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Human Metabolome Database Version 2.5

 

Showing metabocard for (S)-Hydroxyhexanoyl-CoA (HMDB03942)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 08:49:56
Update Date 2009-05-05 20:59:55
Accession Number HMDB03942
Secondary Accession Numbers Not Available
Common Name (S)-Hydroxyhexanoyl-CoA
Description (S)-Hydroxyhexanoyl-CoA is an intermediate in fatty acid metabolism, being the substrate of the enzymes beta-hydroxyacyl-CoA dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase [EC 1.1.1.211-1.1.1.35]; (S)-Hydroxyhexanoyl-CoA is an intermediate in fatty acid elongation in mitochondria, the substrate of the enzymes enoyl-CoA hydratase and long-chain-enoyl-CoA hydratase [EC 4.2.1.17-4.2.1.74]. (KEGG)
Synonyms
  1. [R,S]-Lactyl CoA
  2. S-(3-hydroxyhexanoate)Coenzyme A
  3. (S)-3-Hydroxyhexanoyl-CoA
  4. (S)-3-Hydroxyhexanoyl-Coenzyme A
  5. [R,S]-Lactyl Coenzyme A
  6. S-(3-hydroxyhexanoate)CoA
  7. S-(3-hydroxyhexanoic acid
  8. S-(3-hydroxyhexanoate
Chemical IUPAC Name S-[2-[3-[[4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] (3S)-3-hydroxyhexanethioate
Chemical Formula C27H46N7O18P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Short chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • secondary carboxylic acid amide
  • thiocarboxylic acid ester
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Lipid biosynthesis, Fatty acid transport
Application
—
Source
  • Endogenous
Average Molecular Weight 881.677
Monoisotopic Molecular Weight 881.183289
Isomeric SMILES CCC[C@H](O)CC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12
Canonical SMILES CCCC(O)CC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12
KEGG Compound ID C05268 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB03942 Link Image
Metagene Link HMDB03942 Link Image
METLIN ID Not Available
PubChem Compound 440609 Link Image
PubChem Substance 7655 Link Image
ChEBI ID 28276 Link Image
CAS Registry Number 74875-70-0
InChI Identifier InChI=1/C27H46N7O18P3S/c1-4-5-15(35)10-18(37)56-9-8-29-17(36)6-7-30-25(40)22(39)27(2,3)12-49-55(46,47)52-54(44,45)48-11-16-21(51-53(41,42)43)20(38)26(50-16)34-14-33-19-23(28)31-13-32-24(19)34/h13-16,20-22,26,35,38-39H,4-12H2,1-3H3,(H,29,36)(H,30,40)(H,44,45)(H,46,47)(H2,28,31,32)(H2,41,42,43)/t15-,16+,20+,21+,22?,26+/m0/s1
Synthesis Reference Tamvakopoulos, Constantine S.; Anderson, Vernon E. Detection of acyl-coenzyme A thioester intermediates of fatty acid b-oxidation as the N-acylglycines by negative-ion chemical ionization gas chromatography mass spectrometry. Analytical Biochemistry
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.71 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity -3.019 Source: PhysProp
Predicted LogP/Hydrophobicity -0.28 [Predicted by ALOGPS]; -5.6 [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 Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Fatty Acid Elongation In Mitochondria SMP00054 Link Image map00062 Link Image
