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Human Metabolome Database Version 2.5

 

Showing metabocard for Malonyl-CoA (HMDB01175)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:34
Accession Number HMDB01175
Secondary Accession Numbers Not Available
Common Name Malonyl-CoA
Description A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
Synonyms
  1. Malonyl Coenzyme A
  2. S-(Hydrogen malonyl)coenzyme A
  3. S-(hydrogen propanedioate) Coenzyme A
  4. malonyl-CoA
  5. omega-Carboxyacyl-CoA
  6. Malonyl CoA
  7. S-(hydrogen propanedioate) CoA
  8. malonyl-Coenzyme A
  9. omega-Carboxyacyl-Coenzyme A
  10. S-(hydrogen propanedioic acid
  11. S-(hydrogen propanedioate
Chemical IUPAC Name 3-[2-[3-[4-[[[5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxy-2-hydroxy-3,3-dimethyl-butanoyl]aminopropanoylamino]ethylsulfanyl]-3-oxo-propanoic acid
Chemical Formula C24H38N7O19P3S
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
  • carboxylic acid
  • secondary carboxylic acid amide
  • thiocarboxylic acid ester
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of beta-Alanine metabolism
  • Component of Propanoate metabolism
  • Component of Pyruvate metabolism
  • Component of Tetracycline biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 853.580
Monoisotopic Molecular Weight 853.115601
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)NCCSC(=O)CC(O)=O
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)NCCSC(=O)CC(O)=O
KEGG Compound ID C00083 Link Image
BioCyc ID MALONYL-COA Link Image
BiGG ID 33789 Link Image
Wikipedia Link Malonyl-CoA Link Image
NuGOwiki Link HMDB01175 Link Image
Metagene Link HMDB01175 Link Image
METLIN ID 6056 Link Image
PubChem Compound 10663 Link Image
PubChem Substance 8143233 Link Image
ChEBI ID 15531 Link Image
CAS Registry Number 524-14-1
InChI Identifier InChI=1/C24H38N7O19P3S/c1-24(2,19(37)22(38)27-4-3-13(32)26-5-6-54-15(35)7-14(33)34)9-47-53(44,45)50-52(42,43)46-8-12-18(49-51(39,40)41)17(36)23(48-12)31-11-30-16-20(25)28-10-29-21(16)31/h10-12,17-19,23,36-37H,3-9H2,1-2H3,(H,26,32)(H,27,38)(H,33,34)(H,42,43)(H,44,45)(H2,25,28,29)(H2,39,40,41)/t12-,17-,18-,19?,23-/m1/s1
Synthesis Reference Hulsmann, W. C. Synthesis of malonyl coenzyme A from acetyl coenzyme A and oxalosuccinate in mitochondria. Biochimica et Biophysica Acta (1963), 77(3), 502-3.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.80 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -5
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.62 [Predicted by ALOGPS]; -6.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
  • peroxisome
Biofluid Location Not Available
Tissue Location
Tissue References
Adipose Tissue —
Fibroblasts —
Liver —
Muscle —
Pancreas —
Skeletal Muscle —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Fatty Acid Biosynthesis SMP00456 Link Image
Propanoate Metabolism SMP00016 Link Image map00640 Link Image
Pyruvate Metabolism SMP00060 Link Image map00620 Link Image
General References
  1. Napal L, Dai J, Treber M, Haro D, Marrero PF, Woldegiorgis G: A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme. J Biol Chem. 2003 Sep 5;278(36):34084-9. Epub 2003 Jun 25. [PubMed Link Image]
  2. Kuhl JE, Ruderman NB, Musi N, Goodyear LJ, Patti ME, Crunkhorn S, Dronamraju D, Thorell A, Nygren J, Ljungkvist O, Degerblad M, Stahle A, Brismar TB, Andersen KL, Saha AK, Efendic S, Bavenholm PN: Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle. Am J Physiol Endocrinol Metab. 2006 Jun;290(6):E1296-303. Epub 2006 Jan 24. [PubMed Link Image]
  3. Odland LM, Howlett RA, Heigenhauser GJ, Hultman E, Spriet LL: Skeletal muscle malonyl-CoA content at the onset of exercise at varying power outputs in humans. Am J Physiol. 1998 Jun;274(6 Pt 1):E1080-5. [PubMed Link Image]
  4. Bandyopadhyay GK, Yu JG, Ofrecio J, Olefsky JM: Increased malonyl-CoA levels in muscle from obese and type 2 diabetic subjects lead to decreased fatty acid oxidation and increased lipogenesis; thiazolidinedione treatment reverses these defects. Diabetes. 2006 Aug;55(8):2277-85. [PubMed Link Image]
  5. Pender C, Trentadue AR, Pories WJ, Dohm GL, Houmard JA, Youngren JF: Expression of genes regulating malonyl-CoA in human skeletal muscle. J Cell Biochem. 2006 Oct 15;99(3):860-7. [PubMed Link Image]
  6. Prentki M, Corkey BE: Are the beta-cell signaling molecules malonyl-CoA and cystolic long-chain acyl-CoA implicated in multiple tissue defects of obesity and NIDDM? Diabetes. 1996 Mar;45(3):273-83. [PubMed Link Image]
