTGGGACAAGCTC
ATCTTTGCAAAGATCCAGGACAGCCTGGGCGGAAGGGTTCGTGTAATTGTCACTGGAGCT
GCCCCCATGTCCACTTCAGTCATGACATTCTTCCGGGCAGCAATGGGATGTCAGGTGTAT
GAAGCTTATGGTCAAACAGAATGCACAGGTGGCTGTACATTTACATTACCTGGGGACTGG
ACATCAGGTCACGTTGGGGTGCCCCTGGCTTGCAATTACGTGAAGCTGGAAGATGTGGCT
GACATGAACTACTTTACAGTGAATAATGAAGGAGAGGTCTGCATCAAGGGTACAAACGTG
TTCAAAGGATACCTGAAGGACCCTGAGAAGACACAGGAAGCCCTGGACAGTGATGGCTGG
CTTCACACAGGAGACATTGGTCGCTGGCTCCCGAATGGAACTCTGAAGATCATCGACCGT
AAAAAGAACATTTTCAAGCTGGCCCAAGGAGAATACATTGCACCAGAGAAGATAGAAAAT
ATCTACAACAGGAGTCAACCAGTGTTACAAATTTTTGTACACGGGGAGAGCTTACGGTCA
TCCTTAGTAGGAGTGGTGGTTCCTGACACAGATGTACTTCCCTCATTTGCAGCCAAGCTT
GGGGTGAAGGGCTCCTTTGAGGAACTGTGCCAAAACCAAGTTGTAAGGGAAGCCATTTTA
GAAGACTTGCAGAAAATTGGGAAAGAAAGTGGCCTTAAAACTTTTGAACAGGTCAAAGCC
ATTTTTCTTCATCCAGAGCCATTTTCCATTGAAAATGGGCTCTTGACACCAACATTGAAA
GCAAAGCGAGGAGAGCTTTCCAAATACTTTCGGACCCAAATTGACAGCCTGTATGAGCAC
ATCCAGGATTAG
Enzyme 38 GenBank Gene ID AB033899 Link Image
Enzyme 38 GeneCard ID ACSL5 Link Image
Enzyme 38 GenAtlas ID ACSL5 Link Image
Enzyme 38 HGNC ID HGNC:16526 Link Image
Enzyme 38 Chromosome Location 10
Enzyme 38 Locus 10q25.1-q25.2
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 5919
Enzyme 39 Name Long-chain-fatty-acid--CoA ligase 3
Enzyme 39 Synonyms
  1. Long-chain acyl-CoA synthetase 3
  2. LACS 3
Enzyme 39 Gene Name ACSL3
Enzyme 39 Protein Sequence >Long-chain-fatty-acid--CoA ligase 3
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV
NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN
GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF
MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK
PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS
HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ
SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI
SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES
AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY
KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA
LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK
VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
Enzyme 39 Number of Residues 720
Enzyme 39 Molecular Weight 80421
Enzyme 39 Theoretical pI 8.51
Enzyme 39 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 39 General Function Lipid transport and metabolism
Enzyme 39 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates
Enzyme 39 Pathways
Enzyme 39 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-31
Enzyme 39 Transmembrane Regions Not Available
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 4165018 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID O95573 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name ACSL3_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >2163 bp
ATGAATAACCACGTGTCTTCAAAACCATCTACCATGAAGCTAAAACATACCATCAACCCT
ATTCTTTTATATTTTATACATTTTCTAATATCACTTTATACTATTTTAACATACATTCCG
TTTTATTTTTTCTCCGAGTCAAGACAAGAAAAATCAAACCGAATTAAAGCAAAGCCTGTA
AATTCAAAACCTGATTCTGCATACAGATCTGTTAATAGTTTGGATGGTTTGGCTTCAGTA
TTATACCCTGGATGTGATACTTTAGATAAAGTTTTTACATATGCAAAAAACAAATTTAAG
AACAAAAGACTCTTGGGAACACGTGAAGTTTTAAATGAGGAAGATGAAGTACAACCAAAT
GGAAAAATTTTTAAAAAGGTTATTCTTGGACAGTATAATTGGCTTTCCTATGAAGATGTC
TTTGTTCGAGCCTTTAATTTTGGAAATGGATTACAGATGTTGGGTCAGAAACCAAAGACC
AACATCGCCATCTTCTGTGAGACCAGGGCCGAGTGGATGATAGCTGCACAGGCGTGTTTT
ATGTATAATTTTCAGCTTGTTACATTATATGCCACTCTAGGAGGTCCAGCCATTGTTCAT
GCATTAAATGAAACAGAGGTGACCAACATCATTACTAGTAAAGAACTCTTACAAACAAAG
TTGAAGGATATAGTTTCTTTGGTCCCACGCCTGCGGCACATCATCACTGTTGATGGAAAG
CCACCGACCTGGTCCGACTTCCCCAAGGGCATCATTGTGCATACCATGGCTGCAGTGGAG
GCCCTGGGAGCCAAGGCCAGCATGGAAAACCAACCTCATAGCAAACCATTGCCCTCAGAT
ATTGCAGTAATCATGTACACAAGTGGATCCACAGGACTTCCAAAGGGAGTCATGATCTCA
CATAGTAACATTATTGCTGGTATAACTGGGATGGCAGAAAGGATTCCAGAACTAGGAGAG
GAAGATGTCTACATTGGATATTTGCCTCTGGCCCATGTTCTAGAATTAAGTGCTGAGCTT
GTCTGTCTTTCTCACGGATGCCGCATTGGTTACTCTTCACCACAGACTTTAGCAGATCAG
TCTTCAAAAATTAAAAAAGGAAGCAAAGGGGATACATCCATGTTGAAACCAACACTGATG
GCAGCAGTTCCGGAAATCATGGATCGGATCTACAAAAATGTCATGAATAAAGTCAGTGAA
ATGAGTAGTTTTCAACGTAATCTGTTTATTCTGGCCTATAATTACAAAATGGAACAGATT
TCAAAAGGACGTAATACTCCACTGTGCGACAGCTTTGTTTTCCGGAAAGTTCGAAGCTTG
CTAGGGGGAAATATTCGTCTCCTGTTGTGTGGTGGCGCTCCACTTTCTGCAACCACGCAG
CGATTCATGAACATCTGTTTCTGCTGTCCTGTTGGTCAGGGATACGGGCTCACTGAATCT
GCTGGGGCTGGAACAATTTCCGAAGTGTGGGACTACAATACTGGCAGAGTGGGAGCACCA
TTAGTTTGCTGTGAAATCAAATTAAAAAACTGGGAGGAAGGTGGATACTTTAATACTGAT
AAGCCACACCCCAGGGGTGAAATTCTTATTGGGGGCCAAAGTGTGACAATGGGGTACTAC
AAAAATGAAGCAAAAACAAAAGCTGATTTCTCTGAAGATGAAAATGGACAAAGGTGGCTC
TGTACTGGGGATATTGGAGAGTTTGAACCCGATGGATGCTTAAAGATTATTGATCGTAAA
AAGGACCTTGTAAAACTACAGGCAGGGGAATATGTTTCTCTTGGGAAAGTAGAGGCAGCT
TTGAAGAATCTTCCACTAGTAGATAACATTTGTGCATATGCAAACAGTTATCATTCTTAT
GTCATTGGATTTGTTGTGCCAAATCAAAAGGAACTAACTGAACTAGCTCGAAAGAAAGGA
CTTAAAGGGACTTGGGAGGAGCTGTGTAACAGTTGTGAAATGGAAAATGAGGTACTTAAA
GTGCTTTCCGAAGCTGCTATTTCAGCAAGTCTGGAAAAGTTTGAAATTCCAGTAAAAATT
CGTTTGAGTCCTGAACCGTGGACCCCTGAAACTGGTCTGGTGACAGATGCCTTCAAGCTG
AAACGCAAAGAGCTTAAAACACATTACCAGGCGGACATTGAGCGAATGTATGGAAGAAAA
TAA
Enzyme 39 GenBank Gene ID D89053 Link Image
Enzyme 39 GeneCard ID ACSL3 Link Image
Enzyme 39 GenAtlas ID ACSL3 Link Image
Enzyme 39 HGNC ID HGNC:3570 Link Image
Enzyme 39 Chromosome Location 2
Enzyme 39 Locus 2q34-q35
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT: Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. Genomics. 1997 May 15;42(1):180-1. [PubMed Link Image]
