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Human Metabolome Database Version 2.5

 

Showing metabocard for Caproic acid (HMDB00535)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:02
Accession Number HMDB00535
Secondary Accession Numbers Not Available
Common Name Caproic acid
Description It is a colorless oily liquid smelling of cheese. It is a fatty acid found naturally in various animal fats and oils. Caproic acid is a medium chain triglycerides (MCT). MCTs are widely used for parenteral nutrition in individuals requiring supplemental nutrition and are being more widely used in foods, drugs and cosmetics; they are essentially non-toxic. It is safe for human dietary consumption up to levels of 1g/kg. (PMID 10685018)
Synonyms
  1. 1-Hexanoate
  2. 1-Hexanoic acid
  3. 1-Pentanecarboxylate
  4. 1-Pentanecarboxylic acid
  5. Butylacetate
  6. Butylacetic acid
  7. Caproate
  8. Caproic acid
  9. Capronate
  10. Capronic acid
  11. Hexoate
  12. Hexoic acid
  13. Hexylate
  14. Hexylic acid
  15. Pentylformate
  16. Pentylformic acid
  17. n-Caproate
  18. n-Caproic acid
  19. n-Hexanoate
  20. n-Hexanoic acid
  21. n-Hexoate
  22. n-Hexoic acid
  23. n-Hexylate
  24. n-Hexylic acid
Chemical IUPAC Name Hexanoic acid
Chemical Formula C6H12O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Short chain fatty acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 116.158
Monoisotopic Molecular Weight 116.083733
Isomeric SMILES CCCCCC(O)=O
Canonical SMILES CCCCCC(O)=O
KEGG Compound ID C01585 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Caproic acid Link Image
NuGOwiki Link HMDB00535 Link Image
Metagene Link HMDB00535 Link Image
METLIN ID 5520 Link Image
PubChem Compound 8892 Link Image
PubChem Substance 8156318 Link Image
ChEBI ID 17120 Link Image
CAS Registry Number 142-62-1
InChI Identifier InChI=1/C6H12O2/c1-2-3-4-5-6(7)8/h2-5H2,1H3,(H,7,8)
Synthesis Reference Gao, Fei; Wu, Zongwei. Process for preparation of hexanoic acid by oxidation of 2-octanol with nitric acid. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 7pp.
Melting Point (Experimental) General
Experimental Water Solubility 10.3 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 9.72 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity 1.92 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 1.88 [Predicted by ALOGPS]; 1.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
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
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 17 (0-105) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid CSF
Value 1.5 +/- 0.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid Urine
Value 0.5 (0.0-1.0) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.91 +/- 1.05 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
Fatty Acid Biosynthesis SMP00456 Link Image
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids SMP00480 Link Image
General References
  1. Epps JM, Phillips JO, Mestecky J: IgA-mediated clearance and tissue deposition of dinitrophenylated human serum albumin at various DNP:HSA ratios. Mol Immunol. 1988 Aug;25(8):731-8. [PubMed Link Image]
  2. Varani J, Orr W, Ward PA: Cell-associated proteases affect tumour cell migration in vitro. J Cell Sci. 1979 Apr;36:241-52. [PubMed Link Image]
  3. Schoots AC, Mikkers FE, Cramers CA, Ringoir S: Profiling of uremic serum by high-resolution gas chromatography-electron-impact, chemical ionization mass spectrometry. J Chromatogr. 1979 Sep 11;164(1):1-8. [PubMed Link Image]
  4. Jakobs C, Sweetman L, Nyhan WL: Hydroxy acid metabolites of branched-chain amino acids in amniotic fluid. Clin Chim Acta. 1984 Jul 16;140(2):157-66. [PubMed Link Image]
  5. Nilsen SL, Castellino FJ: Expression of human plasminogen in Drosophila Schneider S2 cells. Protein Expr Purif. 1999 Jun;16(1):136-43. [PubMed Link Image]
  6. Ohdoi C, Nyhan WL, Kuhara T: Chemical diagnosis of Lesch-Nyhan syndrome using gas chromatography-mass spectrometry detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 15;792(1):123-30. [PubMed Link Image]
  7. Varani J, Orr W, Ward PA: Comparison of cell attachment and caseinolytic activities of five tumour cell types. J Cell Sci. 1978 Dec;34:133-44. [PubMed Link Image]