  7. Bavenholm PN, Pigon J, Saha AK, Ruderman NB, Efendic S: Fatty acid oxidation and the regulation of malonyl-CoA in human muscle. Diabetes. 2000 Jul;49(7):1078-83. [PubMed Link Image]
  8. Roepstorff C, Halberg N, Hillig T, Saha AK, Ruderman NB, Wojtaszewski JF, Richter EA, Kiens B: Malonyl-CoA and carnitine in regulation of fat oxidation in human skeletal muscle during exercise. Am J Physiol Endocrinol Metab. 2005 Jan;288(1):E133-42. Epub 2004 Sep 21. [PubMed Link Image]
  9. Ruderman NB, Saha AK, Vavvas D, Witters LA: Malonyl-CoA, fuel sensing, and insulin resistance. Am J Physiol. 1999 Jan;276(1 Pt 1):E1-E18. [PubMed Link Image]
  10. Saha AK, Ruderman NB: Malonyl-CoA and AMP-activated protein kinase: an expanding partnership. Mol Cell Biochem. 2003 Nov;253(1-2):65-70. [PubMed Link Image]
  11. Morillas M, Gomez-Puertas P, Bentebibel A, Selles E, Casals N, Valencia A, Hegardt FG, Asins G, Serra D: Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibition. J Biol Chem. 2003 Mar 14;278(11):9058-63. Epub 2002 Dec 23. [PubMed Link Image]
  12. Odland LM, Heigenhauser GJ, Lopaschuk GD, Spriet LL: Human skeletal muscle malonyl-CoA at rest and during prolonged submaximal exercise. Am J Physiol. 1996 Mar;270(3 Pt 1):E541-4. [PubMed Link Image]
  13. Trevisan CP, Angelini C, Fiorellini LA, Isaya G, Zacchello G: Malonyl-CoA abnormal inhibition of residual enzyme activity in carnitine palmitoyltransferase deficiency. Eur Neurol. 1986;25(4):309-16. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. Malonyl-CoA decarboxylase, mitochondrial precursor
  2. Acetyl-CoA carboxylase 2
  3. Fatty acid synthase
  4. Acetyl-CoA carboxylase 1
  5. Malonyl CoA-acyl carrier protein transacylase, mitochondrial precursor
  6. Putative uncharacterized protein
Enzyme 1 [top]
Enzyme 1 ID 5245
Enzyme 1 Name Malonyl-CoA decarboxylase, mitochondrial precursor
Enzyme 1 Synonyms
  1. MCD
Enzyme 1 Gene Name MLYCD
Enzyme 1 Protein Sequence >Malonyl-CoA decarboxylase, mitochondrial precursor 
MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKT
PAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAA
VLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNG
VLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFF
SHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQG
VELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSEC
KEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVA
NFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQV
LSLVAQFQKNSKL
Enzyme 1 Number of Residues 493
Enzyme 1 Molecular Weight 55004
Enzyme 1 Theoretical pI 9.26
Enzyme 1 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
  • malonyl-CoA decarboxylase activity
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids
Enzyme 1 Pathways
Enzyme 1 Reactions
  • malonyl-CoA = acetyl-CoA + CO2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 5231269 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O95822 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DCMC_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1365 bp 
ATGGACGAGCTGCTGCGCCGCGCGGTGCCGCCGACGCCGGCCTACGAGCTGCGCGAGAAG
ACACCGGCGCCCGCCGAGGGTCAGTGCGCGGACTTCGTGAGCTTCTACGGTGGGCTGGCC
GAGACGGACCAGCGGGCCGAACTGCTGGGCCGCCTGGCGCGGGGCTTCGGCGTGGACCAC
GGCCAGGTGGCGGAGCAGAGCGCCGGCGTGCTCCATCTGCGCCAGCAGCAGCGGGAGGCG
GCGGTGCTGCTGCAGGCCGAGGACCGGCTGCGCTACGCGCTGGTGCCGCGCTATCGCGGC
CTCTTCCACCACATCAGCAAGCTGGACGGCGGCGTGCGCTTCCTGGTGCAGCTGCGGGCC
GACCTGCTGGAGGCGCAGGCCCTCAAGCTGGTGGAGGGGCCGGACGTCCGGGAAATGAAT
GGGGTGCTGAAAGGAATGCTCTCAGAATGGTTTTCCTCCGGGTTCCTGAACCTAGAACGG
GTTACCTGGCATTCACCGTGTGAAGTGCTTCAGAAAATCAGTGAGGCTGAGGCTGTGCAT
CCTGTAAAAAACTGGATGGACATGAAGCGCCGCGTTGGGCCCTACAGAAGGTGTTACTTC
TTTTCTCACTGTTCGACCCCTGGGGAGCCCCTGGTCGTTTTGCACGTGGCACTGACTGGT
GACATCTCCAGCAACATCCAGGCAATCGTGAAGGAACATCCTCCATCAGAAACAGAAGAG
AAGAACAAAATCACTGCTGCGATCTTTTATTCCATCAGCTTGACCCAGCAGGACTCCAAG
GGGTGGAGCTGGGAACATTCCTCAATAAAGCGAGTCGTCAAGGAGTTGCAGAGAGAGTTT
CCTCACCTTGGGGTGTTTTCAAGTCTGTCACCTATACCTGGTTTCACCAAATGGCTTCTG
GGGCTTCTGAACTCGCAAACGAAGGAGCATGGGAGGAATGAACTCTTTACAGATTCGGAA
TGTAAGGAAATCTCGGAGATCACAGGTGGCCCCATTAACGAGACCCTCAAGCTCCTCCTC
AGCAGCAGCGAGTGGGTGCAGTCGGAGAAGCTGGTGCGGGCGCTGCAGACTCCGCTGATG
AGGCTGTGCGCCTGGTACCTGTATGGAGAGAAGCACCGCGGCTACGCGCTGAACCCCGTG
GCCAACTTCCACCTGCAGAACGGGGCGGTGCTGTGGCGCATCAACTGGATGGCGGATGTG
AGCCTCAGAGGCATCACCGGCTCCTGCGGCCTGATGGCCAACTACCGCTACTTCCTGGAG
GAGACGGGCCCCAACAGCACCTCCTACCTCGGCTCCAAGATCATCAAAGCCTCTGAGCAG
GTCCTCAGCCTAGTGGCCCAGTTTCAAAAGAACAGCAAGCTCTGA