  2. Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT: Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. Gene. 2001 Oct 31;278(1-2):185-92. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6170
Enzyme 40 Name Serine palmitoyltransferase 2
Enzyme 40 Synonyms
  1. Long chain base biosynthesis protein 2
  2. LCB 2
  3. Serine-palmitoyl-CoA transferase 2
  4. SPT 2
Enzyme 40 Gene Name SPTLC2
Enzyme 40 Protein Sequence >Serine palmitoyltransferase 2
MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFN
EAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFEN
FYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLG
FARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFA
TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQ
PRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVV
EYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQII
TSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIG
AFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYS
RHRLVPLLDRPFDETTYEETED
Enzyme 40 Number of Residues 562
Enzyme 40 Molecular Weight 62925
Enzyme 40 Theoretical pI 7.85
Enzyme 40 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 40 General Function Coenzyme transport and metabolism
Enzyme 40 Specific Function Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D- sphinganine + CO(2)
Enzyme 40 Pathways
Enzyme 40 Reactions
  • palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • 67-87
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 2564249 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID O15270 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name LCB2_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1689 bp
ATGCGGCCGGAGCCCGGAGGCTGCTGCTGCCGCCGCACGGTGCGGGCGAATGGCTGCGTG
GCGAACGGGGAAGTACGGAACGGGTACGTGAGGAGCAGCGCTGCAGCCGCAGCCGCAGCC
GCCGCCGGCCAGATCCATCATGTTACACAAAATGGAGGACTATATAAAAGACCGTTTAAT
GAAGCTTTTGAAGAAACACCAATGCTGGTTGCTGTGCTCACGTATGTGGGGTATGGCGTA
CTCACCCTCTTTGGATATCTTCGAGATTTCTTGAGGTATTGGAGAATTGAAAAGTGTCAC
CATGCAACAGAAAGAGAAGAACAAAAGGACTTTGTGTCATTGTATCAAGATTTTGAAAAC
TTTTATACAAGGAATCTGTACATGAGGATAAGAGACAACTGGAATCGGCCAATCTGTAGT
GTGCCTGGAGCCAGGGTGGACATCATGGAGAGACAGTCTCATGATTATAACTGGTCCTTC
AAGTATACAGGGAATATAATAAAGGGTGTTATAAACATGGGTTCCTACAACTATCTTGGA
TTTGCACGGAATACTGGATCATGTCAAGAAGCAGCCGCCAAAGTCCTTGAGGAGTATGGA
GCTGGAGTGTGCAGTACTCGGCAGGAAATTGGAAACCTGGACAAGCATGAAGAACTAGAG
GAGCTTGTAGCAAGGTTCTTAGGAGTAGAAGCTGCTATGGCGTATGGCATGGGATTTGCA
ACGAATTCAATGAACATTCCTGCTCTTGTTGGCAAAGGTTGCCTGATTCTGAGTGATGAA
CTGAACCATGCATCACTGGTTCTGGGAGCCAGACTGTCAGGAGCAACCATTAGAATCTTC
AAACACAACAATATGCAAAGCCTAGAGAAGCTATTGAAAGATGCCATTGTTTATGGTCAG
CCTCGGACACGAAGGCCCTGGAAGAAAATTCTCATCCTTGTGGAAGGAATATATAGCATG
GAGGGATCTATTGTTCGTCTTCCTGAAGTGATTGCCCTCAAGAAGAAATACAAGGCATAC
TTGTATCTGGATGAGGCTCACAGCATTGGCGCCCTGGGCCCCACAGGCCGGGGTGTGGTG
GAGTACTTTGGCCTGGATCCCGAGGATGTGGATGTTATGATGGGAACGTTCACAAAGAGT
TTTGGTGCTTCTGGAGGATATATTGGAGGCAAGAAGGAGCTGATAGACTACCTGCGAACA
CATTCTCATAGTGCAGTGTATGCCACGTCATTGTCACCTCCTGTAGTGGAGCAGATCATC
ACCTCCATGAAGTGCATCATGGGGCAGGATGGCACCAGCCTTGGTAAAGAGTGTGTACAA
CAGTTAGCTGAAAACACCAGGTATTTCAGGAGACGCCTGAAAGAGATGGGCTTCATCATC
TATGGAAATGAAGACTCTCCAGTAGTGCCTTTGATGCTCTACATGCCTGCCAAAATTGGC
GCCTTTGGACGGGAGATGCTGAAGCGGAACATCGGTGTCGTTGTGGTTGGATTTCCTGCC
ACCCCAATTATTGAGTCCAGAGCCAGGTTTTGCCTGTCAGCAGCTCATACCAAAGAAATA
CTTGATACTGCTTTAAAGGAGATAGATGAAGTTGGGGACCTATTGCAGCTGAAGTATTCC
CGTCATCGGTTGGTACCTCTACTGGACAGGCCCTTTGACGAGACGACGTATGAAGAAACA
GAAGACTGA
Enzyme 40 GenBank Gene ID Y08686 Link Image
Enzyme 40 GeneCard ID SPTLC2 Link Image
Enzyme 40 GenAtlas ID SPTLC2 Link Image
Enzyme 40 HGNC ID HGNC:11278 Link Image
Enzyme 40 Chromosome Location 14
Enzyme 40 Locus 14q24.3-q31
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  4. Nagiec MM, Lester RL, Dickson RC: Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase. Gene. 1996 Oct 24;177(1-2):237-41. [PubMed Link Image]
  5. Takeda J, Yano H, Eng S, Zeng Y, Bell GI: A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clones. Hum Mol Genet. 1993 Nov;2(11):1793-8. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6171
Enzyme 41 Name Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
Enzyme 41 Synonyms
  1. Succinyl-CoA synthetase subunit alpha
  2. SCS- alpha
Enzyme 41 Gene Name SUCLG1
Enzyme 41 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
MVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQ
QALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAI
EAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKK
GRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGII
LIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKE
KISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
Enzyme 41 Number of Residues 333
Enzyme 41 Molecular Weight 35048
Enzyme 41 Theoretical pI 9.24
Enzyme 41 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 41 General Function Energy production and conversion
Enzyme 41 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 41 Pathways
Enzyme 41 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • 1-19
Enzyme 41 Transmembrane Regions Not Available
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 9409794 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID P53597 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name SUCA_HUMAN Link Image
Enzyme 41 PDB ID 1EUC Link Image
Enzyme 41 PDB File Show
Enzyme 41 3D Structure
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1002 bp