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids SMP00480 Link Image
General References
  1. Dalluge JJ, Gort S, Hobson R, Selifonova O, Amore F, Gokarn R: Separation and identification of organic acid-coenzyme A thioesters using liquid chromatography/electrospray ionization-mass spectrometry. Anal Bioanal Chem. 2002 Nov;374(5):835-40. Epub 2002 Oct 8. [PubMed Link Image]
  2. Klees AG, Linder D, Buckel W: 2-Hydroxyglutaryl-CoA dehydratase from Fusobacterium nucleatum (subsp. nucleatum): an iron-sulfur flavoprotein. Arch Microbiol. 1992;158(4):294-301. [PubMed Link Image]
  3. Kim J, Hetzel M, Boiangiu CD, Buckel W: Dehydration of (R)-2-hydroxyacyl-CoA to enoyl-CoA in the fermentation of alpha-amino acids by anaerobic bacteria. FEMS Microbiol Rev. 2004 Oct;28(4):455-68. [PubMed Link Image]
  4. Hofmeister AE, Buckel W: (R)-lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA. Eur J Biochem. 1992 Jun 1;206(2):547-52. [PubMed Link Image]
  5. Kuchta RD, Hanson GR, Holmquist B, Abeles RH: Fe-S centers in lactyl-CoA dehydratase. Biochemistry. 1986 Nov 18;25(23):7301-7. [PubMed Link Image]
  6. Kuchta RD, Abeles RH: Lactate reduction in Clostridium propionicum. Purification and properties of lactyl-CoA dehydratase. J Biol Chem. 1985 Oct 25;260(24):13181-9. [PubMed Link Image]
  7. Sokatch JR: Alanine and aspartate formation during growth on valine-C14 by Pseudomonas aeruginosa. J Bacteriol. 1966 Jul;92(1):72-5. [PubMed Link Image]
  8. Megraw RE, Reeves HC, Ajl SJ: Formation of lactyl-coenzyme A and pyruvyl-coenzyme A from lactic acid by Escherichia coli. J Bacteriol. 1965 Oct;90(4):984-8. [PubMed Link Image]
Metabolic Enzymes
  1. Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial precursor
  2. Enoyl-CoA hydratase, mitochondrial precursor
  3. Trifunctional enzyme subunit alpha, mitochondrial precursor
  4. Peroxisomal multifunctional enzyme type 2
  5. Hydroxyacyl-Coenzyme A dehydrogenase, type II
  6. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
  7. Putative uncharacterized protein
Enzyme 1 [top]
Enzyme 1 ID 5618
Enzyme 1 Name Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial precursor
Enzyme 1 Synonyms
  1. Short chain 3-hydroxyacyl-CoA dehydrogenase
  2. HCDH
  3. Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Enzyme 1 Gene Name HADH
Enzyme 1 Protein Sequence >Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial precursor 
MAFVTRQFMRSVSSSSTASASAKKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTE
DILAKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAI
VENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKL
VEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDAS
KEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAEN
KFGKKTGEGFYKYK
Enzyme 1 Number of Residues 314
Enzyme 1 Molecular Weight 34278
Enzyme 1 Theoretical pI 9.41
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Plays an essential role in the mitochondrial beta- oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1483511 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16836 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HCDH_HUMAN Link Image