Enzyme 1 GenBank Gene ID AF097832 Link Image
Enzyme 1 GeneCard ID MLYCD Link Image
Enzyme 1 GenAtlas ID MLYCD Link Image
Enzyme 1 HGNC ID HGNC:7150 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. FitzPatrick DR, Hill A, Tolmie JL, Thorburn DR, Christodoulou J: The molecular basis of malonyl-CoA decarboxylase deficiency. Am J Hum Genet. 1999 Aug;65(2):318-26. [PubMed Link Image]
  2. Sacksteder KA, Morrell JC, Wanders RJ, Matalon R, Gould SJ: MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency. J Biol Chem. 1999 Aug 27;274(35):24461-8. [PubMed Link Image]
  3. Gao J, Waber L, Bennett MJ, Gibson KM, Cohen JC: Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase. J Lipid Res. 1999 Jan;40(1):178-82. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5247
Enzyme 2 Name Acetyl-CoA carboxylase 2
Enzyme 2 Synonyms
  1. ACC-beta[Includes: Biotin carboxylase
Enzyme 2 Gene Name ACACB
Enzyme 2 Protein Sequence >Acetyl-CoA carboxylase 2 
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGT
GTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSV
AGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHR
DFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVT
PEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKL
PELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK
RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQV
QSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAP
LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNL
PAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDE
GFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVA
LKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGAL
NVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM
NGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSP
SAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVAR
LELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIK
LKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFP
SQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRV
EHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSD
ELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCP
ENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCV
VEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTR
NFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVP
ILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQL
ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEY
LQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGS
RLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSF
GNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPK
DILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIG
SFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFK
YLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSL
AYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQL
GGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSR
APYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVE
TRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAIKDFNREKLPLMIFANWRGF
SGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYA
DKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLK
AREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVK
QEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIR
ENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
Enzyme 2 Number of Residues 2458
Enzyme 2 Molecular Weight 276558
Enzyme 2 Theoretical pI 6.46
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-24
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2138330 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O00763 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name COA2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >7452 bp 
ATGGTCTTGCTTCTTTGTCTATCTTGTCTGATTTTCTCCTGTCTGACCTTTTCCTGGTTA
AAAATCTGGGAGAAAATGACGGACTCCAAGCCGATCACCAAGAGTAAATCAGAAGCAAAC
CTCATCCCGAGCCAGGAGCCCTTTCCAGCCTCTGATAACTCAGGGGAGACACCGCAGAGA
AATGGGGAGGGCCACACTCTGCACAAAGACACCCAGCCAGGCCGAGCCCAGCCTCCCACA
AAGGCCCAAAGATCCGGTCGGCGGAGAAACTCCCTACCACCCTCCCGCCAGAAGCCCCCA
AGAAACCCCCTTTCTTCCAGTGACGCAGCACCCTCCCCAGAGCTTCAAGCCAACGGGACT
GGGACACAAGGTCTGGAGGCCACAGATACCAATGGCCTGTCCTCCTCAGCCAGGCCCCAG
GGCAGCAAGCTGGTCCCCTCCAAAGAAGACAAGAAGCAGGCAAACATCAAGAGGCAGCTG
ATGACCAACTTCATCCTGGGCTCTTTTGATGACTACTCCTCCGACGAGGACTCTGTTGCT
GGCTCATCTCGTGAGTCTACCCGGAAGGGCAGCCGGGCCAGCTTGGGGGCCCTGTCCCTG
GAGGCTTATCTGACCACAGGTGAAGCTGAGACCCGCGTCCCCACTATGAGGCCGAGCATG
TCGGGACTCCACCTGGTGAAGAGGGGACGGGAACACAAGAAGCTGGACCTGCACAGAGAC
TTTACCGTGGCTTCTCCCGCTGAGTTTGTCACACGCTTTGGGGGGGATCGGGTCATCGAG
