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Human Metabolome Database Version 2.5

 

Showing metabocard for 3-Hydroxybutyryl-CoA (HMDB01166)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:33
Accession Number HMDB01166
Secondary Accession Numbers HMDB02383
Common Name 3-Hydroxybutyryl-CoA
Description 3-Hydroxybutyryl-CoA is a substrate for Enoyl-CoA hydratase (mitochondrial), Trifunctional enzyme alpha subunit (mitochondrial) and Peroxisomal bifunctional enzyme.
Synonyms
  1. (3R)-3-Hydroxybutanoyl-CoA
  2. (R)-3-Hydroxybutanoyl-CoA
  3. (S)-3-hydroxybutanoyl-CoA
  4. 3-OH-butyryl-CoA
  5. 3-hydroxybutanoyl-CoA
  6. 3-hydroxybutanoyl-coenzyme a
  7. 3-hydroxybutyryl-CoA
  8. 3-hydroxybutyryl-coenzyme A
  9. beta-hydroxybutyryl-CoA
  10. beta-hydroxybutyryl-S-CoA
  11. hydroxy-butyryl-CoA
  12. (3R)-3-Hydroxybutanoyl-Coenzyme A
  13. (R)-3-Hydroxybutanoyl-Coenzyme A
  14. (S)-3-hydroxybutanoyl-Coenzyme A
  15. 3-OH-butyryl-Coenzyme A
  16. beta-hydroxybutyryl-Coenzyme A
  17. beta-hydroxybutyryl-S-Coenzyme A
  18. hydroxy-butyryl-Coenzyme A
Chemical IUPAC Name [5-(6-aminopurin-9-yl)-4-hydroxy-2-[[hydroxy-[hydroxy-[3-hydroxy-3-[2-[2-(3-hydroxybutanoylsulfanyl)ethylcarbamoyl]ethylcarbamoyl]-2,2-dimethyl-propoxy]-phosphoryl]oxy-phosphoryl]oxymethyl]oxolan-3-yl]oxyphosphonic acid
Chemical Formula C25H42N7O18P3S
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 853.623
Monoisotopic Molecular Weight 853.151978
Isomeric SMILES C[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=C1N=CN=C2N
Canonical SMILES CC(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=C1N=CN=C2N
KEGG Compound ID C03561 Link Image
BioCyc ID 2-METHYL-3-HYDROXY-BUTYRYL-COA Link Image
BiGG ID 36912 Link Image
Wikipedia Link beta-hydroxybutyryl-CoA Link Image
NuGOwiki Link HMDB01166 Link Image
Metagene Link HMDB01166 Link Image
METLIN ID 456 Link Image
PubChem Compound 521 Link Image
PubChem Substance 2472 Link Image
ChEBI ID 15452 Link Image
CAS Registry Number 2871-66-1
InChI Identifier InChI=1/C25H42N7O18P3S/c1-13(33)8-16(35)54-7-6-27-15(34)4-5-28-23(38)20(37)25(2,3)10-47-53(44,45)50-52(42,43)46-9-14-19(49-51(39,40)41)18(36)24(48-14)32-12-31-17-21(26)29-11-30-22(17)32/h11-14,18-20,24,33,36-37H,4-10H2,1-3H3,(H,27,34)(H,28,38)(H,42,43)(H,44,45)(H2,26,29,30)(H2,39,40,41)/t13-,14-,18-,19-,20?,24-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.07 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.62 [Predicted by ALOGPS]; -6.5 [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 Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Butyrate Metabolism SMP00073 Link Image map00650 Link Image
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
Lysine Degradation SMP00037 Link Image map00310 Link Image
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids SMP00480 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Enoyl-CoA hydratase, mitochondrial precursor
  2. Trifunctional enzyme subunit alpha, mitochondrial precursor
  3. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
Enzyme 1 [top]
Enzyme 1 ID 5625
Enzyme 1 Name Enoyl-CoA hydratase, mitochondrial precursor
Enzyme 1 Synonyms
  1. Short chain enoyl-CoA hydratase
  2. SCEH
  3. Enoyl-CoA hydratase 1
Enzyme 1 Gene Name ECHS1
Enzyme 1 Protein Sequence >Enoyl-CoA hydratase, mitochondrial precursor 
MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNA
LCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHW
DHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLT
RAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMA
KESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
Enzyme 1 Number of Residues 290
Enzyme 1 Molecular Weight 31388
Enzyme 1 Theoretical pI 8.19
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-17
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 433413 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P30084 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ECHM_HUMAN Link Image
Enzyme 1 PDB ID 2DUB Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >873 bp 
ATGGCCGCCCTGCGTGTCCTGCTGTCCTGCGCCCGCGGCCCGCTGAGGCCCCCGGTTCGC
TGTCCCGCCTGGCGTCCCTTCGCCTCGGGTGCTAACTTTGAGTACATCATCGCAGAAAAA
AGAGGGAAGAATAACACCGTGGGGTTGATCCAACTGAACCGCCCCAAGGCCCTCAATGCA
CTTTGCGATGGCCTGATTGACGAGCTCAACCAGGCCCTGAAGATCTTCGAGGAGGACCCG
GCCGTTGGGGGCATTGTCCTCACCGGCGGGGATAAGGCCTTTGCAGCTGGAGCTGATATC
AAGGAAATGCAGAACCTGAGTTTCCAGGACTGTTACTCCAGCAAGTTCTTGAAGCACTGG
GGCCACCTCACCCAGGTCAAGAAGCCAGTCATCGCTGCTGTCAATGGCTATCCGTTTGGC
GGGGGCTGTGAGCTTGCCATGATGTGTGATATCATCTATGCCGGTGAGAAGGCCCAGTTT
GCACAGCCGGAGATCTTAATAGGAACCATCCCAGGTGCAGGCGGCACCCAGAGACTCACC
CGTGCTGTTGGGAAGTCGCTGGAGCTGGAGATGGTCCTCACCGGTGACGCGATCTCAGCC
CAGGACGCCAAGCAAGCAGGTCTTGTCAGCAAGATTTGTCCTGTTGAGACACTGGTGGAA
GAAGCCATCCAGTGTGCAGAAAAAATTGCCAGCAATTCTAAAATTGTAGTAGCGATGGCC
AAAGAATCAGTGAATGCAGCTTTTGAAATGACATTAACAGAAGGAAGTAAGTTGGAGAAG
AAACTCTTTTATTCAACCTTTGCCACTGATGACCGGAAAGAAGGGATGACCGCGTTTGTG
GAAAAGAGAAAGGCCAACTTCAAAGACCAGTGA
Enzyme 1 GenBank Gene ID D13900 Link Image
Enzyme 1 GeneCard ID ECHS1 Link Image
Enzyme 1 GenAtlas ID ECHS1 Link Image
Enzyme 1 HGNC ID HGNC:3151 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10q26.2-q26.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5626
Enzyme 2 Name Trifunctional enzyme subunit alpha, mitochondrial precursor
Enzyme 2 Synonyms
  1. TP-alpha
  2. 78 kDa gastrin-binding protein[Includes: Long-chain enoyl-CoA hydratase
Enzyme 2 Gene Name HADHA
Enzyme 2 Protein Sequence >Trifunctional enzyme subunit alpha, mitochondrial precursor 
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 2 Number of Residues 763
Enzyme 2 Molecular Weight 83001
Enzyme 2 Theoretical pI 9.52
Enzyme 2 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 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Bifunctional subunit
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
  • 1-23
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 862457 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P40939 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ECHA_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID D16480 Link Image
Enzyme 2 GeneCard ID HADHA Link Image
Enzyme 2 GenAtlas ID HADHA Link Image
Enzyme 2 HGNC ID HGNC:4801 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p23
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13010
Enzyme 3 Name Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
Enzyme 3 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 3 Gene Name EHHADH
Enzyme 3 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 3 Number of Residues 723
Enzyme 3 Molecular Weight 79496
Enzyme 3 Theoretical pI 9.54
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 Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 62021246 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q58EZ5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q58EZ5_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID BC038948 Link Image
Enzyme 3 GeneCard ID Q58EZ5 Link Image
Enzyme 3 GenAtlas ID EHHADH Link Image
Enzyme 3 HGNC ID HGNC:3247 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available