Enzyme 1 PDB ID 1F0Y Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >945 bp 
ATGGCCTTCGTCACCAGGCAGTTCATGCGTTCCGTGTCCTCCTCGTCCACCGCCTCGGCC
TCGGCCAAGAAGATAATCGTCAAGCACGTGACGGTCATCGGCGGCGGGCTGATGGGCGCC
GGCATTGCCCAGGTTGCTGCAGCAACTGGTCACACAGTAGTGTTGGTAGACCAGACAGAG
GACATCCTGGCAAAATCCAAAAAGGGAATTGAGGAAAGCCTTAGGAAAGTGGCAAAGAAG
AAGTTTGCAGAAAACCCTAAGGCCGGCGATGAATTTGTGGAGAAGACCCTGAGCACCATA
GCGACCAGCACGGATGCAGCCTCCGTTGTCCACAGCACAGACTTGGTGGTGGAAGCCATC
GTGGAGAATCTGAAGGTGAAAAACGAGCTCTTCAAAAGGCTGGACAAGTTTGCTGCTGAA
CATACAATCTTTGCCAGCAACACTTCCTCCTTGCATATTACAAGCATAGCTAATGCCACC
ACCAGACAAGACCGATTCGCTGGCCTCCATTTCTTCAACCCAGTGCCTGTCATGAAACTT
GTGGAGGTCATTAAAACACCAATGACCAGCCAGAAGACATTTGAATCTTTGGTAGACTTT
AGCAAAGCCCTAGGAAAGCATCCTGTTTCTTGCAAGGACACTCCTGGGTTTATTGTGAAC
CGCCTCCTGGTTCCATACCTCATGGAAGCAATCAGGCTGTATGAACGAGGTGACGCATCC
AAAGAAGACATTGACACTGCTATGAAATTAGGAGCCGGTTACCCCATGGGCCCATTTGAG
CTTCTAGATTATGTCGGACTGGATACTACGAAGTTCATCGTGGATGGGTGGCATGAAATG
GATGCAGAGAACCCATTACATCAGCCCAGCCCATCCTTAAATAAGCTGGTAGCAGAGAAC
AAGTTCGGCAAGAAGACTGGAGAAGGATTTTACAAATACAAGTGA
Enzyme 1 GenBank Gene ID X96752 Link Image
Enzyme 1 GeneCard ID HADH Link Image
Enzyme 1 GenAtlas ID HADH Link Image
Enzyme 1 HGNC ID HGNC:4799 Link Image
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4q22-q26
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Vredendaal PJ, van den Berg IE, Malingre HE, Stroobants AK, Olde Weghuis DE, Berger R: Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence. Biochem Biophys Res Commun. 1996 Jun 25;223(3):718-23. [PubMed Link Image]
  2. Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, Banaszak LJ: Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism. Biochemistry. 1999 May 4;38(18):5786-98. [PubMed Link Image]
  3. Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ: Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J Biol Chem. 2000 Sep 1;275(35):27186-96. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5625
Enzyme 2 Name Enoyl-CoA hydratase, mitochondrial precursor
Enzyme 2 Synonyms
  1. Short chain enoyl-CoA hydratase
  2. SCEH
  3. Enoyl-CoA hydratase 1
Enzyme 2 Gene Name ECHS1
Enzyme 2 Protein Sequence >Enoyl-CoA hydratase, mitochondrial precursor 
MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNA
LCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHW
DHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLT
RAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMA
KESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
Enzyme 2 Number of Residues 290
Enzyme 2 Molecular Weight 31388
Enzyme 2 Theoretical pI 8.19
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-17
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 433413 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P30084 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ECHM_HUMAN Link Image
Enzyme 2 PDB ID 2DUB Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >873 bp 