AAGGTGCTTATTGCCAACAACGGGATTGCCGCTGTGAAGTGCATGCGCTCCATCCGCAGG
TGGGCCTATGAGATGTTCCGCAACGAGCGGGCCATCCGGTTTGTTCGCATGGTGACCCCC
GAGGACCTTAAGGCCAACGCAGAGTACATCAAGATGGCGGATCATTACGGGCCCGCCCCA
GGAGGGCCCAATAACAACAACTATGCCAACGTGGAGCTGATTGTGGACATTGCCAAGAGA
ATCCCGTTGCAGGCGGTGTGGGCTGGCTGGGGCCATGCTTTAGAAAACCCTAAACTTCCG
GAGCTGCTGTGCAAGAATGGAGTTGCTTTCTTAGGCCCTCCCAGGTTGAGGCCAATGGTG
GGTCTAGGAGATAAGATCGCCTCCACCGTTGTCGCCCAGACGCTACAGGTCCCAACCCTG
CCCAGGAGTGGAAGCGCCCTGACAGTGGAGTGGACAGAAGATGATCTGCAGCAGGGAAAA
AGAATCAGTGTCCCAGAAGATGTTTATGACAAGGGTTGCGTGAAAGACGTAGATGAGGGC
TTGGAGGCAGCAGAAAGAATTGGTTTTCCATTGATGATCAAAGCTTCTGAAGGTGGCGGA
GGGAAGGGAATCCGGGAAACTGAGAGTGCGGAGGACTTCCCGATCCTTTTCAGACAAGTA
CAGAGTGAGATCCCAGGCTCGCCCATCTTTCTCATGAAGCTGGCCCAGCACGCCCGTCAC
CTGGAAGTTCAGATCCTCGCTGACCAGTATGGGAATGCTGTGTCTCTGTTTGGTCGCGAC
TGCTCCATCCAGCGGCGGCATCAGAAGATCGTTGAGGAAGCACCGGCCACCATCGCGCCG
CTGGCCATATTCGAGTTCATGGAGCAGTGTGCCATTCGCCTGGCCAAGACCGTGGGCTAT
GTGAGTGCAGGGACAGTGGAATACCTCTATAGTCAGGATGGTAGCTTCCACTTCTTGGAG
CTGAATCCTCGCTTGCAGGTGGAACATCCCTGCACAGAAATGATTGCTGACGTTAATCTG
CCGGCCGCCCAGCTACAGATCGCCATGGGTGCCCCACTGCACCGGCTGAAAGATATCCGG
CTTCTGTATGGAGAGTCACCCTGGGGAGACTCCCCAATTTCTTTTGAAAACTCAGCTCAT
CTCCCCTGCCCCCGAGGCCACGTCATTGCCACCAGAATCACCAGCGAAAACCCAGACGAG
GGTTTTAAGCCGAGCTCCGGGACTGTCCAGGAACTGAATTTCCGGAGCAGCAAGAACGTC
TGGGGTTACTTCACGGTGGCCGCTACTGGAGGCCTGCACGAGTTTGCGATTTCCCAGTTT
GGGCACTGCTTCTCCTGGGGAGAGAACCGGAAAGAGGCCATTTCGAACATGGTGGTGGCT
TTGAAGGAACTGTCCCTCCGAGGCGACTTTAGGACTACCGTGGAATACCTCATTAACCTC
CTGGAGACCGAGAGCTTCCAGAACAACTACATCGACACCGGGTGGTTGGACTACCTCATT
GCTGAGAAAGTGCAAAAGAAACCGAATATCATGCTTGGGGTGGTATGCGGGGCCCTTGAA
CGTGGAGATGCGATGTTCAGAACGTGCATGACAGATTTCTTACACTCCCTGGAAAGGGGC
CAGGTCCTCCCAGCGGATTCACTACTGAACCTCGTAGATGTGGAATTAATTTACGAGGGT
GTAAAGTACATTCTAAAGGTGACCCGGCAGTCTCTGACCATGTTCGTTCTCATCATGAAT
GGCTGCCACATCGAGATTGATGCCCACCGGCTGAATGATGGGGGGCTCCTGCTCTCCTAC
AATGGGAACAGCTACACCACCTACATGAAGGAAGAGGTTGACAGTTACCGTACCATCGGC
AATAAGACGTGTGTTTTTGAGAAGGAGAACGATCCTACAGTCCTGAGATCCCCCTCGGCT
GGGAAGCTGACACAGATCACAGTGGAGGATGGGGGCCACGTTGAGGCTGGGAGACGCTAC
GCTGAGATGGAGGTGATGAAGATGATCATGACCCTGAACGTTCAGGAAAGAGGCCGGGTG
AAGTACATCAAGCGTCCAGGTGCGGTGCTGGAAGCAGGCTGCGTGGTGGCCAGGCTGGAG
CTCGATGACCCTTCTAAAGTCCACCCGGCTGAACCGTTCACAGGAGAACTCCCTGCCCAG
CAGAACACTGCCGACCTCGGAAAGAAACTGCACAGGGTCTTCCACAGCGTCCTGGGAAGC
CTCACCAACGTCATGAGTGGCTTTTGTCTGCCAGAGCCGTTTTTTAGCATAAAGCTGAAG
GAGTGGGTGCAGAAGCTCATGATGACCCTCCGGCACCCGTCACTGCTGCTGGACGTGCAG
GAGATCATGACCAGTCGTGCAGGCCGCATCCCCCCCCCTGTTGAGAAGTCTGTCCGCAAG
GTGATGGCCCAGTATGCCAGCAACATCACCTCGGTGCTGTGCCAGTTCCCCAGCCAGCAG
ATAGCCACCATCCTGGACTGCCATGCAGCCACCCTGCAGCGGAAGGCTGATCGAGAGGTC
TTCTTCATCAACACCCAGAGCATGGTGCAGTTGGTCCAGAGGTACCGAAGTGGAATCCGC
GGTCATATGAAAACAGTGGTGATCGATCTCTTGAGAAGATACTTGCGTGTTGAGACCATT
TTCGGCAAGGCAAGAGATGCTGATGCCAACTCCAGTGGGATGGTGGGGGGCGTGAGGAGC
CTGAGCTTTACCTCTGTGTGGGTGGTTTTGTCTCCCCCAGCCCACTACGACAAGTGTGTG
ATAAACCTCAGGGAACAGTTCAAGCCAGACATGTCCCAGGTGCTGGACTGCATCTTCTCC
CACGCACAGGTGACCAAGAAGAACCAGCTGGTGATCATGTTGATCGATGAGCTGTGTGGC
CCAGACCCTTCCCTGTCGGACGAGCTGATCTCCATCCTCAACGAGCTCACTCAGCTGAGC
AAAAGCGAGCACTGCAAAGTGGCCCTCAGAGCCCGGCAGATCCTGATCGCCTCCCCCTCC
TACGAGCTGCGGCATAACCAGGTGGAGTCCATTTTCCTGTCTGCCATTGACATGTACGGC
CACCAGTTCTGCCCCGAGAACCTCCAGAAATTAATACTTTCGGAAACAACCATCTTCGAC
GTCCTGAATACTTTCTTCTATCACGCAAACAAAGTCGTGTGCATGGCGTCCTTGGAGGTT
TACGTGGGGGGGGCTTACATCGCCTATGTGTTAAACAGCCTGCAGCACCGGCAGCTCCCG
GACGGCACCTGCGTGGTAGAATTCCAGTTCATGCTGCCGTCCTCCCACCCAAACCGGATG
ACCGTGCCCATCAGCATCACCAACCCTGACCTGCTGAGGCACACGACAGAGCTCTTCATG
GACAGCGGCTTCTCCCCACTGTGCCAGCGCATGGGAGCCATGGTAGCCTTCAGGAGATTC
GAGGACTTCACCAGAAATTTTGATGAAGTCATCTCTTGCTTCGCCAACGTGCCGAAAGAC
CCCCCCCTCTTCAGCGAGGCCCGCACCTCCCTATACTCCGAGGATGACTGCAAGAGCCTC
AGAGAAGAGCCCATCCACATTCTGAATGTGTCCATCCAGTGTGCGGACCACCTGGAGGAT
GAGGCACTGGTGCCGATTTTACGTACATTCGTACAGTCCAAGAAAAATATCCTTGTGGAT
TATGGACTCCGACGAATCCCATTCTTGATTGCCCAAGAGAAAGAATTTCCCAAGTTTTTC
ACATTCAGAGCAAGAGATGAGTTTGCAGAAGATCGCATTTACCGTCACTTGGAACCTGCC
CTGGCTTTCCAGCTGGAACTCAACCGGATGCGTAACTTCGATCTGACCGCCGTGCCCTGT
GCCAACCACAAGATGCACCTTTACCTGGGTGCTGCCAAGGTGGAAGGAAGGTATGAAGTG
ACGGACCATAGGTTCTTCATCCGTGCCATCATCAGGCACTCTGACCTGATCACAAAGGAA
GCCTCCTTCGAATACCTGCAGAACGAGGGTGAGCGGCTGCTCCTGGAGGCCATGGACGAG
CTGGAGGTGGCGTTCAATAACACCAACGTGCGCACCGACTGCAACCACATCTTCCTCAAC
TTCGTGCCCACTGTCATCATGGACCCCAACAAGATCGAGGAGTCCGTGCGCTACATGGTT
ATGCGCTACGGCAGCCGGCTGTGGAAACTCCGTGTGCTACAGGCTGAGGTCAAGATCAAC
ATCCGCCAGACCACCACCGGCAGTGCCGTTCCCATCCGCCTGTTCATCACCAATGAGTCG
GGCTACTACCTGGACATCAGCCTCTACAAAGAAGTGACTGACTCCAGATCTGGAAATATC
ATGTTTCACTCCTTCGGCAACAAGCAAGGGCCCCAGCACGGGATGCTGATCAATACTCCC