ATGGTCTCCGGCAGCAGCGGCCTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTG
CCGCAGAATGGAATTCGGCATTGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGAT
AAAAATACAAAGATTATTTGCCAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAG
CAGGCATTGGAATATGGCACCAAACTCGTTGGAGGAACACTCCCAGGGAAAGGAGGCCAG
ACACATCTGGGCTTACCTGTCTTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCA
ACGGCTTCTGTCATTTATGTTCCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATT
GAGGCAGAAATTCCCTTGGTTGTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTA
CGAGTCAAGCACAAACTGCTGCGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCT
GGAGTCATCAATCCTGGAGAATGTAAAATTGGGATCATGCCTGGCCATATTCACAAAAAA
GGAAGGATTGGCATTGTGTCCAGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACA
ACGCAAGTTGGATTGGGGCAGTCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGA
ACAGATTTTATTGACTGCCTCGAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATA
TTGATTGGTGAAATTGGTGGTAATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACAT
AATTCAGGTCCAAATTCCAAGCCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCT
GGGAGAAGAATGGGTCATGCCGGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAG
AAGATCTCTGCCCTTCAGAGTGCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGA
ACCACGATCTACAAGGAATTTGAAAAGAGGAAGATGCTATGA
Enzyme 41 GenBank Gene ID AF104921 Link Image
Enzyme 41 GeneCard ID SUCLG1 Link Image
Enzyme 41 GenAtlas ID SUCLG1 Link Image
Enzyme 41 HGNC ID HGNC:11449 Link Image
Enzyme 41 Chromosome Location 2
Enzyme 41 Locus 2p11.2
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6173
Enzyme 42 Name Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
Enzyme 42 Synonyms
  1. Succinyl-CoA synthetase, betaG chain
  2. SCS-betaG
  3. GTP- specific succinyl-CoA synthetase subunit beta
Enzyme 42 Gene Name SUCLG2
Enzyme 42 Protein Sequence >Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK
Enzyme 42 Number of Residues 432
Enzyme 42 Molecular Weight 46511
Enzyme 42 Theoretical pI 6.18
Enzyme 42 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 42 General Function Energy production and conversion
Enzyme 42 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 42 Pathways
Enzyme 42 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • 1-29
Enzyme 42 Transmembrane Regions Not Available
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 133777003 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q96I99 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name SUCB2_HUMAN Link Image
Enzyme 42 PDB ID 1EUC Link Image
Enzyme 42 PDB File Show
Enzyme 42 3D Structure
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1155 bp
ATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTTGTAGCAGACACTGCAAATGAAGCT
CTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATTGTTTTAAAAGCCCAGATCTTAGCT
GGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTGAAAGGAGGTGTTCATTTAACAAAA
GACCCTAATGTTGTGGGACAGCTGGCTAAACAGATGATTGGGTACAATCTAGCGACAAAA
CAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTGATGGTTGCTGAAGCCTTGGATATT
TCCAGAGAAACCTACCTGGCAATTCTGATGGACCGGTCCTGCAATGGCCCCGTGCTGGTG
GGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTGGCTGCTTCAAACCCGGAGCTCATT
TTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAGGACAGCCAAGCTCAGCGGATGGCC
GAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAGGCTGCAGATCAAATTACGAAGCTG
TATAATCTCTTCCTGAAAATTGATGCTACTCAGGTGGAAGTGAATCCCTTTGGTGAAACT
CCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATAAACTTTGATGACAACGCAGAATTC
CGACAAAAAGACATATTTGCTATGGACGACAAATCAGAGAATGAGCCCATTGAAAATGAA
GCTGCCAAATATGATCTAAAATACATAGGACTAGATGGGAACATTGCCTGCTTTGTGAAT
GGTGCTGGGCTCGCCATGGCTACTTGTGATATCATTTTCCTTAATGGTGGGAAGCCAGCC
AACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCTCAAGTATATCAAGCATTCAAATTG
CTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTCAATATATTTGGTGGTATCGTCAAC
TGTGCCATCATTGCCAATGGGATCACCAAAGCCTGCCGGGAGCTAGAACTCAAGGTGCCC
CTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAGGCCCAGAAGATACTCAACAACAGC
GGACTCCCCATTACTTCAGCCATTGACCTGGAGGATGCAGCCAAGAAGGCTGTGGCCAGT
GTGGCCAAGAAGTGA
Enzyme 42 GenBank Gene ID BC007716 Link Image
Enzyme 42 GeneCard ID SUCLG2 Link Image
Enzyme 42 GenAtlas ID SUCLG2 Link Image
Enzyme 42 HGNC ID HGNC:11450 Link Image
Enzyme 42 Chromosome Location 3
Enzyme 42 Locus 3p14.1
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6198
Enzyme 43 Name 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Enzyme 43 Synonyms
  1. HMG-CoA reductase
Enzyme 43 Gene Name HMGCR
Enzyme 43 Protein Sequence >3-hydroxy-3-methylglutaryl-coenzyme A reductase
MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSS
DIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTG
LNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIG
VGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFAR
VLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKR
IEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVT
QKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNS
SLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK
LETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGV
AGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC
DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMI
SKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV
LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITL
MEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR
IVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA
Enzyme 43 Number of Residues 888
Enzyme 43 Molecular Weight 97477
Enzyme 43 Theoretical pI 6.72
Enzyme 43 GO Classification
Function
  • catalytic activity
  • hydroxymethylglutaryl-CoA reductase (NADPH) activity
  • hydroxymethylglutaryl-CoA reductase (NADPH) activity
  • hydroxymethylglutaryl-CoA reductase (NADPH) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • biosynthesis
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 43 General Function Lipid transport and metabolism
Enzyme 43 Specific Function This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of sterol biosynthesis
Enzyme 43 Pathways
Enzyme 43 Reactions
  • (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • 1-23
Enzyme 43 Transmembrane Regions Not Available
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 306865 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P04035 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name HMDH_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >2667 bp
ATGTTGTCAAGACTTTTTCGAATGCATGGCCTCTTTGTGGCCTCCCATCCCTGGGAAGTC
ATAGTGGGGACAGTGACACTGACCATCTGCATGATGTCCATGAACATGTTTACTGGTAAC
AATAAGATCTGTGGTTGGAATTATGAATGTCCAAAGTTTGAAGAGGATGTTTTGAGCAGT
GACATTATAATTCTGACAATAACACGATGCATAGCCATCCTGTATATTTACTTCCAGTTC
CAGAATTTACGTCAACTTGGATCAAAATATATTTTGGGTATTGCTGGCCTTTTCACAATT
TTCTCAAGTTTTGTATTCAGTACAGTTGTCATTCACTTCTTAGACAAAGAATTGACAGGC
TTGAATGAAGCTTTGCCCTTTTTCCTACTTTTGATTGACCTTTCCAGAGCAAGCACATTA
GCAAAGTTTGCCCTCAGTTCCAACTCACAGGATGAAGTAAGGGAAAATATTGCTCGTGGA
ATGGCAATTTTAGGTCCTACGTTTACCCTCGATGCTCTTGTTGAATGTCTTGTGATTGGA
GTTGGTACCATGTCAGGGGTACGTCAGCTTGAAATTATGTGCTGCTTTGGCTGCATGTCA
GTTCTTGCCAACTACTTCGTGTTCATGACTTTCTTCCCAGCTTGTGTGTCCTTGGTATTA
GAGCTTTCTCGGGAAAGCCGCGAGGGTCGTCCAATTTGGCAGCTCAGCCATTTTGCCCGA
GTTTTAGAAGAAGAAGAAAATAAGCCGAATCCTGTAACTCAGAGGGTCAAGATGATTATG
TCTCTAGGCTTGGTTCTTGTTCATGCTCACAGTCGCTGGATAGCTGATCCTTCTCCTCAA
AACAGTACAGCAGATACTTCTAAGGTTTCATTAGGACTGGATGAAAATGTGTCCAAGAGA
ATTGAACCAAGTGTTTCCCTCTGGCAGTTTTATCTCTCTAAAATGATCAGCATGGATATT
GAACAAGTTATTACCCTAAGTTTAGCTCTCCTTCTGGCTGTCAAGTACATCTTCTTTGAA
CAAACAGAGACAGAATCTACACTCTCATTAAAAAACCCTATCACATCTCCTGTAGTGACA
CAAAAGAAAGTCCCAGACAATTGTTGTAGACGTGAACCTATGCTGGTCAGAAATAACCAG
AAATGTGATTCAGTAGAGGAAGAGACAGGGATAAACCGAGAAAGAAAAGTTGAGGTTATA
AAACCCTTAGTGGCTGAAACAGATACCCCAAACAGAGCTACATTTGTGGTTGGTAACTCC
TCCTTACTCGATACTTCATCAGTACTGGTGACACAGGAACCTGAAATTGAACTTCCCAGG
GAACCTCGGCCTAATGAAGAATGTCTACAGATACTTGGGAATGCAGAGAAAGGTGCAAAA
TTCCTTAGTGATGCTGAGATCATCCAGTTAGTCAATGCTAAGCATATCCCAGCCTACAAG
TTGGAAACTCTGATGGAAACTCATGAGCGTGGTGTATCTATTCGCCGACAGTTACTTTCC
AAGAAGCTTTCAGAACCTTCTTCTCTCCAGTACCTACCTTACAGGGATTATAATTACTCC
TTGGTGATGGGAGCTTGTTGTGAGAATGTTATTGGATATATGCCCATCCCTGTTGGAGTG
GCAGGACCCCTTTGCTTAGATGAAAAAGAATTTCAGGTTCCAATGGCAACAACAGAAGGT
TGTCTTGTGGCCAGCACCAATAGAGGCTGCAGAGCAATAGGTCTTGGTGGAGGTGCCAGC
AGCCGAGTCCTTGCAGATGGGATGACTCGTGGCCCAGTTGTGCGTCTTCCACGTGCTTGT
GACTCTGCAGAAGTGAAAGCCTGGCTCGAAACATCTGAAGGGTTCGCAGTGATAAAGGAG
GCATTTGACAGCACTAGCAGATTTGCACGTCTACAGAAACTTCATACAAGTATAGCTGGA
CGCAACCTTTATATCCGTTTCCAGTCCAGGTCAGGGGATGCCATGGGGATGAACATGATT
TCAAAGGGTACAGAGAAAGCACTTTCAAAACTTCACGAGTATTTCCCTGAAATGCAGATT
CTAGCCGTTAGTGGTAACTATTGTACTGACAAGAAACCTGCTGCTATAAATTGGATAGAG
GGAAGAGGAAAATCTGTTGTTTGTGAAGCTGTCATTCCAGCCAAGGTTGTCAGAGAAGTA
TTAAAGACTACCACAGAGGCTATGATTGAGGTCAACATTAACAAGAATTTAGTGGGCTCT
GCCATGGCTGGGAGCATAGGAGGCTACAACGCCCATGCAGCAAACATTGTCACCGCCATC
TACATTGCCTGTGGACAGGATGCAGCACAGAATGTTGGTAGTTCAAACTGTATTACTTTA
ATGGAAGCAAGTGGTCCCACAAATGAAGATTTATATATCAGCTGCACCATGCCATCTATA
GAGATAGGAACGGTGGGTGGTGGGACCAACCTACTACCTCAGCAAGCCTGTTTGCAGATG
CTAGGTGTTCAAGGAGCATGCAAAGATAATCCTGGGGAAAATGCCCGGCAGCTTGCCCGA
ATTGTGTGTGGGACCGTAATGGCTGGGGAATTGTCACTTATGGCAGCATTGGCAGCAGGA
CATCTTGTCAAAAGTCACATGATTCACAACAGGTCGAAGATCAATTTACAAGACCTCCAA
GGAGCTTGCACCAAGAAGACAGCCTGA
Enzyme 43 GenBank Gene ID M11058 Link Image
Enzyme 43 GeneCard ID HMGCR Link Image
Enzyme 43 GenAtlas ID HMGCR Link Image
Enzyme 43 HGNC ID HGNC:5006 Link Image
Enzyme 43 Chromosome Location 5
Enzyme 43 Locus 5q13.3-q14
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Luskey KL, Stevens B: Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. J Biol Chem. 1985 Aug 25;260(18):10271-7. [PubMed Link Image]
  2. Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J: Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 2000 Mar 1;19(5):819-30. [PubMed Link Image]
  3. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6335
Enzyme 44 Name Cytosolic acyl coenzyme A thioester hydrolase
Enzyme 44 Synonyms
  1. Long chain acyl-CoA thioester hydrolase
  2. CTE-II
  3. CTE-IIa
  4. Brain acyl-CoA hydrolase
  5. Acyl-CoA thioesterase 7
Enzyme 44 Gene Name ACOT7
Enzyme 44 Protein Sequence >Cytosolic acyl coenzyme A thioester hydrolase
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
Enzyme 44 Number of Residues 380
Enzyme 44 Molecular Weight 41797
Enzyme 44 Theoretical pI 8.66
Enzyme 44 GO Classification
Function
  • catalytic activity
Process
Component
Enzyme 44 General Function Lipid transport and metabolism
Enzyme 44 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • 1-19
Enzyme 44 Transmembrane Regions Not Available
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 2780414 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID O00154 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name BACH_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1017 bp