ATGGCCGCCCTGCGTGTCCTGCTGTCCTGCGCCCGCGGCCCGCTGAGGCCCCCGGTTCGC
TGTCCCGCCTGGCGTCCCTTCGCCTCGGGTGCTAACTTTGAGTACATCATCGCAGAAAAA
AGAGGGAAGAATAACACCGTGGGGTTGATCCAACTGAACCGCCCCAAGGCCCTCAATGCA
CTTTGCGATGGCCTGATTGACGAGCTCAACCAGGCCCTGAAGATCTTCGAGGAGGACCCG
GCCGTTGGGGGCATTGTCCTCACCGGCGGGGATAAGGCCTTTGCAGCTGGAGCTGATATC
AAGGAAATGCAGAACCTGAGTTTCCAGGACTGTTACTCCAGCAAGTTCTTGAAGCACTGG
GGCCACCTCACCCAGGTCAAGAAGCCAGTCATCGCTGCTGTCAATGGCTATCCGTTTGGC
GGGGGCTGTGAGCTTGCCATGATGTGTGATATCATCTATGCCGGTGAGAAGGCCCAGTTT
GCACAGCCGGAGATCTTAATAGGAACCATCCCAGGTGCAGGCGGCACCCAGAGACTCACC
CGTGCTGTTGGGAAGTCGCTGGAGCTGGAGATGGTCCTCACCGGTGACGCGATCTCAGCC
CAGGACGCCAAGCAAGCAGGTCTTGTCAGCAAGATTTGTCCTGTTGAGACACTGGTGGAA
GAAGCCATCCAGTGTGCAGAAAAAATTGCCAGCAATTCTAAAATTGTAGTAGCGATGGCC
AAAGAATCAGTGAATGCAGCTTTTGAAATGACATTAACAGAAGGAAGTAAGTTGGAGAAG
AAACTCTTTTATTCAACCTTTGCCACTGATGACCGGAAAGAAGGGATGACCGCGTTTGTG
GAAAAGAGAAAGGCCAACTTCAAAGACCAGTGA
Enzyme 2 GenBank Gene ID D13900 Link Image
Enzyme 2 GeneCard ID ECHS1 Link Image
Enzyme 2 GenAtlas ID ECHS1 Link Image
Enzyme 2 HGNC ID HGNC:3151 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q26.2-q26.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kanazawa M, Ohtake A, Abe H, Yamamoto S, Satoh Y, Takayanagi M, Niimi H, Mori M, Hashimoto T: Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase. Enzyme Protein. 1993;47(1):9-13. [PubMed Link Image]
  2. Janssen U, Davis EM, Le Beau MM, Stoffel W: Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3. Genomics. 1997 Mar 15;40(3):470-5. [PubMed Link Image]
  3. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  4. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5626
Enzyme 3 Name Trifunctional enzyme subunit alpha, mitochondrial precursor
Enzyme 3 Synonyms
  1. TP-alpha
  2. 78 kDa gastrin-binding protein[Includes: Long-chain enoyl-CoA hydratase
Enzyme 3 Gene Name HADHA
Enzyme 3 Protein Sequence >Trifunctional enzyme subunit alpha, mitochondrial precursor 
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 3 Number of Residues 763
Enzyme 3 Molecular Weight 83001
Enzyme 3 Theoretical pI 9.52
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Bifunctional subunit
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-23
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 862457 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P40939 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ECHA_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2292 bp 
ATGGTGGCCTGCCGGGCGATTGGCATCCTCAGCCGCTTTTCTGCCTTCAGGATCCTCCGC
TCCCGAGGTTATATATGCCGCAATTTTACAGGGTCTTCTGCTTTGCTGACCAGAACCCAT
ATTAACTATGGAGTCAAAGGGGATGTGGCAGTTGTTCGAATTAACTCTCCCAATTCAAAG
GTAAATACACTGAGTAAAGAGCTACATTCAGAGTTCTCAGAAGTTATGAATGAAATCTGG
GCTAGTGATCAAATCAGAAGTGCCGTCCTTATCTCATCAAAGCCAGGCTGCTTTATTGCA
GGTGCTGATATCAACATGTTAGCCGCTTGCAAGACCCTTCAAGAAGTAACACAGCTATCA
CAAGAAGCACAGAGAATAGTTGAGAAACTTGAAAAGTCCACAAAGCCTATTGTGGCTGCC
ATCAATGGATCCTGCGTGGGAGGAGGACTTGAGGTTGCCATTTCATGCCAATACAGAATA
GCAACAAAAGACAGAAAAACAGTATTAGGTACCCCTGAAGTTTTGCTGGGGGCCTTACCA
GGAGCAGGAGGCACACAAAGGCTGCCCAAAATGGTGGGTGTGCCTGCTGCTTTGGACATG