TACGTCACCAAGGATCTGCTCCAGGCCAAGCGATTCCAGGCCCAGACCCTGGGAACCACC
TACATCTATGACTTCCCGGAAATGTTCAGGCAGGCTCTCTTTAAACTGTGGGGCTCCCCA
GACAAGTATCCCAAAGACATCCTGACATACACTGAATTAGTGTTGGACTCTCAGGGCCAG
CTGGTGGAGATGAACCGACTTCCTGGTGGAAATGAGGTGGGCATGGTGGCCTTCAAAATG
AGGTTTAAGACCCAGGAGTACCCGGAAGGACGGGATGTGATCGTCATCGGCAATGACATC
ACCTTTCGCATTGGATCCTTTGGCCCTGGAGAGGACCTTCTGTACCTGCGGGCATCCGAG
ATGGCCCGGGCAGAGGCGATTCCCAAAATTTACGTGGCAGCCAACAGTGGCGCCCGTATT
GGCATGGCAGAGGAGATCAAACACATGTTCCACGTGGCTTGGGTGGACCCAGAAGACCCC
CACAAAGGATTTAAATACCTGTACCTGACTCCCCAAGACTACACCAGAATCAGCTCCCTG
AACTCCGTCCACTGTAAACACATCGAGGAAGGAGGAGAGTCCAGATACATGATCACGGAT
ATCATCGGGAAGGATGATGGCTTGGGCGTGGAGAATCTGAGGGGCTCAGGCATGATTGCT
GGGGAGTCCTCTCTGGCTTACGAAGAGATCGTCACCATTAGCTTGGTGACCTGCCGAGCC
ATTGGGATTGGGGCCTACTTGGTGAGGCTGGGCCAGCGAGTGATCCAGGTGGAGAATTCC
CACATCATCCTCACAGGAGCAAGTGCTCTCAACAAGGTCCTGGGAAGAGAGGTCTACACA
TCCAACAACCAGCTGGGTGGCGTTCAGATCATGCATTACAATGGTGTCTCCCACATCACC
GTGCCAGATGACTTTGAGGGGGTTTATACCATCCTGGAGTGGCTGTCCTATATGCCAAAG
GATAATCACAGCCCTGTCCCTATCATCACACCCACTGACCCCATTGACAGAGAAATTGAA
TTCCTCCCATCCAGAGCTCCCTACGACCCCCGGTGGATGCTTGCAGGAAGGCCTCACCCA
ACTCTGAAGGGAACGTGGCAGAGCGGATTCTTTGACCACGGCAGTTTCAAGGAAATCATG
GCACCCTGGGCGCAGACCGTGGTGACAGGACGAGCAAGGCTTGGGGGGATTCCCGTGGGA
GTGATTGCTGTGGAGACACGGACTGTGGAGGTGGCAGTCCCTGCAGACCCTGCCAACCTG
GATTCTGAGGCCAAGATAATTCAGCAGGCAGGACAGGTGTGGTTCCCAGACTCAGCCTAC
AAAACCGCCCAGGCCATCAAGGACTTCAACCGGGAGAAGTTGCCCCTGATGATCTTTGCC
AACTGGAGGGGGTTCTCCGGTGGCATGAAAGACATGTATGACCAGGTGCTGAAGTTTGGA
GCCTACATCGTGGACGGCCTTAGACAATACAAACAGCCCATCCTGATCTATATCCGCCCT
ATGCGGGAGCTCCGGGGAGGCTCCTGGGTGGTCATAGATGCCACCATCAACCCGCTGTGC
ATAGAAATGTATGCAGACAAAGAGAGCAGGGGTGGTGTTCTGGAACCAGAGGGGACAGTG
GAGATTAAGTTCCGAAAGGAAGATCTGATAAAGTCCATGAGAAGGATCGATCCAGCTTAC
AAGAAGCTCATGGAACAGCTAGGGGAACCTGATCTCTCCGACAAGGACCGAAAGGACCTG
GAGGGCCGGCTAAAGGCTCGCGAGGACCTGCTGCTCCCCATCTACCACCAGGTGGCGGTG
CAGTTCGCCGACTTCCATGACACACCCGGCCGGATGCTGGAGAAGGGCGTCATATCTGAC
ATCCTGGAGTGGAAGACCGCACGCACCTTCCTGTATTGGCGTCTGCGCCGCCTCCTCCTG
GAGGACCAGGTCAAGCAGGAGATCCTGCAGGCCAGCGGGGAGCTGAGTCACGTGCATATC
CAGTCCATGCTGCGTCGCTGGTTCGTGGAGACGGAGGGGGCTGTCAAGGCCTACTTGTGG
GACAACAACCAGGTGGTTGTGCAGTGGCTGGAACAGCACTGGCAGGCAGGGGATGGCCCG
CGCTCCACCATCCGTGAGAACATCACGTACCTGAAGCACGACTCTGTCCTCAAGACCATC
CGAGGCCTGGTTGAAGAAAACCCCGAGGTGGCCGTGGACTGTGTGATATACCTGAGCCAG
CACATCAGCCCAGCTGAGCGGGCGCAGGTCGTTCACCTGCTGTCTACCATGGACAGCCCG
GCCTCCACCTGA
Enzyme 2 GenBank Gene ID U89344 Link Image
Enzyme 2 GeneCard ID ACACB Link Image
Enzyme 2 GenAtlas ID ACACB Link Image
Enzyme 2 HGNC ID HGNC:85 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12q24.11
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Abu-Elheiga L, Almarza-Ortega DB, Baldini A, Wakil SJ: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. J Biol Chem. 1997 Apr 18;272(16):10669-77. [PubMed Link Image]
  2. Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA: Identification of a second human acetyl-CoA carboxylase gene. Biochem J. 1996 Jun 15;316 ( Pt 3):915-22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5264
Enzyme 3 Name Fatty acid synthase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name FASN
Enzyme 3 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 3 Number of Residues 2511
Enzyme 3 Molecular Weight 273403
Enzyme 3 Theoretical pI 6.39
Enzyme 3 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 3 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = 2-hexadecenoyl-[acyl-carrier protein] + H2O
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1049053 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P49327 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name FAS_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID U26644 Link Image
Enzyme 3 GeneCard ID FASN Link Image
Enzyme 3 GenAtlas ID FASN Link Image
Enzyme 3 HGNC ID HGNC:3594 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5276
Enzyme 4 Name Acetyl-CoA carboxylase 1
Enzyme 4 Synonyms
  1. ACC-alpha[Includes: Biotin carboxylase
Enzyme 4 Gene Name ACACA
Enzyme 4 Protein Sequence >Acetyl-CoA carboxylase 1 
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLS
DLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK
VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG
GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL
GDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQA
AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV
QILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSA
GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY
GVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY
FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET
ESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQV
LPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDG
SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYA
EIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQ
STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQ
DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV
FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD
MNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALR
ARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH
SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM
SFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSP
PQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLV
DHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ
LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE
YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG
SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA
YGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQA
FLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVI
GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVD
PEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGS
GMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR
EVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPID
RIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG
IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL
MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSI
NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAE
RKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLR
RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTE
EDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILST
MDSPST
Enzyme 4 Number of Residues 2346
Enzyme 4 Molecular Weight 265557
Enzyme 4 Theoretical pI 6.32
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 849083 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q13085 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name COA1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >7041 bp 
ATGGATGAACCATCTCCCTTGGCCCAACCTCTGGAGCTGAACCAGCACTCTCGATTCATA
ATAGGTTCTGTGTCAGAAGATAACTCAGAGGATGAGATCAGCAACCTGGTGAAGCTGGAC
CTACTGGAGGAGAAGGAGGGCTCCTTGTCACCTGCTTCTGTTGGCTCAGATACACTCTCT
GATTTGGGGATCTCTGCCCTACAGGATGGCTTGGCCTTGCACATAAGGTCCAGCTGGTCT
GGCTTGCACCTAGTAAAGCAGGGCGGAGACAGAAAGAAAATAGATTCTCAACGAGATTTC
ACTGTGGCTTCTCCAGCAGAATTTGTTACTCGCTTTGGGGGAAATAAAGTGATTGAGAAG
GTTCTCATCGCTAACAATGGCATTGCAGCAGTGAAATGCATGCGGTCTATCCGTAGGTGG
TCTTATGAAATGTTTCGAAATGAACGTGCAATTAGATTCGTTGTCATGGTCACACCTGAA
GACCTTAAAGCCAATGCAGAATACATTAAGATGGCAGATCACTATGTGCCGGTGCCTGGA
GGAGCAAACAACAACAACTATGCAAATGTGGAATTAATTCTTGATATTGCTAAAAGGATC
CCAGTGCAAGCAGTGTGGGCTGGCTGGGGTCATGCTTCTGAGAATCCCAAACTACCGGAA
CTTCTCTTGAAAAATGGCATTGCCTTCATGGGTCCTCCAAACCAGGCCATGTGGGCTTTA
GGGGATAAGATTGCATCTTCCATAGTGGCTCAAACTGCAGGTATCCCAACTCTTCCCTGG
AGCGGCAGTGGTCTTCGTGTGGACTGGCAGGAAAATGATTTTTCAAAACGTATCTTAAAT
GTTCCCCAGGAGCTATATGAAAAAGGTTATGTGAAAGATGTGGATGATGGGCTAAAGGCA
GCTGAGAAGGTTGGATATCCAGTAATGATCAAGGCCTCAGAGGGAGGAGGAGGGAAGGGA
ATTAGAAAAGTTAACAATGCAGATGACTTCCCTAATCTCTTCAGACAGGTTCAAGCTGAA
GTTCCTGGATCTCCCATATTTGTGATGAGACTAGCCAAACAATCTCGTCATCTGGAGGTG
CAGATCTTAGCGGACCAATATGGCAATGCTATCTCTTTGTTTGGTCGTGATTGCTCTGTA
CAACGCAGGCATCAGAAGATTATTGAAGAAGCACCTGCTACTATTGCTACTCCAGCAGTA
TTTGAACACATGGAACAGTGTGCGGTGAAACTTGCCAAAATGGTGGGTTATGTGAGTGCT
GGGACTGTGGAATACCTGTACAGCCAGGATGGCAGCTTCTACTTTCTAGAATTGAACCCT
CGGCTACAGGTTGAACAACCTTGTACAGAGATGGTGGCTGATGTCAATCTCCCCGCAGCA
CAGCTCCAGATTGCCATGGGGATTCCTCTATATAGAATCAAGGATATCCGTATGATGTAT
GGGGTATCTCCTTGGGGTGATTCTCCCATTGATTTTGAAAATTCTGCTCACGTTCCTTGT
CCAAGGGGCCATGTTATTGCTGCTCGGATCACTAGTGAAAATCCAGATGAGGGTTTTAAG
CCCAGCTCAGGAACAGTTCAGGAGCTAAATTTCCGCAGCAATAAGAATGTTTGGGGATAT
TTCAGTGTTGCTGCTGCAGGGGGACTTCATGAATTTGCTGGTTCTCAGTTTGGTCACTGC
TTTTCTTGGGGAGAAAACAGAGAAGAAGCAATTTCAAACATGGTGGTGGCATTGAAGGAG
CTGTCTATTCGGGGTGACTTTCGAACTACAGTTGAATACCTGATCAAATTGTTAGAGACT
GAAAGCTTTCAAATGAACAGAATTGATACTGGCTGGCTGGACAGACTGATAGCAGAAAAA
GTACGGGCTGAGCGTCCTGACACCATGTTGGGGGTTGTGTGTGGTGCCCTCCACGTCGGA
GATGTGAGCCTGCGAAATAGCGTCTCTAACTTCCTTCACTCCTTAGAAAGGGGTCAAGTC
CTTCCGGCTCATACACTTCTGAATACAGTAGATGTTGAACTTATCTATGAGGGAGTCAAG
TATGTACTTAAGGTGACTCGACAGTCCCCCAACTCCTATGTGGTGATCATGAATGGCTCA
TGTGTAGAAGTAGATGTACATCGGCTGAGTGACGGTGGACTGCTCTTGTCCTATGATGGC
AGCAGTTACACCACGTATATGAAGGAGGAAGTAGACAGATATCGCATCACAATTGGCAAT
AAAACCTGTGTGTTTGAGAAGGAAAATGACCCATCGGTGATGCGCTCACCTTCTGCTGGG
AAGTTAATCCAGTACATTGTAGAAGATGGAGGTCATGTGTTTGCCGGCCAGTGCTATGCA