  8. Hoverstad T, Fausa O, Bjorneklett A, Bohmer T: Short-chain fatty acids in the normal human feces. Scand J Gastroenterol. 1984 May;19(3):375-81. [PubMed Link Image]
  9. Harkness RA: Lesch-Nyhan syndrome: reduced amino acid concentrations in CSF and brain. Adv Exp Med Biol. 1989;253A:159-63. [PubMed Link Image]
  10. Wikipedia Link Image
Metabolic Enzymes
  1. Peroxisomal carnitine O-octanoyltransferase
  2. Carnitine O-palmitoyltransferase 2, mitochondrial precursor
  3. Mitochondrial carnitine/acylcarnitine carrier protein
  4. Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
  5. Uncharacterized protein C10orf129
  6. Acyl-coenzyme A synthetase ACSM2A, mitochondrial precursor
  7. Acyl-coenzyme A synthetase ACSM2B, mitochondrial precursor
  8. Acyl-coenzyme A synthetase ACSM3, mitochondrial precursor
  9. Acyl-coenzyme A synthetase ACSM5, mitochondrial precursor
  10. Not Available
Enzyme 1 [top]
Enzyme 1 ID 5542
Enzyme 1 Name Peroxisomal carnitine O-octanoyltransferase
Enzyme 1 Synonyms
  1. COT
Enzyme 1 Gene Name CROT
Enzyme 1 Protein Sequence >Peroxisomal carnitine O-octanoyltransferase 
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS
GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT
QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF
RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL
TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG
DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR
DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI
QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ
QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV
LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF
HDMIQLMNSTHL
Enzyme 1 Number of Residues 612
Enzyme 1 Molecular Weight 70179
Enzyme 1 Theoretical pI 7.09
Enzyme 1 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 1 General Function Not Available
Enzyme 1 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 1 Pathways Not Available
Enzyme 1 Reactions
  • octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 6066280 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9UKG9 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name OCTC_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID AF168793 Link Image
Enzyme 1 GeneCard ID CROT Link Image
Enzyme 1 GenAtlas ID CROT Link Image
Enzyme 1 HGNC ID HGNC:2366 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5546
Enzyme 2 Name Carnitine O-palmitoyltransferase 2, mitochondrial precursor
Enzyme 2 Synonyms
  1. Carnitine palmitoyltransferase II
  2. CPT II
Enzyme 2 Gene Name CPT2
Enzyme 2 Protein Sequence >Carnitine O-palmitoyltransferase 2, mitochondrial precursor 
MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDT
IRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMY
LSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNP
AKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKA
RHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWA
ELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLII
AKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELT
DALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYG
QTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHG
QLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLG
GFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS
Enzyme 2 Number of Residues 658
Enzyme 2 Molecular Weight 73778
Enzyme 2 Theoretical pI 8.30
Enzyme 2 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 2 General Function Not Available
Enzyme 2 Specific Function Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-15
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1041195 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P23786 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CPT2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1977 bp 
ATGGTGCCCCGCCTGCTGCTGCGCGCCTGGCCCCGGGGCCCCGCGGTTGGTCCGGGAGCC
CCCAGTCGGCCCCTCAGCGCCGGCTCCGGGCCCGGCCAGTACCTGCAGCGCAGCATCGTG
CCCACCATGCACTACCAGGACAGCCTGCCCAGGCTGCCTATTCCCAAACTTGAAGACACC
ATTAGGAGATACCTCAGTGCACAGAAGCCTCTCTTGAATGATGGCCAGTTCAGGAAAACA
GAACAATTTTGCAAGAGTTTTGAAAATGGGATTGGAAAAGAACTGCATGAGCAGCTGGTT