ATGCTGACTGGTAGAAGCATTCGTGCAGACAGGGCAAAGAAAATGGGACTGGTTGACCAA
CTGGTGGAACCCCTGGGACCAGGACTAAAACCTCCAGAGGAACGGACAATAGAATACCTA
GAAGAAGTTGCAATTACTTTTGCCAAAGGACTAGCTGATAAGAAGATCTCTCCAAAGAGA
GACAAGGGATTGGTGGAAAAATTGACAGCGTATGCCATGACTATTCCATTTGTCAGGCAA
CAGGTTTACAAAAAAGTGGAAGAAAAAGTGCGAAAGCAGACTAAAGGCCTTTATCCTGCA
CCTCTGAAAATAATTGATGTGGTAAAGACTGGAATTGAGCAAGGGAGTGATGCCGGTTAT
CTCTGTGAATCTCAGAAATTTGGAGAGCTTGTAATGACCAAAGAATCAAAGGCCTTGATG
GGACTCTACCATGGTCAGGTCCTGTGCAAGAAGAATAAATTTGGAGCTCCACAGAAGGAT
GTTAAGCATCTGGCTATTCTTGGTGCAGGGCTGATGGGAGCAGGCATCGCCCAAGTCTCC
GTGGATAAGGGGCTAAAGACTATACTTAAAGATGCCACCCTCACTGCGCTAGACCGAGGA
CAGCAACAAGTGTTCAAAGGATTGAATGACAAAGTGAAGAAGAAAGCTCTAACATCATTT
GAAAGGGATTCCATCTTCAGCAACTTGACTGGGCAGCTTGATTACCAAGGTTTTGAAAAG
GCCGACATGGTGATTGAAGCTGTGTTTGAGGACCTTAGTCTTAAGCACAGAGTGCTAAAG
GAAGTAGAAGCGGTGATTCCAGATCACTGTATCTTTGCCAGTAACACATCTGCTCTCCCA
ATCAGTGAAATCGCTGCTGTCAGCAAAAGACCTGAGAAGGTGATTGGCATGCACTACTTC
TCTCCCGTGGACAAGATGCAGCTGCTGGAGATTATCACGACCGAGAAAACTTCCAAAGAC
ACCAGTGCTTCAGCTGTAGCAGTTGGTCTCAAGCAGGGGAAGGTCATCATTGTGGTTAAG
GATGGACCTGGCTTCTATACTACCAGGTGTCTTGCGCCCATGATGTCTGAAGTCATCCGA
ATCCTCCAGGAAGGAGTTGACCCGAAGAAGCTGGATTCCCTGACCACAAGCTTTGGCTTT
CCTGTGGGTGCCGCCACACTGGTGGATGAAGTTGGTGTGGATGTAGCGAAACATGTGGCG
GAAGATCTGGGCAAAGTCTTTGGGGAGCGGTTTGGAGGTGGAAACCCAGAACTGCTGACA
CAGATGGTGTCCAAGGGCTTCCTAGGTCGTAAATCTGGGAAGGGCTTTTACATCTATCAG
GAGGGTGTGAAGAGGAAGGATTTGAATTCTGACATGGATAGTATTTTAGCGAGTCTGAAG
CTGCCTCCTAAGTCTGAAGTCTCATCAGACGAAGACATCCAGTTCCGCCTGGTGACAAGA
TTTGTGAATGAGGCAGTCATGTGCCTGCAAGAGGGGATCTCGGCCACACCTGCAGAGGGA
GACATCGGAGCCGTCTTTGGGCTTGGCTTCCCGCCTTGTCTGGGAGGGCCTTTCCGCTTT
GTGGATCTGTATGGCGCCCAGAAGATAGTGGACCGGCTCAAGAAATATGAAGCTGCCTAT
GGAAAACAGTTCACCCCATGCCAGCTGCTAGCTGACCATGCTAACAGCCCTAACAAGAAG
TTCTACCAGTGA
Enzyme 3 GenBank Gene ID D16480 Link Image
Enzyme 3 GeneCard ID HADHA Link Image
Enzyme 3 GenAtlas ID HADHA Link Image
Enzyme 3 HGNC ID HGNC:4801 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p23
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed Link Image]
  2. Zhang QX, Baldwin GS: Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene. Biochim Biophys Acta. 1994 Oct 18;1219(2):567-75. [PubMed Link Image]
  3. Sims HF, Brackett JC, Powell CK, Treem WR, Hale DE, Bennett MJ, Gibson B, Shapiro S, Strauss AW: The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):841-5. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5716
Enzyme 4 Name Peroxisomal multifunctional enzyme type 2
Enzyme 4 Synonyms
  1. MFE-2
  2. D-bifunctional protein
  3. DBP
  4. 17-beta-hydroxysteroid dehydrogenase 4
  5. 17-beta-HSD 4
  6. D-3-hydroxyacyl-CoA dehydratase
  7. 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
  8. 3- hydroxyacyl-CoA dehydrogenase
Enzyme 4 Gene Name HSD17B4
Enzyme 4 Protein Sequence >Peroxisomal multifunctional enzyme type 2 
MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVE
EIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIH
RVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAI
EGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVG
AGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLS
KIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKD
LKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRA
GKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKV
AVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFS
ARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISN
AYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNI
GAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNI
MLSQKLQMILKDYAKL
Enzyme 4 Number of Residues 736
Enzyme 4 Molecular Weight 79687
Enzyme 4 Theoretical pI 9.21
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • steroid binding
  • sterol carrier activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids
Enzyme 4 Pathways
Enzyme 4 Reactions
  • (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1050517 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P51659 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DHB4_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2211 bp 
ATGGGCTCACCGCTGAGGTTCGACGGGCGGGTGGTACTGGTCACCGGCGCGGGGGCAGGA
TTGGGCCGAGCCTATGCCCTGGCTTTTGCAGAAAGAGGAGCGTTAGTTGTTGTGAATGAT
TTGGGAGGGGACTTCAAAGGAGTTGGTAAAGGCTCCTTAGCTGCTGATAAGGTTGTTGAA
GAAATAAGAAGGAGAGGTGGAAAAGCAGTGGCCAACTATGATTCAGTGGAAGAAGGAGAG
AAGGTTGTGAAGACAGCCCTGGATGCTTTTGGAAGAATAGATGTTGTGGTCAACAATGCT
GGAATTCTGAGGGATCGTTCCTTTGCTAGGATAAGTGATGAAGACTGGGATATAATCCAC
AGAGTTCATTTGCGGGGTTCATTCCAAGTGACACGGGCAGCATGGGAACACATGAAGAAA
CAGAAGTATGGAAGGATTATTATGACTTCATCAGCTTCAGGAATATATGGCAACTTTGGC
CAGGCCAATTATAGTGCTGCAAAGTTGGGTCTTCTGGGCCTTGCAAATTCTCTTGCAATT
GAAGGCAGGAAAAGCAACATTCATTGTAACACCATTGCTCCTAATGCGGGATCACGGATG
ACTCAGACAGTTATGCCTGAAGATCTTGTGGAAGCCCTGAAGCCAGAGTATGTGGCACCT
CTTGTCCTTTGGCTTTGTCACGAGAGTTGTGAGGAGAATGGTGGCTTGTTTGAGGTTGGA
GCAGGATGGATTGGAAAATTACGCTGGGAGCGGACTCTTGGAGCTATTGTAAGACAAAAG
AATCACCCAATGACTCCTGAGGCAGTCAAGGCTAACTGGAAGAAGATCTGTGACTTTGAG
AATGCCAGCAAGCCTCAGAGTATCCAAGAATCAACTGGCAGTATAATTGAAGTTCTGAGT
AAAATAGATTCAGAAGGAGGAGTTTCAGCAAATCATACTAGTCGTGCAACGTCTACAGCA
ACATCAGGATTTGCTGGAGCTATTGGCCAGAAACTCCCTCCATTTTCTTATGCTTATACG
GAACTGGAAGCTATTATGTATGCCCTTGGAGTGGGAGCGTCAATCAAGGATCCAAAAGAT
TTGAAATTTATTTATGAAGGAAGTTCTGATTTCTCCTGTTTGCCCACCTTCGGAGTTATC
ATAGGTCAGAAATCTATGATGGGTGGAGGATTAGCAGAAATTCCTGGACTTTCAATCAAC
TTTGCAAAGGTTCTTCATGGAGAGCAGTACTTAGAGTTATATAAACCACTTCCCAGAGCA
GGAAAATTAAAATGTGAAGCAGTTGTTGCTGATGTCCTAGATAAAGGATCCGGTGTAGTG
ATTATTATGGATGTCTATTCTTATTCTGAGAAGGAACTTATATGCCACAATCAGTTCTCT
CTCTTTCTTGTTGGCTCTGGAGGCTTTGGTGGAAAACGGACATCAGACAAAGTCAAGGTA
GCTGTAGCCATACCTAATAGACCTCCTGATGCTGTACTTACAGATACCACCTCTCTTAAT
CAGGCTGCTTTGTACCGCCTCAGTGGAGACTGGAATCCCTTACACATTGATCCTAACTTT
GCTAGTCTAGCAGGTTTTGACAAGCCCATATTACATGGATTATGTACATTTGGATTTTCT
GCCAGGCGTGTGTTACAGCAGTTTGCAGATAATGATGTGTCAAGATTCAAGGCAATTAAG
GCTCGTTTTGCAAAACCAGTATATCCAGGACAAACTCTACAAACTGAGATGTGGAAGGAA
GGAAACAGAATTCATTTTCAAACCAAGGTCCAAGAAACTGGAGACATTGTCATTTCAAAT
GCATATGTGGATCTTGCACCAACATCTGGTACTTCAGCTAAGACACCCTCTGAGGGCGGG
AAGCTTCAGAGTACCTTTGTATTTGAGGAAATAGGACGCCGCCTAAAGGATATTGGGCCT
GAGGTGGTGAAGAAAGTAAATGCTGTATTTGAGTGGCATATAACCAAAGGCGGAAATATT