GAGATTGAGGTAATGAAGATGGTAATGACTTTGACAGCTGTGGAGTCTGGCTGTATCCAT
TACGTCAAGCGTCCTGGAGCAGCTCTTGACCCTGGCTGTGTACTCGCCAAAATGCAACTG
GACAACCCCAGCAAGGTTCAGCAGGCTGAACTTCACACAGGTAGTCTGCCACGGATCCAG
AGCACCGCTCTCCGAGGCGAGAAGCTCCATCGAGTGTTCCACTATGTCCTGGATAATCTG
GTCAATGTAATGAATGGATACTGCCTTCCAGATCCTTTCTTTAGCAGCAAGGTAAAAGAC
TGGGTAGAACGATTGATGAAAACCCTCAGAGATCCCTCCCTGCCTCTCCTAGAATTGCAA
GATATTATGACCAGTGTGTCTGGCCGCATTCCCCCCAATGTGGAGAAGTCTATCAAGAAG
GAAATGGCTCAGTATGCTAGCAACATCACATCAGTCCTCTGTCAGTTTCCCAGCCAGCAG
ATTGCAAACATCCTAGATAGCCATGCAGCTACATTGAACCGGAAATCTGAACGGGAAGTC
TTCTTTATGAATACTCAGAGCATTGTCCAGCTGGTACAGAGGTACCGAAGTGGCATCCGA
GGCCACATGAAGGCTGTGGTGATGGATCTGCTCCGGCAGTACCTGCGAGTAGAGACACAA
TTCCAGAATGGTCACTATGACAAATGTGTATTCGCCCTTCGAGAAGAGAATAAGAGTGAC
ATGAACACTGTACTGAACTACATCTTCTCTCACGCTCAAGTCACCAAGAAGAATCTTCTG
GTCACAATGCTTATTGATCAGTTGTGTGGCCGGGACCCTACTCTAACTGATGAGCTGCTG
AGTATTCTCACAGAGCTAACTCAACTCAGTAAGACCACCAATGCCAAAGTAGCACTTCGA
GCACGCCAGGTTCTTATTGCCTCCCATTTGCCATCATATGACGTTCGCCATAACCAAGTA
GAGTCTATCTTCCTATCAGCTATTGACATGTATGGACATCAATTTTGCATTGAGAACCTG
CAGAAACTCATCCTATCAGAAACATCTATTTTTGATGTCCTACCAAACTTCTTCTATCAC
AGCAACCAAGTAGTGAGGATGGCAGCTCTGGAGGTGTACGTTCGAAGGGCTTATATTGCC
TATGAACTTAACAGCGTACAACACCGCCAGCTTAAGGACAACACCTGCGTGGTGGAATTC
CAGTTCATGCTGCCCACATCTCATCCAAACAGAGGGAACATCCCTACGCTAAACAGAATG
TCCTTCTCCTCCAACCTCAACCACTATGGCATGACCCATGTAGCTAGTGTCAGCGATGTT
CTGTTGGACAACGCCTTCACACCACCTTGTCAACGCATGGGCGGAATGGTCTCTTTTCGG
ACTTTTGAAGATTTTGTCAGGATCTTTGATGAAGTAATGGGCTGCTTCTGTGACTCCCCA
CCCCAGAGTCCCACATTCCCTGAGGCAGGTCACACGTCTCTTTATGATGAGGATAAGGTT
CCCAGGGATGAACCAATTCACATTCTCAATGTGGCTATCAAGACTGACGGTGATATTGAG
GATGACAGGCTGGCAGCTATGTTCAGAGAATTCACCCAGCAAAATAAAGCTACCCTGGCT
GACCATGGGATCCGGCGCCTGACTTTCCTGGTTGCACAAAAGGATTTCAGAAAGCAGGTC
AACTATGAGGTGGATCGGAGATTTCATAGAGAATTCCCTAAATTTTTTACATTCCGAGCA
AGGGATAAGTTTGAGGAGGATCGTATCTATCGTCATCTGGAGCCTGCTCTGGCTTTCCAG
TTAGAGCTGAACCGGATGAGAAATTTTGACCTCACTGCCATTCCATGTGCTAATCACAAG
ATGCACCTGTATCTCGGGGCAGCCAAGGTGGAAGTGGGCACAGAAGTGACAGACTACAGG
TTCTTTGTTCGTGCAATCATCAGGCATTCTGATCTGGTCACCAAGGAAGCTTCTTTTGAA
TATCTGCAAAGTGAAGGGGAGCGGCTACTCCTGGAAGCCATGGATGAGTTGGAAGTTGCT
TTTAACAATACAAATGTCCGCACTGACTGTAACCACATCCTCCTCAACTTTGTGCCCACG
GTTATCATGGACCCATCAAAGATTGAGGAATCCGTGCGGAGCATGGTAATGCGGTATGGA
AGTCGCCTGTGGAAATTGCGCGTCCTCCAGGCAGAACTGAAAATCAACATTCGCCTGACG
CCAACTGGAAAAGCAATTCCCATCCGCCTTTTCCTGACAAACGAGTCTGGCTATTACTTG
GATATCAGCCTATACAAGGAAGTGACTGACTCCAGGACAGCACAGATCATGTTTCAGGCA
TATGGAGACAAGCAGGGACCACTGCATGGAATGTTAATCAATACTCCATATGTGACCAAA
GACCTGCTGCAATCAAAGAGGTTCCAGGCACAATCCTTAGGGACAACGTACATATATGAT
ATCCCAGAGATGTTTCGGCAGTCCCTGATCAAACTCTGGGAGTCTATGTCAACTCAAGCA
TTTCTTCCATCTCCCCCTCTGCCTTCTGACATGCTGACTTACACTGAACTGGTACTGGAT
GATCAAGGTCAGCTGGTCCACATGAACAGGCTTCCAGGAGGAAATGAGATTGGCATGGTA
GCTTGGAAAATGAGCCTTAAAAGTCCTGAATATCCAGAAGGCCGAGATGTTATTGTTATT
GGCAATGACATTACATACCGAATTGGGTCCTTTGGGCCTCAAGAAGATTTGTTATTTCTC
AGAGCTTCCGAACTTGCTAGGGCCGAAGGCATTCCACGCATCTATGTATCAGCCAACAGT
GGAGCAAGAATCGGACTGGCAGAAGAAATTCGCCATATGTTTCATGTGGCCTGGGTAGAT
TCTGAGGATCCTTACAAGGGATACAGGTATTTATATCTGACTCCTCAAGATTATAAGAGA
GTCGGTGCTCTCAACTCTGTCCATTGTGAACACGTGGAAGATGAAGGAGAATCCAGGTAC
AAGATAACAGATATTATTGGGAAAGAAGAGGGAATTGGACCCGAGAACCTTCGAGGTTCT
GGAATGATCGCTGGAGAATCCTCATTGGCCTATAATGAGATCATTACCATCAGCCTGGTG
ACGTCCCGGGCCATTGGGATTGGGGCTTACCTTGTCCGGCTGGGACAGAGAACCATCCAG
GTTGAGAATTCTCACTTGATTCTAACAGGAGCTGGAGCCCTCAACAAAGTCCTCGGGCGG
GAAGTGTACACCTCCAATAACCAGCTGGGGGGCATCCAGATTACGCACAACAATGGGGTG
ACCCACTGCACTGTGTGTGACGGCTTTGAAGGGGTTTTCACTGTCCTGCACTGGCTGTCT
TACATGCCCAAGAGCGTACACAGTTCAGTTCCTCTTCTGAACTCAAAGGATCCTATAGAC
AGAATCATCGAGTTTGTTCCCACAAAGACCCCATATGATCCTCGATGGATGCTAGCAGGC
CGCCCTCACCCAACCCAAAAAGGTCAGTGGTTGAGTGGCTTTTTTGACTATGGATCTTTC
TCAGAGATTATGCAGCCCTGGGCACAGACGGTGGTGGTTGGTAGAGCCAGGTTAGGGGGA
ATACCTGTGGGAGTTGTTGCTGTAGAAACCCGGACAGTAGAACTAAGTGTACCAGCTGAT
CCAGCAAACCTGGATTCTGAAGCCAAGATAATCCAGCACGCCGGCCAAGTTTGGTTTCCG
GATTCTGCGTTTAAGACGTATCAGGCCATCAAGGACTTCAACCGGGAAGGGCTACCTCTA
ATGGTCTTTGCCAACTGGAGAGGCTTCTCTGGTGGAATGAAAGATATGTATCACCAAGTG
CTGAAGTTTGGTGCTTACATTGTGGATGGCTTGCGGGAATGTTCCCAGCCTGTGCTGGTC
TACATTCCTCCCCAGGCTGAGCTGCGGGGTGGCTCCTGGGTGGTGATCGACCCAACCATC
AATCCTCGGCACATGGAGATGTATGCTGACCGAGAAAGCAGGGGATCTGTTCTGGAGCCA
GAAGGGACGGTAGAAATCAAATTCCGCAGAAAGGATCTGGTGAAAACCATGCGTCGGGTG
GACCCAGTCTACATCCACTTGGCTGAGCGATTGGGGACCCCAGAGCTGAGCCCAACTGAG
CGGAAGGAGTTGGAGAGCAAGTTGAAGGAGCGGGAGGAATTCCTAATTCCAATTTACCAT
CAGGTAGCCGTGCAGTTTGCTGACTTGCACGACACTCCAGGCCGGATGCAGGAGAAGGGT
GTTATTAGCGATATCCTGGATTGGAAAACATCCCGTACCTTCTTCTACTGGCGACTGAGG
CGTCTTCTGCTGGAGGACCTGGTCAAGAAGAAAATCCACAGTGCCAACCCTGAGCTGACT