GCTCTGGACAAACAGAATAAACATACAAGCTACATTTCGGGACCCTGGTTTGATATGTAC
CTATCTGCTCGAGACTCCGTTGTTCTGAACTTTAATCCATTTATGGCTTTCAATCCTGAC
CCAAAATCTGAGTATAATGACCAGCTCACCCGGGCAACCAACATGACTGTTTCTGCCATC
CGGTTTCTGAAGACACTCCGGGCTGGCCTTCTGGAGCCAGAAGTGTTCCACTTGAACCCT
GCAAAAAGTGACACTATCACCTTCAAGAGACTCATACGCTTTGTGCCTTCCTCTCTGTCC
TGGTATGGGGCCTACCTGGTCAATGCGTATCCCCTGGATATGTCCCAGTATTTTCGGCTT
TTCAACTCAACTCGTTTACCCAAACCCAGTCGGGATGAACTCTTCACTGATGACAAGGCC
AGACACCTCCTGGTCCTAAGGAAAGGAAATTTTTATATCTTTGATGTCCTGGATCAAGAT
GGGAACATTGTGAGCCCCTCGGAAATCCAGGCACATCTGAAGTACATTCTCTCAGACAGC
AGCCCCGCCCCCGAGTTTCCCCTGGCATACCTGACCAGTGAGAACCGAGACATCTGGGCA
GAGCTCAGGCAGAAGCTGATGAGTAGTGGCAATGAGGAGAGCCTGAGGAAAGTGGACTCG
GCAGTGTTCTGTCTCTGCCTAGATGACTTCCCCATTAAGGACCTTGTCCACTTGTCCCAC
AATATGCTGCATGGGGATGGCACAAACCGCTGGTTTGATAAATCCTTTAACCTCATTATC
GCCAAGGATGGCTCTACTGCCGTCCACTTTGAGCACTCTTGGGGTGATGGTGTGGCAGTG
CTCAGATTTTTTAATGAAGTATTTAAAGACAGCACTCAGACCCCTGCCGTCACTCCACAG
AGCCAGCCAGCTACCACTGACTCTACTGTCACGGTGCAGAAACTCAACTTCGAGCTGACT
GATGCCTTAAAGACTGGCATCACAGCTGCTAAGGAAAAGTTTGATGCCACCATGAAAACC
CTCACTATTGACTGCGTCCAGTTTCAGAGAGGAGGCAAAGAATTCCTGAAGAAGCAAAAG
CTGAGCCCTGACGCAGTTGCCCAGCTGGCATTCCAGATGGCCTTCCTGCGGCAGTACGGG
CAGACAGTGGCCACCTACGAGTCCTGTAGCACTGCCGCATTCAAGCACGGCCGCACTGAG
ACCATCCGCCCGGCCTCCGTCTATACAAAGAGGTGCTCTGAGGCCTTTGTCAGGGAGCCC
TCCAGGCACAGTGCTGGTGAGCTTCAGCAGATGATGGTTGAGTGCTCCAAGTACCATGGC
CAGCTGACCAAAGAAGCAGCAATGGGCCAGGGCTTTGACCGACACTTGTTTGCTCTGCGG
CATCTGGCAGCAGCCAAAGGGATCATCTTGCCTGAGCTCTACCTGGACCCTGCATACGGG
CAGATAAACCACAATGTCCTGTCCACGAGCACACTGAGCAGCCCAGCAGTGAACCTTGGG
GGCTTTGCCCCTGTGGTCTCTGATGGCTTTGGTGTTGGGTATGCTGTTCATGACAACTGG
ATAGGCTGCAATGTCTCTTCCTACCCAGGCCGCAATGCCCGGGAGTTTCTCCAATGTGTG
GAGAAGGCCTTAGAAGACATGTTTGATGCCTTAGAAGGCAAATCCATCAAAAGTTAA
Enzyme 2 GenBank Gene ID U09648 Link Image
Enzyme 2 GeneCard ID CPT2 Link Image
Enzyme 2 GenAtlas ID CPT2 Link Image
Enzyme 2 HGNC ID HGNC:2330 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p32
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Finocchiaro G, Taroni F, Rocchi M, Martin AL, Colombo I, Tarelli GT, DiDonato S: cDNA cloning, sequence analysis, and chromosomal localization of the gene for human carnitine palmitoyltransferase. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):661-5. [PubMed Link Image]
  2. Finocchiaro G, Taroni F, Rocchi M, Liras Martin A, Colombo I, Tarelli GT, DiDonato S: cDNA cloning, sequence analysis, and chromosomal localization of human carnitine palmitoyltransferase. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10981. [PubMed Link Image]
  3. Verderio E, Cavadini P, Montermini L, Wang H, Lamantea E, Finocchiaro G, DiDonato S, Gellera C, Taroni F: Carnitine palmitoyltransferase II deficiency: structure of the gene and characterization of two novel disease-causing mutations. Hum Mol Genet. 1995 Jan;4(1):19-29. [PubMed Link Image]
  4. Finocchiaro G, Colombo I, DiDonato S: Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver. FEBS Lett. 1990 Nov 12;274(1-2):163-6. [PubMed Link Image]
  5. Taroni F, Verderio E, Fiorucci S, Cavadini P, Finocchiaro G, Uziel G, Lamantea E, Gellera C, DiDonato S: Molecular characterization of inherited carnitine palmitoyltransferase II deficiency. Proc Natl Acad Sci U S A. 1992 Sep 15;89(18):8429-33. [PubMed Link Image]
  6. Taroni F, Verderio E, Dworzak F, Willems PJ, Cavadini P, DiDonato S: Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients. Nat Genet. 1993 Jul;4(3):314-20. [PubMed Link Image]
  7. Bonnefont JP, Taroni F, Cavadini P, Cepanec C, Brivet M, Saudubray JM, Leroux JP, Demaugre F: Molecular analysis of carnitine palmitoyltransferase II deficiency with hepatocardiomuscular expression. Am J Hum Genet. 1996 May;58(5):971-8. [PubMed Link Image]
  8. Wataya K, Akanuma J, Cavadini P, Aoki Y, Kure S, Invernizzi F, Yoshida I, Kira J, Taroni F, Matsubara Y, Narisawa K: Two CPT2 mutations in three Japanese patients with carnitine palmitoyltransferase II deficiency: functional analysis and association with polymorphic haplotypes and two clinical phenotypes. Hum Mutat. 1998;11(5):377-86. [PubMed Link Image]
  9. Taggart RT, Smail D, Apolito C, Vladutiu GD: Novel mutations associated with carnitine palmitoyltransferase II deficiency. Hum Mutat. 1999;13(3):210-20. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8300