ATGTCGGGCCCAGACGTCGAGACGCCGTCCGCCATCCAGATCTGCCGGATCATGCGGCCA
GATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATCGAGGAG
GCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGTGTGGCC
GCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAGGTGGCG
CATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTCAACGTG
ATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTGTGGTAT
GTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTGTATTCC
CGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAGCGCATG
GAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCGAACACT
GTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACCCTGCAC
GGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATCGTGGCT
GCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTTCATGAC
AAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGCAATAAG
TCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAGAAGCGC
TACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGGTCGCTG
CCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAAGGCAAA
GGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCCTAG
Enzyme 44 GenBank Gene ID D88894 Link Image
Enzyme 44 GeneCard ID ACOT7 Link Image
Enzyme 44 GenAtlas ID ACOT7 Link Image
Enzyme 44 HGNC ID HGNC:24157 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 1p36.31-p36.11
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J Biochem (Tokyo). 1999 Dec;126(6):1013-9. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 6336
Enzyme 45 Name Acyl-coenzyme A thioesterase 2
Enzyme 45 Synonyms
  1. Acyl-CoA thioesterase 2
  2. Peroxisomal acyl-coenzyme A thioester hydrolase 2a
  3. Peroxisomal long-chain acyl-coA thioesterase 2
  4. ZAP128
  5. CTE-Ia
Enzyme 45 Gene Name ACOT2
Enzyme 45 Protein Sequence >Acyl-coenzyme A thioesterase 2
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGREGTIP
SKV
Enzyme 45 Number of Residues 483
Enzyme 45 Molecular Weight 53257
Enzyme 45 Theoretical pI 8.93
Enzyme 45 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 45 General Function Not Available
Enzyme 45 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 887376 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P49753 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name ACOT2_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >937 bp
CCCCCGGGCTGCAGGAATTCCTGAATTCAAAATGGCCTCATCTCCTGCTGTCCTTCGAGC
GTCCCGGCTGTACCAATGGAGCCTGAAGAGTTCGGCGCAGTTCCTGGGGTCTCCACAGCT
GAGGCAGAACCTGGGCCCTTTCCTGGGATTGTGGACATGTTCGGGAACTGGAGGTGGCCT
GCTGGAGTATCGGGCTAGTCTGCTGGCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTA
TTATAACTATGAAGACCTCCCCAAGACCATGGAGACGCTCCATCTGGAGTACTTTGAAGA
AGCCATGAACTACTTGCTCAGTCATCCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGG
AATTTCCAAAGGGGGTGAGCTCTGCCTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGC
TGCTGTCGTCATCAACGGCTCTGTGGCCAATGTTGGGGGAACCTTACACTACAAGGGCGA
GACCCTGCCCCCTGTGGGCGTCAACAGAAATCGCATCAAGGTGACCAAAGATGGCTATGC
AGACATTGTGGATGTCCTGAACAGCCCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCC
TGTGGAAAGGGCAGAGAGCACCTTCCTGTTCCTGGTAGGTCAGGATGACCACAACTGGAA
GAGTGAGTTCTATGCTAATGAGGCCTGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCC
CCAGATCATCTGTTACCCAGAGACAGGGCACTATATTGAGCCTCCTTACTTCCCCCTGTG
TCGGGCTTCCCTGCATGCCTTGGTGGGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGC
TCATGCCATGGCTCAGGTGGATGCTTGGAAACAACTCCAGACTTTCTTCCACAAACACTT
GGGTGGCCACGAGGGGACAATCCCATCAAAAGTGTAA
Enzyme 45 GenBank Gene ID L40401 Link Image
Enzyme 45 GeneCard ID ACOT2 Link Image
Enzyme 45 GenAtlas ID ACOT2 Link Image
Enzyme 45 HGNC ID HGNC:18431 Link Image
Enzyme 45 Chromosome Location 14
Enzyme 45 Locus 14q24.3
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed Link Image]
  2. Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 6338
Enzyme 46 Name Acyl-coenzyme A thioesterase 8
Enzyme 46 Synonyms
  1. Choloyl-coenzyme A thioesterase
  2. Acyl-CoA thioesterase 8
  3. Peroxisomal acyl-coenzyme A thioester hydrolase 1
  4. PTE-1
  5. Peroxisomal long-chain acyl-coA thioesterase 1
  6. HIV-Nef-associated acyl coA thioesterase
  7. Thioesterase II
  8. hTE
  9. hACTEIII
  10. hACTE-III
  11. PTE-2
Enzyme 46 Gene Name ACOT8
Enzyme 46 Protein Sequence >Acyl-coenzyme A thioesterase 8
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
Enzyme 46 Number of Residues 319
Enzyme 46 Molecular Weight 35915
Enzyme 46 Theoretical pI 7.60
Enzyme 46 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolism
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
Enzyme 46 General Function Lipid transport and metabolism
Enzyme 46 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA:amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 2318125 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID O14734 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name ACOT8_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >960 bp
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
Enzyme 46 GenBank Gene ID AF014404 Link Image
Enzyme 46 GeneCard ID ACOT8 Link Image
Enzyme 46 GenAtlas ID ACOT8 Link Image
Enzyme 46 HGNC ID HGNC:15919 Link Image
Enzyme 46 Chromosome Location 20
Enzyme 46 Locus 20q13.12
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Watanabe H, Shiratori T, Shoji H, Miyatake S, Okazaki Y, Ikuta K, Sato T, Saito T: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem Biophys Res Commun. 1997 Sep 8;238(1):234-9. [PubMed Link Image]
