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Human Metabolome Database Version 2.5

 

Showing metabocard for (S)-3-Hydroxyisobutyryl-CoA (HMDB01052)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:27
Accession Number HMDB01052
Secondary Accession Numbers Not Available
Common Name (S)-3-Hydroxyisobutyryl-CoA
Description (S)-3-Hydroxyisobutyryl-CoA is s metabolite of 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4 ) during beta-alanine metabolism (KEGG 00410), propanoate metabolism (KEGG 00640), and valine, leucine and isoleucine degradation (KEGG 00280). Deficiencies of this enzyme in valine degradation can result in hypotonia, poor feeding, motor delay, and subsequent neurological regression in infancy, episodes of ketoacidosis and Leigh-like changes in the basal ganglia on a magnetic resonance imaging scan (PMID 17160907).
Synonyms
  1. 3-Hydroxy-2-methylpropanoyl-CoA
  2. 3-Hydroxy-2-methylpropionyl-CoA
  3. 3-hydroxy-isobutyryl-CoA
  4. 3-hydroxy-isobutyryl-coenzyme A
  5. (S)-3-Hydroxyisobutyryl-CoA
  6. 3-Hydroxy-2-methylpropanoyl-Coenzyme A
  7. 3-Hydroxy-2-methylpropionyl-Coenzyme A
  8. (S)-3-Hydroxyisobutyryl-Coenzyme A
  9. 3-hydroxyisobutyryl-CoA
  10. 3-hydroxyisobutyryl-Coenzyme A
Chemical IUPAC Name S-[2-[3-[[4-[[[5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] 3-hydroxy-2-methylpropanethioate
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
  • primary alcohol
  • 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 CC(CO)C(=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
Canonical SMILES CC(CO)C(=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 C06000 Link Image
BioCyc ID 3-HYDROXY-ISOBUTYRYL-COA Link Image
BiGG ID 47176 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01052 Link Image
Metagene Link HMDB01052 Link Image
METLIN ID 453 Link Image
PubChem Compound 88 Link Image
PubChem Substance 8274 Link Image
ChEBI ID 28259 Link Image
CAS Registry Number 319440-43-2
InChI Identifier InChI=1/C25H42N7O18P3S/c1-13(8-33)24(38)54-7-6-27-15(34)4-5-28-22(37)19(36)25(2,3)10-47-53(44,45)50-52(42,43)46-9-14-18(49-51(39,40)41)17(35)23(48-14)32-12-31-16-20(26)29-11-30-21(16)32/h11-14,17-19,23,33,35-36H,4-10H2,1-3H3,(H,27,34)(H,28,37)(H,42,43)(H,44,45)(H2,26,29,30)(H2,39,40,41)
Synthesis Reference Hawes, John W.; Harper, Edwin T. Synthesis of methacrylyl-CoA and (R)- and (S)-3-hydroxyisobutyryl-CoA. Methods in Enzymology (2000), 324(Branched-Chain Amino Acids), 73-79.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.14 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -6.7 [Predicted by PubChem via XLOGP]; -0.56 [Predicted by ALOGPS] 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
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
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. Lehnert W, Sass JO: Glutaconyl-CoA is the main toxic agent in glutaryl-CoA dehydrogenase deficiency (glutaric aciduria type I). Med Hypotheses. 2005;65(2):330-3. [PubMed Link Image]
Metabolic Enzymes
  1. Enoyl-CoA hydratase, mitochondrial precursor
  2. 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial precursor
  3. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
  4. Putative uncharacterized protein
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 10303
Enzyme 2 Name 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial precursor
Enzyme 2 Synonyms
  1. 3-hydroxyisobutyryl-coenzyme A hydrolase
  2. HIBYL-CoA-H
  3. HIB-CoA hydrolase
Enzyme 2 Gene Name HIBCH
Enzyme 2 Protein Sequence >3-hydroxyisobutyryl-CoA hydrolase, mitochondrial precursor 
MGQREMWRLMSRFNAFKRTNTILHHLRMSKHTDAAEEVLLEKKGCTGVITLNRPKFLNAL
TLNMIRQIYPQLKKWEQDPETFLIIIKGAGGKAFCAGGDIRVISEAEKAKQKIAPVFFRE
EYMLNNAVGSCQKPYVALIHGITMGGGVGLSVHGQFRVATEKCLFAMPETAIGLFPDVGG
GYFLPRLQGKLGYFLALTGFRLKGRDVYRAGIATHFVDSEKLAMLEEDLLALKSPSKENI
ASVLENYHTESKIDRDKSFILEEHMDKINSCFSANTVEEIIENLQQDGSSFALEQLKVIN
KMSPTSLKITLRQLMEGSSKTLQEVLTMEYRLSQACMRGHDFHEGVRAVLIDKDQSPKWK
PADLKEVTEEDLNNHFKSLGSSDLKF
Enzyme 2 Number of Residues 386
Enzyme 2 Molecular Weight 43483
Enzyme 2 Theoretical pI Not Available
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 3-Hydroxypropionyl-CoA + H2O --> 3-Hydroxypropanoate + Coenzyme A + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 3320120 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q6NVY1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HIBCH_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID U66669 Link Image
Enzyme 2 GeneCard ID Not Available
Enzyme 2 GenAtlas ID HIBCH Link Image
Enzyme 2 HGNC ID HGNC:4908 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hawes JW, Jaskiewicz J, Shimomura Y, Huang B, Bunting J, Harper ET, Harris RA: Primary structure and tissue-specific expression of human beta-hydroxyisobutyryl-coenzyme A hydrolase. J Biol Chem. 1996 Oct 18;271(42):26430-4. [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
Enzyme 4 [top]
Enzyme 4 ID 13022
Enzyme 4 Name Putative uncharacterized protein
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name HADHA
Enzyme 4 Protein Sequence >Putative uncharacterized protein 
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 4 Number of Residues 763
Enzyme 4 Molecular Weight 83000
Enzyme 4 Theoretical pI Not Available
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID B2R7L4 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B2R7L4_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 Not Available
Enzyme 4 GeneCard ID B2R7L4 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available