GATGGCCAGATTCAAGCCATGTTAAGACGCTGGTTTGTGGAAGTGGAAGGAACAGTGAAG
GCTTATGTTTGGGACAATAATAAGGATCTGGCGGAGTGGCTAGAGAAACAGCTGACAGAG
GAGGATGGTGTTCACTCGGTAATAGAGGAAAACATCAAATGCATCAGCAGAGACTACGTC
CTCAAGCAAATCCGCAGCTTGGTCCAGGCCAATCCAGAGGTTGCCATGGATTCCATCATC
CATATGACGCAGCACATATCACCCACTCAGCGGGCAGAAGTCATAAGGATCCTTTCCACT
ATGGACTCCCCTTCTACGTAG
Enzyme 4 GenBank Gene ID U19822 Link Image
Enzyme 4 GeneCard ID ACACA Link Image
Enzyme 4 GenAtlas ID ACACA Link Image
Enzyme 4 HGNC ID HGNC:84 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17q21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4011-5. [PubMed Link Image]
  2. Mao J, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7515-20. Epub 2003 Jun 16. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5635
Enzyme 5 Name Malonyl CoA-acyl carrier protein transacylase, mitochondrial precursor
Enzyme 5 Synonyms
  1. MCT
  2. Mitochondrial malonyltransferase
Enzyme 5 Gene Name MCAT
Enzyme 5 Protein Sequence >Malonyl CoA-acyl carrier protein transacylase, mitochondrial precursor 
MSVRVARVAWVRGLGASYRRGASSFPVPPPGAQGVAELLRDATGAEEEAPWAATERRMPG
QCSVLLFPGQGSQVVGMGRGLLNYPRVRELYAAARRVLGYDLLELSLHGPQETLDRTVHC
QPAIFVASLAAVEKLHHLQPSVIENCVAAAGFSVGEFAALVFAGAMEFAEGLYAVKIRAE
AMQEASEAVPSGMLSVLGQPQSKFNFACLEAREHCKSLGIENPVCEVSNYLFPDCRVISG
HQEALRFLQKNSSKFHFRRTRMLPVSGAFHTRLMEPAVEPLTQALKAVDIKKPLVSVYSN
VHAHRYRHPGHIHKLLAQQLVSPVKWEQTMHAIYERKKGRGFPQTFEVGPGRQLGAILKS
CNMQAWKSYSAVDVLQTLEHVDLDPQEPPR
Enzyme 5 Number of Residues 390
Enzyme 5 Molecular Weight 42962
Enzyme 5 Theoretical pI 8.88
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Lipid transport and metabolism
Enzyme 5 Specific Function Catalyzes the transfer of a malonyl moiety from malonyl- CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias
Enzyme 5 Pathways
Enzyme 5 Reactions
  • malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 8574364 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q8IVS2 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name FABD_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1173 bp 
ATGAGCGTCCGGGTCGCACGGGTAGCGTGGGTCAGGGGCTTGGGCGCCAGCTACCGCCGC
GGCGCCTCGAGCTTCCCGGTGCCTCCGCCGGGCGCCCAGGGTGTAGCGGAGCTGCTGCGA
GATGCGACCGGGGCGGAGGAGGAGGCGCCCTGGGCGGCGACGGAGCGGCGAATGCCGGGC
CAGTGCTCCGTGCTGCTCTTCCCGGGCCAGGGCAGCCAGGTGGTGGGCATGGGCCGCGGT
CTGCTCAACTACCCGCGCGTCCGCGAACTCTACGCCGCCGCCCGCCGCGTGCTGGGCTAC
GACCTGCTGGAACTGAGCCTGCACGGGCCGCAGGAGACCCTGGACCGCACCGTGCACTGT
CAGCCCGCGATCTTCGTGGCATCGCTGGCCGCTGTCGAGAAACTACATCACCTGCAGCCC
TCGGTGATTGAGAACTGTGTTGCTGCTGCTGGATTCAGTGTGGGAGAGTTTGCAGCCCTA
GTGTTTGCCGGAGCCATGGAATTTGCTGAAGGTTTGTATGCAGTGAAAATCCGAGCTGAG
GCCATGCAGGAAGCTTCAGAAGCTGTCCCCAGTGGGATGCTGTCTGTCCTCGGCCAGCCT
CAGTCCAAGTTCAACTTCGCCTGTTTGGAAGCCCGGGAACACTGCAAGTCTTTAGGCATA
GAGAACCCCGTATGTGAAGTGTCCAACTACCTCTTTCCAGATTGCAGGGTGATTTCAGGA
CACCAAGAGGCTCTACGGTTTCTCCAGAAGAATTCCTCTAAGTTTCATTTCAGACGCACC
AGGATGTTGCCGGTTAGTGGCGCATTCCACACCCGCCTCATGGAGCCAGCCGTGGAGCCC
CTGACGCAAGCTTTAAAGGCAGTCGACATTAAGAAGCCTCTGGTTTCTGTCTACTCCAAC
GTCCACGCGCATAGATACAGGCATCCCGGGCACATCCACAAGCTGCTGGCCCAGCAGCTG
GTCTCCCCAGTGAAGTGGGAGCAGACGATGCATGCCATATACGAAAGGAAAAAGGGCAGG
GGGTTCCCCCAAACTTTCGAAGTAGGCCCTGGCAGGCAGCTGGGAGCCATCCTGAAGAGC
TGTAACATGCAGGCCTGGAAGTCCTACAGCGCCGTGGATGTGCTGCAGACCCTCGAACAT
GTGGACCTGGACCCTCAGGAGCCCCCGAGATGA
Enzyme 5 GenBank Gene ID AL359401 Link Image
Enzyme 5 GeneCard ID MCAT Link Image
Enzyme 5 GenAtlas ID MCAT Link Image
Enzyme 5 HGNC ID HGNC:29622 Link Image
Enzyme 5 Chromosome Location 22
Enzyme 5 Locus 22q13.31
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16719
Enzyme 6 Name Putative uncharacterized protein
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name MCAT
Enzyme 6 Protein Sequence >Putative uncharacterized protein 
MSVRVARVAWVRGLGASYRRGASSFPVPPPGAQGVAELLRDATGAEEEAPWAATERRMPG
QCSVLLFPGQGSQVVGMGRGLLNYPRVRELYAAARRVLGYDLLELSLHGPQETLDRTVHC
QPAIFVASLAAVEKLHHLQPSVIENCVAAAGFSVGEFAALVFAGAMEFAEGSTVSPEEFL
Enzyme 6 Number of Residues 180
Enzyme 6 Molecular Weight 19176
Enzyme 6 Theoretical pI 6.11
Enzyme 6 GO Classification
Function
  • catalytic activity
  • transferase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
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 Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B0QY72 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B0QY72_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AK314059 Link Image
Enzyme 6 GeneCard ID B0QY72 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 22
Enzyme 6 Locus 22q13.31
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available