  2. Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed Link Image]
  3. Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem. 1999 Apr 2;274(14):9216-23. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 6339
Enzyme 47 Name Palmitoyl-protein thioesterase 1 precursor
Enzyme 47 Synonyms
  1. PPT-1
  2. Palmitoyl-protein hydrolase 1
Enzyme 47 Gene Name PPT1
Enzyme 47 Protein Sequence >Palmitoyl-protein thioesterase 1 precursor
MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEK
KIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQF
LRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERL
VQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVD
SEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAH
IIPFLG
Enzyme 47 Number of Residues 306
Enzyme 47 Molecular Weight 34194
Enzyme 47 Theoretical pI 6.50
Enzyme 47 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-(protein) hydrolase activity
  • thiolester hydrolase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
Component
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions
  • palmitoyl[protein] + H2O = palmitate + protein
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • 1-27
Enzyme 47 Transmembrane Regions Not Available
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 1160967 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P50897 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name PPT1_HUMAN Link Image
Enzyme 47 PDB ID 1EXW Link Image
Enzyme 47 PDB File Show
Enzyme 47 3D Structure
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >921 bp
ATGGCGTCGCCCGGCTGCCTGTGGCTCTTGGCTGTGGCTCTCCTGCCATGGACCTGCGCT
TCTCGGGCGCTGCAGCATCTGGACCCGCCGGCGCCGCTGCCGTTGGTGATCTGGCATGGG
ATGGGAGACAGCTGTTGCAATCCCTTAAGCATGGGTGCTATTAAAAAAATGGTGGAGAAG
AAAATACCTGGAATTTACGTCTTATCTTTAGAGATTGGGAAGACCCTGATGGAGGACGTG
GAGAACAGCTTCTTCTTGAATGTCAATTCCCAAGTAACAACAGTGTGTCAGGCACTTGCT
AAGGATCCTAAATTGCAGCAAGGCTACAATGCTATGGGATTCTCCCAGGGAGGCCAATTT
CTGAGGGCAGTGGCTCAGAGATGCCCTTCACCTCCCATGATCAATCTGATCTCGGTTGGG
GGACAACATCAAGGTGTTTTTGGACTCCCTCGATGCCCAGGAGAGAGCTCTCACATCTGT
GACTTCATCCGAAAAACACTGAATGCTGGGGCGTACTCCAAAGTTGTTCAGGAACGCCTC
GTGCAAGCCGAATACTGGCATGACCCCATAAAGGAGGATGTGTATCGCAACCACAGCATC
TTCTTGGCAGATATAAATCAGGAGCGGGGTATCAATGAGTCCTACAAGAAAAACCTGATG
GCCCTGAAGAAGTTTGTGATGGTGAAATTCCTCAATGATTCCATTGTGGACCCTGTAGAT
TCGGAGTGGTTTGGATTTTACAGAAGTGGCCAAGCCAAGGAAACCATTCCCTTACAGGAG
ACCTCCCTGTACACACAGGACCGCCTGGGGCTAAAGGAAATGGACAATGCAGGACAGCTA
GTGTTTCTGGCTACAGAAGGGGACCATCTTCAGTTGTCTGAAGAATGGTTTTATGCCCAC
ATCATACCATTCCTTGGATGA
Enzyme 47 GenBank Gene ID L42809 Link Image
Enzyme 47 GeneCard ID PPT1 Link Image
Enzyme 47 GenAtlas ID PPT1 Link Image
Enzyme 47 HGNC ID HGNC:9325 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 1p32
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L: Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature. 1995 Aug 17;376(6541):584-7. [PubMed Link Image]
  2. Crews CM, Lane WS, Schreiber SL: Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4316-9. [PubMed Link Image]
  3. Schriner JE, Yi W, Hofmann SL: cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis. Genomics. 1996 Jun 15;34(3):317-22. [PubMed Link Image]
  4. Lu JY, Verkruyse LA, Hofmann SL: Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10046-50. [PubMed Link Image]
  5. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  6. Mitchison HM, Hofmann SL, Becerra CH, Munroe PB, Lake BD, Crow YJ, Stephenson JB, Williams RE, Hofman IL, Taschner PE, Martin JJ, Philippart M, Andermann E, Andermann F, Mole SE, Gardiner RM, O'Rawe AM: Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing juvenile neuronal ceroid lipofuscinosis with granular osmiophilic deposits. Hum Mol Genet. 1998 Feb;7(2):291-7. [PubMed Link Image]
  7. Das AK, Becerra CH, Yi W, Lu JY, Siakotos AN, Wisniewski KE, Hofmann SL: Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S. J Clin Invest. 1998 Jul 15;102(2):361-70. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 6839
Enzyme 48 Name Dihydroxyacetone phosphate acyltransferase
Enzyme 48 Synonyms
  1. DHAP-AT
  2. DAP-AT
  3. Glycerone-phosphate O-acyltransferase
  4. Acyl- CoA:dihydroxyacetonephosphateacyltransferase
Enzyme 48 Gene Name GNPAT
Enzyme 48 Protein Sequence >Dihydroxyacetone phosphate acyltransferase
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVY
KGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIR
FCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDL
PVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEF
FLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGV
PKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSE
DMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFG
GFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSA
YRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGC
YLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQY
LAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATT
KLEEMLGCKTPIGKPATAKL
Enzyme 48 Number of Residues 680
Enzyme 48 Molecular Weight 77189
Enzyme 48 Theoretical pI 6.52
Enzyme 48 GO Classification
Function
  • O-acetyltransferase activity
  • O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycerone-phosphate O-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • biosynthesis