Enzyme 3 Name Mitochondrial carnitine/acylcarnitine carrier protein
Enzyme 3 Synonyms
  1. Carnitine/acylcarnitine translocase
  2. CAC
  3. Solute carrier family 25 member 20
Enzyme 3 Gene Name SLC25A20
Enzyme 3 Protein Sequence >Mitochondrial carnitine/acylcarnitine carrier protein 
MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFR
KTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLS
GVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDV
PASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTA
PPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPN
L
Enzyme 3 Number of Residues 301
Enzyme 3 Molecular Weight 32944
Enzyme 3 Theoretical pI 9.84
Enzyme 3 GO Classification
Function
  • binding
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
  • mitochondrial inner membrane
  • organelle inner membrane
  • organelle membrane
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Mediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fatty acid-oxidation pathway
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 13-31 74-93 113-131 171-190 212-230 268-287
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2765075 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O43772 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name MCAT_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >906 bp 
ATGGCCGACCAGCCAAAACCCATCAGCCCGCTCAAGAACCTGCTGGCCGGCGGCTTTGGC
GGCGTGTGCCTGGTGTTCGTCGGTCACCCTCTGGACACGGTCAAGGTCCGACTGCAGACA
CAGCCACCGAGTTTGCCTGGACAACCTCCCATGTACTCTGGGACCTTTGACTGTTTCCGG
AAGACTCTTTTTAGAGAGGGCATCACGGGGCTATATCGGGGAATGGCTGCCCCTATCATC
GGGGTCACTCCCATGTTTGCCGTGTGCTTCTTTGGGTTTGGTTTGGGGAAGAAACTACAA
CAGAAACACCCAGAAGATGTGCTCAGCTATCCCCAGCTTTTTGCAGCTGGGATGTTATCT
GGCGTATTCACCACAGGAATCATGACTCCTGGAGAACGGATCAAGTGCTTATTACAGATT
CAGGCTTCTTCAGGAGAAAGCAAGTACACTGGTACCTTGGACTGTGCAAAGAAGCTGTAC
CAGGAGTTTGGGATCCGAGGCATCTACAAAGGGACTGTGCTTACCCTTATGCGAGATGTC
CCAGCTAGTGGAATGTATTTCATGACATATGAATGGCTGAAAAATATCTTCACTCCGGAG
GGAAAGAGGGTCAGTGAGCTCAGTGCCCCTCGGATCTTGGTGGCTGGGGGCATTGCAGGG
ATCTTCAACTGGGCTGTGGCAATCCCCCCAGATGTGCTCAAGTCTCGATTCCAGACTGCA
CCTCCTGGGAAATATCCTAATGGTTTCAGAGATGTGCTGAGGGAGCTGATCCGGGATGAA
GGAGTCACATCCTTGTACAAAGGGTTCAATGCAGTGATGATCCGAGCCTTCCCAGCCAAT
GCGGCCTGTTTCCTTGGCTTTGAAGTTGCCATGAAGTTCCTTAATTGGGCCACCCCCAAC
TTGTGA
Enzyme 3 GenBank Gene ID Y10319 Link Image
Enzyme 3 GeneCard ID SLC25A20 Link Image
Enzyme 3 GenAtlas ID SLC25A20 Link Image
Enzyme 3 HGNC ID HGNC:1421 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3p21.31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Huizing M, Iacobazzi V, Ijlst L, Savelkoul P, Ruitenbeek W, van den Heuvel L, Indiveri C, Smeitink J, Trijbels F, Wanders R, Palmieri F: Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient. Am J Hum Genet. 1997 Dec;61(6):1239-45. [PubMed Link Image]
  2. Iacobazzi V, Naglieri MA, Stanley CA, Wanders RJ, Palmieri F: The structure and organization of the human carnitine/acylcarnitine translocase (CACT1) gene2. Biochem Biophys Res Commun. 1998 Nov 27;252(3):770-4. [PubMed Link Image]
  3. Al Aqeel AI, Rashid MS, Ruiter JP, Ijlst L, Wanders RJ: A novel molecular defect of the carnitine acylcarnitine translocase gene in a Saudi patient. Clin Genet. 2003 Aug;64(2):163-5. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 9777
Enzyme 4 Name Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
Enzyme 4 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 1
  2. Middle-chain acyl- CoA synthetase 1
  3. Butyrate--CoA ligase 1
  4. Butyryl coenzyme A synthetase 1
  5. Lipoate-activating enzyme
Enzyme 4 Gene Name ACSM1
Enzyme 4 Protein Sequence >Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor 
MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWA
QKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPR
VPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCP
SLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH
GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK
VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG
LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRI
KPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG
PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV
TAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM
Enzyme 4 Number of Residues 577
Enzyme 4 Molecular Weight 65274
Enzyme 4 Theoretical pI Not Available
Enzyme 4 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). Functions as GTP-dependent lipoate- activating enzyme that generates the substrate for lipoyltransferase
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + Butyrate (n-C4:0) + Coenzyme A --> AMP + Butanoyl-CoA + Diphosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 15487302 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q08AH1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ACSM1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AB059429 Link Image
Enzyme 4 GeneCard ID Not Available
Enzyme 4 GenAtlas ID ACSM1 Link Image
Enzyme 4 HGNC ID HGNC:18049 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Fujino T, Takei YA, Sone H, Ioka RX, Kamataki A, Magoori K, Takahashi S, Sakai J, Yamamoto TT: Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J Biol Chem. 2001 Sep 21;276(38):35961-6. Epub 2001 Jul 24. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14011
Enzyme 5 Name Uncharacterized protein C10orf129
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name C10orf129
Enzyme 5 Protein Sequence >Uncharacterized protein C10orf129 
VANEAMAPVVNSAVSDCPTLKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMA
IFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGT
WFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCV
AAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIV
DENSNLLPPGEEGNIAIRIKLNQPASLYCPHMVSWEEYASARGHMLYLTGDRGIMDEDGY
FWWSGRVDDVANALGQRL
Enzyme 5 Number of Residues 318
Enzyme 5 Molecular Weight 35252
Enzyme 5 Theoretical pI 7.30
Enzyme 5 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Lipid transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 39645901 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q6P461 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q6P461_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >957 bp 
GTGGCTAATGAAGCTATGGCCCCAGTTGTAAACTCTGCCGTGTCCGACTGCCCCACCTTG
AAAACCAAGCTCCTGGTGTCAGATAAGAGCTATGATGGGTGGTTGGATTTCAAGAAGTTG
ATTCAAGTTGCCCCTCCAAAGCAGACCTACATGAGGACCAAAAGCCAAGATCCAATGGCC
ATATTCTTCACCAAGGGTACAACAGGAGCTCCCAAAATGGTCGAGTATTCCCAGTATGGT
TTGGGAATGGGATTCAGCCAGGCTTCCAGACGGTGGATGGATCTCCAGCCAACAGATGTC
TTGTGGAGTCTGGGTGATGCCTTTGGTGGATCTTTATCCCTGAGCGCTGTCTTGGGAACT
TGGTTCCAAGGAGCCTGTGTGTTTCTGTGTCACATGCCAACCTTCTGCCCTGAGACTGTT
CTAAATGTCCTGTCCAGATTTCCCATCACCACTCTATCTGCAAATCCAGAGATGTACCAG
GAACTGCTTCAGCACAAGTGTTTCACCAGCTACAGATTCAAGAGTCTGAAGCAGTGTGTG
GCTGCAGGAGGACCCATCAGCCCTGGGGTGATTGAGGACTGGAAACGCATCACTAAGTTG
GACATCTATGAAGGCTATGGGCAGACGGAAACTGGTCTACTCTGTGCCACTTCCAAAACA
ATAAAATTGAAGCCAAGCTCTCTGGGGAAGCCATTGCCACCTTATATTGTCCAGATTGTG
GATGAAAACTCAAATCTCCTGCCTCCAGGGGAAGAAGGAAATATTGCAATCCGCATAAAA
CTAAACCAACCTGCTTCTCTGTACTGTCCACACATGGTGAGCTGGGAGGAATATGCTTCA
GCAAGAGGCCACATGCTTTACCTCACAGGTGACAGAGGGATCATGGATGAAGACGGCTAC
TTCTGGTGGTCTGGTAGAGTTGATGATGTTGCCAATGCATTGGGTCAGAGATTGTGA
Enzyme 5 GenBank Gene ID BC063654 Link Image
Enzyme 5 GeneCard ID Q6P461 Link Image
Enzyme 5 GenAtlas ID ACSM6 Link Image
Enzyme 5 HGNC ID HGNC:31665 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q23.33
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 14420
Enzyme 6 Name Acyl-coenzyme A synthetase ACSM2A, mitochondrial precursor
Enzyme 6 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 2A
  2. Middle-chain acyl-CoA synthetase 2A
  3. Butyrate--CoA ligase 2A
  4. Butyryl coenzyme A synthetase 2A
Enzyme 6 Gene Name ACSM2A
Enzyme 6 Protein Sequence >Acyl-coenzyme A synthetase ACSM2A, mitochondrial precursor 
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN
ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ
Enzyme 6 Number of Residues 577
Enzyme 6 Molecular Weight 64225
Enzyme 6 Theoretical pI 8.05
Enzyme 6 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro)
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389] ALL_REAC R00389 > R01176
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-19
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 115528937 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q08AH3 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ACS2A_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1734 bp 
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTG
CCGGCCAAGTTTAACTTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGGTGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCTTTATGCCTGGAACCATCCAGATG
AAATCCACTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGTGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGTGCTCACTTATGGAACCTTGGGCATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCCATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCGTCACTGTAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATCC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGATCATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGACAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGGAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGGTCCTGGCCTCGCAGTTCCTGTCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
GCCAAGCTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
Enzyme 6 GenBank Gene ID BC125176 Link Image
Enzyme 6 GeneCard ID Q08AH3 Link Image
Enzyme 6 GenAtlas ID ACSM2A Link Image
Enzyme 6 HGNC ID HGNC:32017 Link Image
Enzyme 6 Chromosome Location 16
Enzyme 6 Locus 16p12.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 14421
Enzyme 7 Name Acyl-coenzyme A synthetase ACSM2B, mitochondrial precursor
Enzyme 7 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 2B
  2. Middle-chain acyl-CoA synthetase 2B
  3. Butyrate--CoA ligase 2B
  4. Butyryl coenzyme A synthetase 2B
  5. Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A
Enzyme 7 Gene Name ACSM2B
Enzyme 7 Protein Sequence >Acyl-coenzyme A synthetase ACSM2B, mitochondrial precursor 
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVMLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN
ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGKARAQ
Enzyme 7 Number of Residues 577
Enzyme 7 Molecular Weight 64258
Enzyme 7 Theoretical pI 8.38
Enzyme 7 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Lipid transport and metabolism
Enzyme 7 Specific Function Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389] ALL_REAC R00389 > R01176
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-19
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 27651993 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q68CK6 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ACS2B_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1734 bp 
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTG
CCGGCCAAGTTTAACCTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGATGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCATTATGCCTGAAACCATCCAGATG
AAATCCGCTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGCGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGGGCTCACTTTTGGAATCTTGGACATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCTATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCCTCGCTGGAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATTC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGGTTATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGAAAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGAAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGATACTGGCCTCGCAGTTCCTATCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
ACCAAACTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
Enzyme 7 GenBank Gene ID AY160217 Link Image
Enzyme 7 GeneCard ID Q68CK6 Link Image
Enzyme 7 GenAtlas ID ACSM2B Link Image
Enzyme 7 HGNC ID HGNC:30931 Link Image
Enzyme 7 Chromosome Location 16
Enzyme 7 Locus 16p12.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 14422
Enzyme 8 Name Acyl-coenzyme A synthetase ACSM3, mitochondrial precursor
Enzyme 8 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 3
  2. Middle-chain acyl- CoA synthetase 3
  3. Butyrate--CoA ligase 3
  4. Butyryl coenzyme A synthetase 3
  5. Protein SA homolog
Enzyme 8 Gene Name ACSM3
Enzyme 8 Protein Sequence >Acyl-coenzyme A synthetase ACSM3, mitochondrial precursor 
MLARVTRKMLRHAKCFQRLAIFGSVRALHKDNRTATPQNFSNYESMKQDFKLGIPEYFNF
AKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRG
DRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPA
VDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSG
YPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFT
HHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDV
TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPG
QEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDV
ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIK
EIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKTI
Enzyme 8 Number of Residues 586
Enzyme 8 Molecular Weight 66153
Enzyme 8 Theoretical pI 9.45
Enzyme 8 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Lipid transport and metabolism
Enzyme 8 Specific Function Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro)
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389] ALL_REAC R00389 > R01176
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 666014 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q53FZ2 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ACSM3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1737 bp 
ATGCTACGTCATGCCAAGTGTTTTCAGCGCCTAGCAATTTTTGGTTCTGTGAGGGCACTG
CATAAAGATAATAGAACAGCAACCCCTCAGAATTTCTCCAACTATGAATCCATGAAACAG
GACTTCAAACTGGGGATTCCAGAGTATTTCAACTTTGCTAAAGATGTCCTGGACCAATGG
ACTGATAAGGAAAAGGCTGGAAAGAAACCTTCAAATCCAGCCTTCTGGTGGATCAACAGA
AATGGAGAAGAGATGCGATGGAGTTTTGAGGAACTGGGATCTCTGTCCAGAAAATTTGCC
AATATACTTTCAGAAGCCTGTTCCCTACAAAGAGGAGATCGGGTAATTCTGATTCTGCCC
AGGGTCCCGAGATGGTGGCTTGCAAATGTGGCCTGTCTGCGAACAGGGACAGTTTTAATT
CCAGGAACCACTCAGCTGACCCAGAAAGACATTCTCTACAGACTACAATCTTCAAAAGCA
AACTGCATTATCACCAATGATGTTTTAGCCCCAGCAGTAGACGCTGTTGCATCCAAATGT
GAAAATCTGCACTCCAAGCTGATTGTATCAGAGAACTCCAGAGAGGGGTGGGGGAACCTC
AAGGAGTTGATGAAACATGCCAGTGACAGCCACACCTGTGTGAAGACAAAACACAATGAG
ATCATGGCCATATTCTTTACCAGTGCAACAAGTGGATATCCGAAAATGTCTGCACACACC
CACAGCAGTTTTGGTTTAGGTTTATCTGTAAATGGAAGGTTCTGGCTAGATTTGACACCC
TCAGATGTGATGTGGAATACCTCAGATACGGGCTGGGCAAAGTCTGCATGGAGTAGTGTT
TTTTCTCCGTGGATCCAGGGAGCATGTGTATTCACACACCATTTACCCCGTTTTGAGCCG
ACTTCTATCTTGCAAACACTCTCCAAGTACCCCATCACAGTCTTCTGTTCAGCACCAACT
GTATACCGAATGCTTGTACAGAATGATATAACCAGCTATAAGTTTAAAAGCTTAAAGCAC
TGTGTGAGTGCTGGGGAACCAATTACCCCTGACGTGACTGAAAAATGGAGAAACAAGACG
GGCCTGGATATCTACGAAGGATATGGACAGACTGAAACGGTGCTAATCTGTGGAAATTTT
AAGGGAATGAAAATTAAACCTGGCTCAATGGGAAAACCTTCTCCTGCTTTCGATGTTAAG
ATTGTAGATGTAAATGGCAATGTTCTACCTCCTGGACAAGAAGGAGATATTGGCATTCAA
GTTCTACCCAACCGACCATTTGGCCTTTTTACTCATTACGTAGATAATCCTTCAAAAACA
GCTTCAACTCTACGAGGCAATTTCTATATCACTGGGGACAGAGCATATATGGATAAAGAT
GGGTATTTCTGGTTTGTTGCAAGAGCAGATGATGTCATATTATCCTCTGGCTATCGAATT
GGACCATTTGAGGTAGAAAATGCCCTGAATGAACACCCTTCAGTTGCAGAGTCAGCTGTT
GTCAGCAGCCCAGACCCCATCAGAGGAGAGGTAGTAAAGGCTTTTGTCGTTCTAAATCCT
GATTACAAGTCACATGATCAAGAACAACTAATAAAGGAGATTCAGGAGCATGTTAAAAAA
ACTACAGCACCTTACAAATATCCCAGAAAGGTAGAATTTATTCAAGAGCTGCCAAAGACT
GTCAGTGGGAAGACAAAAAGAAATGAACTGAGGAAGAAAGAATGGAAGACAATTTAA
Enzyme 8 GenBank Gene ID D16350 Link Image
Enzyme 8 GeneCard ID Q53FZ2 Link Image
Enzyme 8 GenAtlas ID ACSM3 Link Image
Enzyme 8 HGNC ID HGNC:10522 Link Image
Enzyme 8 Chromosome Location 16
Enzyme 8 Locus 16p13.11
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Iwai N, Ohmichi N, Hanai K, Nakamura Y, Kinoshita M: Human SA gene locus as a candidate locus for essential hypertension. Hypertension. 1994 Mar;23(3):375-80. [PubMed Link Image]
  2. Nabika T, Bonnardeaux A, James M, Julier C, Jeunemaitre X, Corvol P, Lathrop M, Soubrier F: Evaluation of the SA locus in human hypertension. Hypertension. 1995 Jan;25(1):6-13. [PubMed Link Image]
  3. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 14424
Enzyme 9 Name Acyl-coenzyme A synthetase ACSM5, mitochondrial precursor
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name ACSM5
Enzyme 9 Protein Sequence >Acyl-coenzyme A synthetase ACSM5, mitochondrial precursor 
MRPWLRHLVLQALRNSRAFCGSHGKPAPLPVPQKIVATWEAISLGRQLVPEYFNFAHDVL
DVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMML
VLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAIS
AECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMV
EHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRV
DAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKH
QTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVA
VRIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSY
RIGPVEVESALAEHPAVLESAAVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRELQEHV
KRVTAPYKYPRKVAFVSELPKTVSGKIQRSKLRSQEWGK
Enzyme 9 Number of Residues 579
Enzyme 9 Molecular Weight 64733
Enzyme 9 Theoretical pI 8.52
Enzyme 9 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 9 General Function Lipid transport and metabolism
Enzyme 9 Specific Function Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro)
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389] ALL_REAC R00389 > R01176
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 7020785 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q6NUN0 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ACSM5_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1716 bp 
ATGAGACCATGGCTGAGACACCTAGTCCTCCAGGCACTGAGGAACTCCAGGGCATTCTGT
GGGTCTCATGGGAAGCCAGCACCTCTACCTGTTCCTCAGAAGATCGTGGCCACCTGGGAA
GCCATCAGCCTGGGAAGGCAGCTGGTGCCTGAGTACTTCAACTTCGCCCATGATGTGCTG
GATGTGTGGAGTCGGCTGGAAGAGGCTGGACACCGCCCCCCAAATCCTGCCTTCTGGTGG
GTCAATGGCACAGGAGCAGAGATCAAGTGGAGCTTTGAGGAGCTGGGGAAGCAGTCCAGG
AAGGCAGCCAATGTGCTGGGGGGTGCATGCGGCCTGCAGCCTGGGGACAGAATGATGCTG
GTACTCCCACGGCTCCCGGAGTGGTGGCTGGTCAGTGTGGCTTGCATGCGGACAGGGACT
GTGATGATTCCGGGTGTGACTCAGCTGACAGAGAAGGACCTCAAGTACCGGCTGCAGGCG
TCCAGGGCCAAGTCCATTATCACCAGTGACTCCCTAGCTCCAAGGGTGGATGCCATCAGT
GCCGAATGCCCCTCCCTCCAGACCAAGCTGCTGGTGTCAGACAGCAGTCGGCCAGGCTGG
TTGAACTTCAGGGAACTCCTCCGGGAGGCTTCTACAGAGCACAACTGCATGAGGACAAAG
AGTCGAGACCCGCTGGCCATCTACTTTACCAAGCGGGAACCACCGGGGGCCCCCAAGATG
GTCGAGCACTCCCAGAGCAGCTACGGACTGGGTTTTGTGGCCAGCGGAAGACGGTGGGTG
GCCTTGACCGAATCTGACATCTTCTGGAACACGACTGACACTGGCTGGGTGAAGGCAGCC
TGGACTCTCTTCTCTGCCTGGCCTAATGGATCTTGCATTTTTGTGCATGAGCTGCCCCGA
GTTGATGCCAAAGTTATCCTGAATACTCTCTCCAAATTCCCGATAACCACCCTCTGCTGT
GTCCCAACCATCTTTCGGCTGCTTGTGCAGGAGGATCTGACCAGGTACCAGTTTCAGAGC
TTGAGGCACTGTCTGACCGGAGGAGAGGCCCTCAACCCTGACGTGAGGGAGAAGTGGAAA
CACCAGACTGGTGTGGAGCTGTACGAAGGCTATGGCCAGTCTGAAACGGTTGTCATCTGT
GCCAATCCAAAAGGCATGAAAATCAAGTCTGGATCCATGGGGAAGGCGTCCCCACCCTAC
GATGTGCAGATTGTGGATGATGAGGGCAACGTCCTGCCTCCTGGAGAAGAGGGGAATGTT
GCTGTCCGTATCAGACCCACTCGGCCCTTCTGTTTCTTCAATTGCTATTTGGACAATCCT
GAGAAGACAGCTGCATCAGAACAAGGGGACTTTTACATCACAGGGGACCGAGCTCGCATG
GACAAGGATGGCTACTTTTGGTTCATGGGAAGAAACGACGATGTGATCAATTCTTCAAGC
TACCGGATCGGGCCTGTTGAAGTGGAAAGTGCCCTGGCAGAGCATCCTGCTGTCCTGGAG
TCGGCTGTGGTCAGCAGCCCAGACCCCATCAGGGGAGAGGTGGTAAAGGCATTTATAGTC
CTTACTCCAGCCTACTCCTCTCATGACCCAGAGGCACTAACGCGGGAACTCCAGGAGCAT
GTGAAAAGGGTGACTGCTCCATACAAATACCCCAGGAAGGTGGCCTTTGTTTCAGAACTT
GCCAAAGACGGTTTCTGGAAAGATCCAAAGGAGTAA
Enzyme 9 GenBank Gene ID AK000588 Link Image
Enzyme 9 GeneCard ID Q6NUN0 Link Image
Enzyme 9 GenAtlas ID ACSM5 Link Image
Enzyme 9 HGNC ID HGNC:26060 Link Image
Enzyme 9 Chromosome Location 16
Enzyme 9 Locus 16p12.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 14869
Enzyme 10 Name Not Available
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name ACSM4
Enzyme 10 Protein Sequence >MKIFFRYQTFRFIWLTKPPGRRLHKDHQLWTPLTLADFEAINRCNRPLPKNFNFAADVLDQWSQKEKTGE 
RPANPALWWVNGKGDEVKWSFRELGSLSRKAANVLTKPCGLQRGDRLAVILPRIPEWWLV
NVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLL
VSPQSWNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGF
TLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLT
TYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRVQTGLELYEGY
GQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPFC
FFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESA
LIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKLTLELQDHVKKSTAPYKYP
RKVEFVQELPKTITGKIKRNVLRDQEWRGR
Enzyme 10 Number of Residues 580
Enzyme 10 Molecular Weight 65703
Enzyme 10 Theoretical pI 8.76
Enzyme 10 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro)
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID P0C7M7 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ACSM4_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AC131205 Link Image
Enzyme 10 GeneCard ID P0C7M7 Link Image
Enzyme 10 GenAtlas ID ACSM4 Link Image
Enzyme 10 HGNC ID HGNC:32016 Link Image
Enzyme 10 Chromosome Location 12
Enzyme 10 Locus 12p13.31
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available