GGGGCTAAGTGGACTATTGACCTGAAAAGTGGTTCTGGAAAAGTGTACCAAGGCCCTGCA
AAAGGTGCTGCTGATACAACAATCATACTTTCAGATGAAGATTTCATGGAGGTGGTCCTG
GGCAAGCTTGACCCTCAGAAGGCATTCTTTAGTGGCAGGCTGAAGGCCAGAGGGAACATC
ATGCTGAGCCAGAAACTTCAGATGATTCTTAAAGACTACGCCAAGCTCTGA
Enzyme 4 GenBank Gene ID X87176 Link Image
Enzyme 4 GeneCard ID HSD17B4 Link Image
Enzyme 4 GenAtlas ID HSD17B4 Link Image
Enzyme 4 HGNC ID HGNC:5213 Link Image
Enzyme 4 Chromosome Location 5
Enzyme 4 Locus 5q21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Adamski J, Normand T, Leenders F, Monte D, Begue A, Stehelin D, Jungblut PW, de Launoit Y: Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV. Biochem J. 1995 Oct 15;311 ( Pt 2):437-43. [PubMed Link Image]
  2. Jiang LL, Miyazawa S, Souri M, Hashimoto T: Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J Biochem (Tokyo). 1997 Feb;121(2):364-9. [PubMed Link Image]
  3. Leenders F, Dolez V, Begue A, Moller G, Gloeckner JC, de Launoit Y, Adamski J: Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV. Mamm Genome. 1998 Dec;9(12):1036-41. [PubMed Link Image]
  4. Jiang LL, Kobayashi A, Matsuura H, Fukushima H, Hashimoto T: Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. J Biochem (Tokyo). 1996 Sep;120(3):624-32. [PubMed Link Image]
  5. Haapalainen AM, van Aalten DM, Merilainen G, Jalonen JE, Pirila P, Wierenga RK, Hiltunen JK, Glumoff T: Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution. J Mol Biol. 2001 Nov 9;313(5):1127-38. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8815
Enzyme 5 Name Hydroxyacyl-Coenzyme A dehydrogenase, type II
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name HADH2
Enzyme 5 Protein Sequence >Hydroxyacyl-Coenzyme A dehydrogenase, type II 
MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVF
APADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDV
NLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTL
PIARDLAPIGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGE
VIRLDGAIRMQP
Enzyme 5 Number of Residues 252
Enzyme 5 Molecular Weight 25984
Enzyme 5 Theoretical pI 7.29
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase 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
  • 1-27
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 57210025 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q5H927 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q5H927_HUMAN Link Image
Enzyme 5 PDB ID 1SO8 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >759 bp 
ATGGCAGCAGCGTGTCGGAGCGTGAAGGGCCTGGTGGCGGTAATAACCGGAGGAGCCTCG
GGCCTGGGCCTGGCCACGGCGGAGCGACTTGTGGGGCAGGGAGCCTCTGCTGTGCTTCTG
GACCTGCCCAACTCGGGTGGGGAGGCCCAAGCCAAGAAGTTAGGAAACAACTGCGTTTTC
GCCCCAGCCGACGTGACCTCTGAGAAGGATGTGCAAACAGCTCTGGCTCTAGCAAAAGGA
AAGTTTGGCCGTGTGGATGTAGCTGTCAACTGTGCAGGCATCGCGGTGGCTAGCAAGACG
TACAACTTAAAGAAGGGCCAGACCCATACCTTGGAAGACTTCCAGCGAGTTCTTGATGTG
AATCTCATGGGCACCTTCAATGTGATCCGCCTGGTGGCTGGTGAGATGGGCCAGAATGAA
CCAGACCAGGGAGGCCAACGTGGGGTCATCATCAACACTGCCAGTGTGGCTGCCTTCGAG
GGTCAGGTTGGACAAGCTGCATACTCTGCTTCCAAGGGGGGAATAGTGGGCATGACACTG
CCCATTGCTCGGGATCTGGCTCCCATAGGTCTGTTTGGCACCCCACTGCTGACCAGCCTC
CCAGAGAAAGTGTGCAACTTCTTGGCCAGCCAAGTGCCCTTCCCTAGCCGACTGGGTGAC
CCTGCTGAGTATGCTCACCTCGTACAGGCCATCATCGAGAACCCATTCCTCAATGGAGAG
GTCATCCGGCTGGATGGGGCCATTCGTATGCAGCCTTGA
Enzyme 5 GenBank Gene ID Z97054 Link Image
Enzyme 5 GeneCard ID HADH2 Link Image
Enzyme 5 GenAtlas ID HADH2 Link Image
Enzyme 5 HGNC ID HGNC:4800 Link Image
Enzyme 5 Chromosome Location X
Enzyme 5 Locus Xp11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 13010
Enzyme 6 Name Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
Enzyme 6 Synonyms
  1. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase, isoform CRA_b
  2. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase variant
Enzyme 6 Gene Name EHHADH
Enzyme 6 Protein Sequence >Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase 
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAG
ADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQV
GLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEE
AIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAA
VQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSV
GVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSG
PKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIAS
STDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFV
GNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLT
GPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFL
SRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHK
GGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPS
SKL
Enzyme 6 Number of Residues 723
Enzyme 6 Molecular Weight 79496
Enzyme 6 Theoretical pI 9.54
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid 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
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 62021246 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q58EZ5 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q58EZ5_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 BC038948 Link Image
Enzyme 6 GeneCard ID Q58EZ5 Link Image
Enzyme 6 GenAtlas ID EHHADH Link Image
Enzyme 6 HGNC ID HGNC:3247 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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]
  2. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  3. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 13022
Enzyme 7 Name Putative uncharacterized protein
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name HADHA
Enzyme 7 Protein Sequence >Putative uncharacterized protein 
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 7 Number of Residues 763
Enzyme 7 Molecular Weight 83000
Enzyme 7 Theoretical pI Not Available
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function Not Available
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B2R7L4 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2R7L4_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID Not Available
Enzyme 7 GeneCard ID B2R7L4 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available