  • cellular lipid metabolism
  • ether lipid biosynthesis
  • glycerolipid biosynthesis
  • lipid biosynthesis
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
  • microbody membrane
  • organelle membrane
  • peroxisomal membrane
Enzyme 48 General Function Lipid transport and metabolism
Enzyme 48 Specific Function Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Enzyme 48 Pathways
Enzyme 48 Reactions
  • acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 2584769 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID O15228 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name GNPAT_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >2043 bp
ATGGAGTCTTCCAGTTCATCTAACTCTTATTTCTCCGTTGGCCCAACCAGTCCCAGCGCT
GTCGTGCTCCTCTACTCGAAGGAGCTCAAAAAGTGGGATGAGTTTGAAGATATTTTAGAA
GAGAGGAGGCATGTCAGTGACTTGAAATTTGCAATGAAATGCTACACACCTCTTGTCTAT
AAGGGAATTACTCCATGTAAACCAATTGATATTAAATGTAGTGTTCTCAATTCTGAGGAG
ATTCATTATGTCATTAAACAGCTTTCCAAGGAATCCCTTCAATCTGTGGATGTCCTCCGA
GAGGAAGTGAGTGAGATCTTAGATGAAATGAGTCACAAACTGCGTCTTGGAGCCATTCGG
TTTTGTGCCTTCACCCTGAGCAAAGTATTTAAACAAATTTTCTCGAAGGTGTGTGTAAAT
GAAGAAGGTATTCAGAAACTACAAAGAGCCATCCAGGAGCATCCTGTTGTTCTGCTGCCT
AGTCATCGAAGTTACATTGACTTCCTCATGTTGTCTTTTCTTCTATACAATTATGATTTG
CCTGTGCCAGTTATAGCAGCAGGAATGGACTTCCTGGGAATGAAAATGGTTGGTGAGCTG
CTACGAATGTCGGGTGCCTTTTTCATGCGGCGTACCTTTGGTGGCAATAAACTCTACTGG
GCTGTATTCTCTGAATATGTAAAAACTATGTTACGGAATGGTTATGCTCCTGTTGAATTT
TTCCTCGAAGGGACAAGAAGCCGCTCTGCCAAGACATTGACTCCTAAATTTGGTCTTCTG
AATATTGTGATGGAGCCATTTTTTAAAAGAGAAGTTTTTGATACCTACCTTGTCCCAATT
AGTATCAGTTATGATAAGATCTTGGAAGAAACTCTTTATGTGTATGAGCTTCTAGGGGTT
CCTAAACCAAAAGAGTCTACAACTGGGTTGCTGAAAGCCAGAAAGATTCTCTCTGAAAAT
TTTGGAAGCATCCATGTGTACTTTGGAGATCCTGTGTCACTTCGATCTTTGGCAGCTGGG
AGGATGAGTCGGAGCTCATATAACTTGGTTCCAAGATACATTCCTCAGAAACAGTCTGAG
GACATGCATGCCTTTGTCACTGAAGTTGCCTACAAAATGGAGCTTCTGCAAATTGAAAAC
ATGGTTTTGAGCCCCTGGACCCTAATAGTTGCTGTTCTGCTTCAGAACCGGCCATCCATG
GACTTTGATGCTCTGGTGGAAAAGACTTTATGGCTAAAAGGCTTAACCCAGGCATTTGGA
GGGTTTCTCATTTGGCCTGATAATAAACCTGCTGAAGAAGTTGTCCCGGCCAGCATTCTT
CTGCATTCCAACATTGCCAGCCTTGTCAAAGACCAGGTGATTCTGAAAGTGGACTCCGGA
GACTCGGAAGTGGTCGATGGGCTTATGCTCCAGCACATCACTCTCCTCATGTGCTCAGCT
TATAGGAACCAGCTGCTCAACATTTTTGTGCGCCCATCCTTAGTAGCAGTAGCATTGCAG
ATGACACCAGGGTTCAGGAAAGAGGATGTCTACAGTTGCTTTCGCTTCCTACGTGATGTT
TTTGCAGATGAGTTCATCTTCCTTCCAGGAAACACACTAAAGGACTTTGAAGAAGGCTGT
TACCTGCTTTGTAAAAGTGAAGCCATACAAGTGACTACGAAAGACATCCTAGTTACAGAG
AAAGGAAATACTGTGTTAGAATTTTTAGTAGGACTCTTTAAACCTTTTGTGGAAAGCTAT
CAGATAATTTGCAAGTACCTTTTGAGTGAAGAAGAGGACCACTTCAGTGAGGAACAGTAC
TTGGCTGCAGTCAGAAAATTCACAAGTCAGCTTCTCGATCAAGGTACCTCTCAATGTTAT
GATGTATTATCTTCTGATGTGCAGAAAAACGCCTTAGCAGCCTGTGTGAGGCTCGGAGTA
GTGGAGAAGAAGAAGATAAATAATAACTGTATATTTAATGTGAATGAACCTGCCACAACC
AAATTAGAAGAAATGCTTGGTTGTAAGACACCAATAGGAAAACCAGCCACTGCAAAACTT
TAA
Enzyme 48 GenBank Gene ID AJ002190 Link Image
Enzyme 48 GeneCard ID GNPAT Link Image
Enzyme 48 GenAtlas ID GNPAT Link Image
Enzyme 48 HGNC ID HGNC:4416 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 1q42.11-42.3
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Thai TP, Heid H, Rackwitz HR, Hunziker A, Gorgas K, Just WW: Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase. FEBS Lett. 1997 Dec 29;420(2-3):205-11. [PubMed Link Image]
  2. Ofman R, Hettema EH, Hogenhout EM, Caruso U, Muijsers AO, Wanders RJ: Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2. Hum Mol Genet. 1998 May;7(5):847-53. [PubMed Link Image]
  3. Ofman R, Lajmir S, Wanders RJ: Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations. Biochem Biophys Res Commun. 2001 Mar 2;281(3):754-60. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 6873
Enzyme 49 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Enzyme 49 Synonyms
  1. 1- AGP acyltransferase 3
  2. 1-AGPAT 3
  3. Lysophosphatidic acid acyltransferase gamma
  4. LPAAT-gamma
  5. 1-acylglycerol-3-phosphate O- acyltransferase 3
Enzyme 49 Gene Name AGPAT3
Enzyme 49 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ
LVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKV
LAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRF
TETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFK
PARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTE
IEKGSSYGNQEFKKKE
Enzyme 49 Number of Residues 376
Enzyme 49 Molecular Weight 43381
Enzyme 49 Theoretical pI 8.91
Enzyme 49 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 49 General Function Lipid transport and metabolism
Enzyme 49 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 49 Pathways
Enzyme 49 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • 1-25
Enzyme 49 Transmembrane Regions Not Available
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 8886001 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q9NRZ7 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name PLCC_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1131 bp
ATGGGCCTGCTGGCCTTCCTGAAGACCCAGTTCGTGCTGCACCTGCTGGTCGGCTTTGTC
TTCGTGGTGAGTGGTCTGGTCATCAACTTCGTCCAGCTGTGCACGCTGGCGCTCTGGCCG
GTCAGCAAGCAGCTCTACCGCCGCCTCAACTGCCGCCTCGCATACTCACTCTGGAGCCAA
CTGGTCATGCTGCTGGAGTGGTGGTCCTGCACGGAGTGTACACTGTTCACGGACCAGGCC
ACGGTAGAGCGCTTTGGGAAGGAGCACGCAGTCATCATCCTCAACCACAACTTCGAGATC
GACTTCCTCTGTGGGTGGACCATGTGTGAGCGCTTCGGAGTGCTGGGGAGCTCCAAGGTC
CTCGCTAAGAAGGAGCTGCTCTACGTGCCCCTCATCGGCTGGACGTGGTACTTTCTGGAG
ATTGTGTTCTGCAAGCGGAAGTGGGAGGAGGACCGGGACACCGTGGTCGAAGGGCTGAGG
CGCCTGTCGGACTACCCCGAGTACATGTGGTTTCTCCTGTACTGCGAGGGGACGCGCTTC
ACGGAGACCAAGCACCGCGTTAGCATGGAGGTGGCGGCTGCTAAGGGGCTTCCTGTCCTC
AAGTACCACCTGCTGCCGCGGACCAAGGGCTTCACCACCGCAGTCAAGTGCCTCCGGGGG
ACAGTCGCAGCTGTCTATGATGTAACCCTGAACTTCAGAGGAAACAAGAACCCGTCCCTG
CTGGGGATCCTCTACGGGAAGAAGTACGAGGCGGACATGTGCGTGAGGAGATTTCCTCTG
GAAGACATCCCGCTGGATGAAAAGGAAGCAGCTCAGTGGCTTCATAAACTGTACCAGGAG
AAGGACGCGCTCCAGGAGATATATAATCAGAAGGGCATGTTTCCAGGGGAGCAGTTTAAG
CCTGCCCGGAGGCCGTGGACCCTCCTGAACTTCCTGTCCTGGGCCACCATTCTCCTGTCT
CCCCTCTTCAGTTTTGTCTTGGGCGTCTTTGCCAGCGGATCACCTCTCCTGATCCTGACT
TTCTTGGGGTTTGTGGGAGCAGCTTCCTTTGGAGTTCGCAGACTGATAGGAGTAACTGAG
ATAGAAAAAGGCTCCAGCTACGGAAACCAAGAGTTTAAGAAAAAGGAATAA
Enzyme 49 GenBank Gene ID AF156774 Link Image
Enzyme 49 GeneCard ID AGPAT3 Link Image
Enzyme 49 GenAtlas ID AGPAT3 Link Image
Enzyme 49 HGNC ID HGNC:326 Link Image
Enzyme 49 Chromosome Location Not Available
Enzyme 49 Locus Not Available
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 6875
Enzyme 50 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
Enzyme 50 Synonyms
  1. 1- AGP acyltransferase 2
  2. 1-AGPAT 2
  3. Lysophosphatidic acid acyltransferase beta
  4. LPAAT-beta
  5. 1-acylglycerol-3-phosphate O- acyltransferase 2
Enzyme 50 Gene Name AGPAT2
Enzyme 50 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase beta
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENM
SIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAK
RELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGD
LLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAAD
VPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
Enzyme 50 Number of Residues 278
Enzyme 50 Molecular Weight 30915
Enzyme 50 Theoretical pI 9.22
Enzyme 50 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 50 General Function Lipid transport and metabolism
Enzyme 50 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 50 Pathways
Enzyme 50 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • 1-23
Enzyme 50 Transmembrane Regions Not Available
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 2282590 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID O15120 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name PLCB_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >837 bp
ATGGAGCTGTGGCCGTGTCTGGCCGCGGCGCTGCTGTTGCTGCTGCTGCTGGTGCAGCTG
AGCCGCGCGGCCGAGTTCTACGCCAAGGTCGCCCTGTACTGCGCGCTGTGCTTCACGGTG
TCCGCCGTGGCCTCGCTCGTCTGCCTGCTGCGCCACGGCGGCCGGACGGTGGAGAACATG
AGCATCATCGGCTGGTTCGTGCGAAGCTTCAAGTACTTTTACGGGCTCCGCTTCGAGGTG
CGGGACCCGCGCAGGCTGCAGGAGGCCCGTCCCTGTGTCATCGTCTCCAACCACCAGAGC
ATCCTGGACATGATGGGCCTCATGGAGGTCCTTCCGGAGCGCTGCGTGCAGATCGCCAAG
CGGGAGCTGCTCTTCCTGGGGCCCGTGGGCCTCATCATGTACCTCGGGGGCGTCTTCTTC
ATCAACCGGCAGCGCTCTAGCACTGCCATGACAGTGATGGCCGACCTGGGCGAGCGCATG
GTCAGGGAGAACCTCAAAGTGTGGATCTATCCCGAGGGTACTCGCAACGACAATGGGGAC
CTGCTGCCTTTTAAGAAGGGCGCCTTCTACCTGGCAGTCCAGGCACAGGTGCCCATCGTC
CCCGTGGTGTACTCTTCCTTCTCCTCCTTCTACAACACCAAGAAGAAGTTCTTCACTTCA
GGAACAGTCACAGTGCAGGTGCTGGAAGCCATCCCCACCAGCGGCCTCACTGCGGCGGAC
GTCCCTGCGCTCGTGGACACCTGCCACCGGGCCATGAGGACCACCTTCCTCCACATCTCC
AAGACCCCCCAGGAGAACGGGGCCACTGCGGGGTCTGGCGTGCAGCCGGCCCAGTAG
Enzyme 50 GenBank Gene ID AF000237 Link Image
Enzyme 50 GeneCard ID AGPAT2 Link Image
Enzyme 50 GenAtlas ID AGPAT2 Link Image
Enzyme 50 HGNC ID HGNC:325 Link Image
Enzyme 50 Chromosome Location 9
Enzyme 50 Locus 9q34.3
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Eberhardt C, Gray PW, Tjoelker LW: Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3. J Biol Chem. 1997 Aug 8;272(32):20299-305. [PubMed Link Image]
  2. Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed Link Image]
  3. West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed Link Image]
  4. Agarwal AK, Arioglu E, De Almeida S, Akkoc N, Taylor SI, Bowcock AM, Barnes RI, Garg A: AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Nat Genet. 2002 May;31(1):21-3. Epub 2002 Apr 22. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 7284
Enzyme 51 Name Bifunctional coenzyme A synthase
Enzyme 51 Synonyms
  1. CoA synthase
  2. NBP
  3. POV-2[Includes: Phosphopantetheine adenylyltransferase
  4. Pantetheine-phosphate adenylyltransferase
  5. PPAT
  6. Dephospho-CoA pyrophosphorylase
  7. Dephospho-CoA kinase
  8. DPCK
  9. Dephosphocoenzyme A kinase
  10. DPCOAK]
Enzyme 51 Gene Name COASY
Enzyme 51 Protein Sequence >Bifunctional coenzyme A synthase
MAVFRSGLLVLTTPLASLAPRLASILTSAARLVNHTLYVHLQPGMSLEGPAQPQSSPVQA
TFEVLDFITHLYAGADVHRHLDVRILLTNIRTKSTFLPPLPTSVQNLAHPPEVVLTDFQT
LDGSQYNPVKQQLVRYATSCYSCCPRLASVLLYSDYGIGEVPVEPLDVPLPSTIRPASPV
AGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPEL
LQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINR
FRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCLYV
IGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGI
INRKVLGSRVFGNKKQLKILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQ
NLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVEQSHVVLSTLWEPHI
TQRQVEKAWALLQKRIPKTHQALD
Enzyme 51 Number of Residues 564
Enzyme 51 Molecular Weight 62330
Enzyme 51 Theoretical pI 6.99
Enzyme 51 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • nucleotidyltransferase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 51 General Function Not Available
Enzyme 51 Specific Function Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopan