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Human Metabolome Database Version 2.5

 

Showing metabocard for Biotin (HMDB00030)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:38
Accession Number HMDB00030
Secondary Accession Numbers Not Available
Common Name Biotin
Description Biotin is an enzyme co-factor present in minute amounts in every living cell. Biotin is also known as vitamin H or B7 or coenzyme R. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk. Biotin has been recognized as an essential nutrient. Our biotin requirement is fulfilled in part through diet, through endogenous reutilization of biotin and perhaps through capture of biotin generated in the intestinal flora. The utilization of biotin for covalent attachment to carboxylases and its reutilization through the release of carboxylase biotin after proteolytic degradation constitutes the 'biotin cycle'. Biotin deficiency is associated with neurological manifestations, skin rash, hair loss and metabolic disturbances that are thought to relate to the various carboxylase deficiencies (metabolic ketoacidosis with lactic acidosis). It has also been suggested that biotin deficiency is associated with protein malnutrition, and that marginal biotin deficiency in pregnant women may be teratogenic. Biotin acts as a carboxyl carrier in carboxylation reactions. There are four biotin-dependent carboxylases in mammals: those of propionyl-CoA (PCC), 3-methylcrotonyl-CoA (MCC), pyruvate (PC) and acetyl-CoA carboxylases (isoforms ACC-1 and ACC-2). All but ACC-2 are mitochondrial enzymes. The biotin moiety is covalently bound to the epsilon amino group of a Lysine residue in each of these carboxylases in a domain 60-80 amino acids long. The domain is structurally similar among carboxylases from bacteria to mammals. There are four biotin-dependent carboxylases in mammals: those of propionyl-CoA (PCC), 3-methylcrotonyl-CoA (MCC), pyruvate (PC) and acetyl-CoA carboxylases (isoforms ACC-1 and ACC-2). All but ACC-2 are mitochondrial enzymes. The biotin moiety is covalently bound to the epsilon amino group of a Lys residue in each of these carboxylases in a domain 60-80 amino acids long. The domain is structurally similar among carboxylases from bacteria to mammals. Evidence is emerging that biotin participates in processes other than classical carboxylation reactions. Specifically, novel roles for biotin in cell signaling, gene expression, and chromatin structure have been identified in recent years. Human cells accumulate biotin by using both the sodium-dependent multivitamin transporter and monocarboxylate transporter 1. These transporters and other biotin-binding proteins partition biotin to compartments involved in biotin signaling: cytoplasm, mitochondria, and nuclei. The activity of cell signals such as biotinyl-AMP, Sp1 and Sp3, nuclear factor (NF)-kappaB, and receptor tyrosine kinases depends on biotin supply. Consistent with a role for biotin and its catabolites in modulating these cell signals, greater than 2000 biotin-dependent genes have been identified in various human tissues. Many biotin-dependent gene products play roles in signal transduction and localize to the cell nucleus, consistent with a role for biotin in cell signaling. Posttranscriptional events related to ribosomal activity and protein folding may further contribute to effects of biotin on gene expression. Finally, research has shown that biotinidase and holocarboxylase synthetase mediate covalent binding of biotin to histones (DNA-binding proteins), affecting chromatin structure; at least seven biotinylation sites have been identified in human histones. Biotinylation of histones appears to play a role in cell proliferation, gene silencing, and the cellular response to DNA repair. Roles for biotin in cell signaling and chromatin structure are consistent with the notion that biotin has a unique significance in cell biology. (PMID: 15992684, 16011464)
Synonyms
  1. (+)-Biotin
  2. (+)-cis-Hexahydro-2-oxo-1H-thieno[3,4]imidazole-4-valerate
  3. (+)-cis-Hexahydro-2-oxo-1H-thieno[3,4]imidazole-4-valeric acid
  4. (3aS,4S,6aR)-Hexahydro-2-oxo-1H-thieno[3,4-d]imidazole-4-valerate
  5. (3aS,4S,6aR)-Hexahydro-2-oxo-1H-thieno[3,4-d]imidazole-4-valeric acid
  6. -(+)-biotin
  7. 1swk
  8. 1swn
  9. 1swr
  10. 5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoate
  11. 5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoic acid
  12. Biodermatin
  13. Bioepiderm
  14. Bios h
  15. Bios II
  16. Biotin
  17. cis-(+)-Tetrahydro-2-oxothieno[3,4]imidazoline-4-valerate
  18. cis-(+)-Tetrahydro-2-oxothieno[3,4]imidazoline-4-valeric acid
  19. cis-Hexahydro-2-oxo-1H-thieno(3,4)imidazole-4-valeric acid
  20. cis-Tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid
  21. Coenzyme R
  22. D(+)-Biotin
  23. D-(+)-biotin
  24. d-Biotin
  25. D-biotin factor s
  26. delta-(+)-Biotin
  27. delta-Biotin
  28. Factor s
  29. Factor s (vitamin)
  30. Hexahydro-2-oxo-1H-thieno(3,4-d)imidazole-4-pentanoic acid
  31. hexahydro-2-oxo-[3aS-(3aa,4b,6aa)]-1H-Thieno[3,4-d]imidazole-4-pentanoate
  32. hexahydro-2-oxo-[3aS-(3aa,4b,6aa)]-1H-Thieno[3,4-d]imidazole-4-pentanoic acid
  33. hexahydro-2-oxo-[3as-(3alpha,4beta,6alpha)]-1H-Thieno[3,4-d]imidazole-4-pentanoate
  34. hexahydro-2-oxo-[3as-(3alpha,4beta,6alpha)]-1H-Thieno[3,4-d]imidazole-4-pentanoic acid
  35. Rovimix H 2
  36. Vitamin B7
  37. Vitamin H
  38. Vitamin-h
  39. delta-biotin factor s
  40. Lutavit H2
  41. Meribin
  42. Hexahydro-2-oxo-1H-thieno(3,4-d)imidazole-4-pentanoate
Chemical IUPAC Name 5-(7-oxo-3-thia-6,8-diazabicyclo[3.3.0]oct-4-yl)pentanoic acid
Chemical Formula C10H16N2O3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Biotin and Derivatives
Sub Class
  • Modified biotins
Family
  • Mammalian Metabolite
Species
  • thioether
  • carboxylic acid
  • urea
  • heterocyclic compound
Biofunction
  • Essential vitamins
  • Component of Biotin metabolism
Application
—
Source
  • Exogenous
Average Molecular Weight 244.311
Monoisotopic Molecular Weight 244.088165
Isomeric SMILES OC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12
Canonical SMILES OC(=O)CCCCC1SCC2NC(=O)NC12
KEGG Compound ID C00120 Link Image
BioCyc ID BIOTIN Link Image
BiGG ID 33931 Link Image
Wikipedia Link Biotin Link Image
NuGOwiki Link HMDB00030 Link Image
Metagene Link HMDB00030 Link Image
METLIN ID 243 Link Image
PubChem Compound 171548 Link Image
PubChem Substance 10257672 Link Image
ChEBI ID 15956 Link Image
CAS Registry Number 58-85-5
InChI Identifier InChI=1/C10H16N2O3S/c13-8(14)4-2-1-3-7-9-6(5-16-7)11-10(15)12-9/h6-7,9H,1-5H2,(H,13,14)(H2,11,12,15)/t6-,7-,9-/m0/s1
Synthesis Reference Corey, E. J.; Mehrotra, Mukund M. A simple and enantioselective synthesis of (+)-biotin. Tetrahedron Letters (1988), 29(1), 57-60.
Melting Point (Experimental) 232 oC
Experimental Water Solubility 0.22 mg/mL at 25 oC [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 1.22 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity . Source: PhysProp
Predicted LogP/Hydrophobicity 0.39 [MEYLAN,WM & HOWARD,PH (1995)]; 0.17 [Predicted by ALOGPS]; 0.5 [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 1AVD Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
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 Not Available
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 0.00127 +/- 0.00067 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Thuy LP, Sweetman L, Nyhan WL: A new immunochemical assay for biotin. Clin Chim Acta. 1991 Oct 31;202(3):191-7. [PubMed Link Image]
Biofluid Blood
Value 0.0034 (0.002 - 0.0051) uM
Age Newborn:0-30 days 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 Blood
Value 0.0016 (0.0009 - 0.0028) uM
Age Children:1-13 yrs old
Sex N/A
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 Blood
Value 0.0024 (0.0008 - 0.0041) uM
Age Adult:>18 yrs old
Sex Female
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 CSF
Value 0.0005 +/- 0.0002 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Livaniou E, Nyalala JO, Anagnostouli M, Papageorgiou C, Evangelatos GP, Ithakissios DS: Determination of biotin levels in cerebrospinal fluid samples. J Pharm Biomed Anal. 1999 Dec;21(4):875-9. [PubMed Link Image]
Biofluid Urine
Value 0.049 +/- 0.035 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Thuy LP, Sweetman L, Nyhan WL: A new immunochemical assay for biotin. Clin Chim Acta. 1991 Oct 31;202(3):191-7. [PubMed Link Image]
Biofluid Urine
Value 0.023 (0.013-0.032) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Zempleni J, McCormick DB, Mock DM: Identification of biotin sulfone, bisnorbiotin methyl ketone, and tetranorbiotin-l-sulfoxide in human urine. Am J Clin Nutr. 1997 Feb;65(2):508-11. [PubMed Link Image]
Biofluid Urine
Value 0.014 (0.002-0.044) umol/mmol creatinine
Age Children:1-13 yrs 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.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Biotin Metabolism SMP00066 Link Image map00780 Link Image
General References
  1. Thuy LP, Belmont J, Nyhan WL: Prenatal diagnosis and treatment of holocarboxylase synthetase deficiency. Prenat Diagn. 1999 Feb;19(2):108-12. [PubMed Link Image]
  2. Zempleni J, McCormick DB, Mock DM: Identification of biotin sulfone, bisnorbiotin methyl ketone, and tetranorbiotin-l-sulfoxide in human urine. Am J Clin Nutr. 1997 Feb;65(2):508-11. [PubMed Link Image]
  3. Bussolati G, Gugliotta P, Volante M, Pace M, Papotti M: Retrieved endogenous biotin: a novel marker and a potential pitfall in diagnostic immunohistochemistry. Histopathology. 1997 Nov;31(5):400-7. [PubMed Link Image]
  4. Mock DM, Stadler DD, Stratton SL, Mock NI: Biotin status assessed longitudinally in pregnant women. J Nutr. 1997 May;127(5):710-6. [PubMed Link Image]
  5. Thuy LP, Sweetman L, Nyhan WL: A new immunochemical assay for biotin. Clin Chim Acta. 1991 Oct 31;202(3):191-7. [PubMed Link Image]
  6. Limat A, Suormala T, Hunziker T, Waelti ER, Braathen LR, Baumgartner R: Proliferation and differentiation of cultured human follicular keratinocytes are not influenced by biotin. Arch Dermatol Res. 1996;288(1):31-8. [PubMed Link Image]
  7. Bigham SL, Ballard JD, Giles KD, Clelland CS, Jeffcoat R, Griffin KS, Farley TD, Bushman DR, Wright JR: Synthesis and possible applications of biotin-linked copper clusters. Physiol Chem Phys Med NMR. 1990;22(2):63-72. [PubMed Link Image]
  8. Mock DM, Stadler DD: Conflicting indicators of biotin status from a cross-sectional study of normal pregnancy. J Am Coll Nutr. 1997 Jun;16(3):252-7. [PubMed Link Image]
  9. Bingham JP, Bian S, Tan ZY, Takacs Z, Moczydlowski E: Synthesis of a biotin derivative of iberiotoxin: binding interactions with streptavidin and the BK Ca2+-activated K+ channel expressed in a human cell line. Bioconjug Chem. 2006 May-Jun;17(3):689-99. [PubMed Link Image]
  10. Mock DM: Biotin status: which are valid indicators and how do we know? J Nutr. 1999 Feb;129(2S Suppl):498S-503S. [PubMed Link Image]
  11. Mock DM, Dyken ME: Biotin catabolism is accelerated in adults receiving long-term therapy with anticonvulsants. Neurology. 1997 Nov;49(5):1444-7. [PubMed Link Image]
  12. Mock DM, Nyalala JO, Raguseo RM: A direct streptavidin-binding assay does not accurately quantitate biotin in human urine. J Nutr. 2001 Aug;131(8):2208-14. [PubMed Link Image]
  13. Mardach R, Zempleni J, Wolf B, Cannon MJ, Jennings ML, Cress S, Boylan J, Roth S, Cederbaum S, Mock DM: Biotin dependency due to a defect in biotin transport. J Clin Invest. 2002 Jun;109(12):1617-23. [PubMed Link Image]
  14. Mock DM, Heird GM: Urinary biotin analogs increase in humans during chronic supplementation: the analogs are biotin metabolites. Am J Physiol. 1997 Jan;272(1 Pt 1):E83-5. [PubMed Link Image]
  15. Fujimoto W, Inaoki M, Fukui T, Inoue Y, Kuhara T: Biotin deficiency in an infant fed with amino acid formula. J Dermatol. 2005 Apr;32(4):256-61. [PubMed Link Image]
  16. Schenker S, Hu ZQ, Johnson RF, Yang Y, Frosto T, Elliott BD, Henderson GI, Mock DM: Human placental biotin transport: normal characteristics and effect of ethanol. Alcohol Clin Exp Res. 1993 Jun;17(3):566-75. [PubMed Link Image]
  17. Mock NI, Malik MI, Stumbo PJ, Bishop WP, Mock DM: Increased urinary excretion of 3-hydroxyisovaleric acid and decreased urinary excretion of biotin are sensitive early indicators of decreased biotin status in experimental biotin deficiency. Am J Clin Nutr. 1997 Apr;65(4):951-8. [PubMed Link Image]
  18. Grafe F, Wohlrab W, Neubert RH, Brandsch M: Transport of biotin in human keratinocytes. J Invest Dermatol. 2003 Mar;120(3):428-33. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Acetyl-CoA carboxylase 2
  2. Pyruvate carboxylase, mitochondrial precursor
  3. Acetyl-CoA carboxylase 1
  4. Propionyl-CoA carboxylase beta chain, mitochondrial precursor
  5. Propionyl-CoA carboxylase alpha chain, mitochondrial precursor
  6. Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor
  7. Biotin--protein ligase
  8. Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor
  9. Biotinidase precursor
  10. Sodium-dependent multivitamin transporter
  11. Propionyl-CoA carboxylase alpha subunit
  12. cDNA, FLJ93758, Homo sapiens biotinidase (BTD), mRNA (Biotinidase, isoform CRA_a)
  13. cDNA, FLJ96567, highly similar to Homo sapiens propionyl Coenzyme A carboxylase, alpha polypeptide(PCCA), mRNA
  14. Putative uncharacterized protein ACACB
  15. Putative uncharacterized protein DKFZp686B20267
Enzyme 1 [top]
Enzyme 1 ID 5247
Enzyme 1 Name Acetyl-CoA carboxylase 2
Enzyme 1 Synonyms
  1. ACC-beta[Includes: Biotin carboxylase
Enzyme 1 Gene Name ACACB
Enzyme 1 Protein Sequence >Acetyl-CoA carboxylase 2 
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGT
GTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSV
AGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHR
DFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVT
PEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKL
PELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK
RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQV
QSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAP
LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNL
PAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDE
GFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVA
LKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGAL
NVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM
NGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSP
SAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVAR
LELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIK
LKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFP
SQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRV
EHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSD
ELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCP
ENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCV
VEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTR
NFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVP
ILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQL
ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEY
LQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGS
RLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSF
GNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPK
DILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIG
SFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFK
YLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSL
AYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQL
GGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSR
APYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVE
TRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAIKDFNREKLPLMIFANWRGF
SGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYA
DKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLK
AREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVK
QEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIR
ENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
Enzyme 1 Number of Residues 2458
Enzyme 1 Molecular Weight 276558
Enzyme 1 Theoretical pI 6.46
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-24
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2138330 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O00763 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name COA2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >7452 bp 
ATGGTCTTGCTTCTTTGTCTATCTTGTCTGATTTTCTCCTGTCTGACCTTTTCCTGGTTA
AAAATCTGGGAGAAAATGACGGACTCCAAGCCGATCACCAAGAGTAAATCAGAAGCAAAC
CTCATCCCGAGCCAGGAGCCCTTTCCAGCCTCTGATAACTCAGGGGAGACACCGCAGAGA
AATGGGGAGGGCCACACTCTGCACAAAGACACCCAGCCAGGCCGAGCCCAGCCTCCCACA
AAGGCCCAAAGATCCGGTCGGCGGAGAAACTCCCTACCACCCTCCCGCCAGAAGCCCCCA
AGAAACCCCCTTTCTTCCAGTGACGCAGCACCCTCCCCAGAGCTTCAAGCCAACGGGACT
GGGACACAAGGTCTGGAGGCCACAGATACCAATGGCCTGTCCTCCTCAGCCAGGCCCCAG
GGCAGCAAGCTGGTCCCCTCCAAAGAAGACAAGAAGCAGGCAAACATCAAGAGGCAGCTG
ATGACCAACTTCATCCTGGGCTCTTTTGATGACTACTCCTCCGACGAGGACTCTGTTGCT
GGCTCATCTCGTGAGTCTACCCGGAAGGGCAGCCGGGCCAGCTTGGGGGCCCTGTCCCTG
GAGGCTTATCTGACCACAGGTGAAGCTGAGACCCGCGTCCCCACTATGAGGCCGAGCATG
TCGGGACTCCACCTGGTGAAGAGGGGACGGGAACACAAGAAGCTGGACCTGCACAGAGAC
TTTACCGTGGCTTCTCCCGCTGAGTTTGTCACACGCTTTGGGGGGGATCGGGTCATCGAG
AAGGTGCTTATTGCCAACAACGGGATTGCCGCTGTGAAGTGCATGCGCTCCATCCGCAGG
TGGGCCTATGAGATGTTCCGCAACGAGCGGGCCATCCGGTTTGTTCGCATGGTGACCCCC
GAGGACCTTAAGGCCAACGCAGAGTACATCAAGATGGCGGATCATTACGGGCCCGCCCCA
GGAGGGCCCAATAACAACAACTATGCCAACGTGGAGCTGATTGTGGACATTGCCAAGAGA
ATCCCGTTGCAGGCGGTGTGGGCTGGCTGGGGCCATGCTTTAGAAAACCCTAAACTTCCG
GAGCTGCTGTGCAAGAATGGAGTTGCTTTCTTAGGCCCTCCCAGGTTGAGGCCAATGGTG
GGTCTAGGAGATAAGATCGCCTCCACCGTTGTCGCCCAGACGCTACAGGTCCCAACCCTG
CCCAGGAGTGGAAGCGCCCTGACAGTGGAGTGGACAGAAGATGATCTGCAGCAGGGAAAA
AGAATCAGTGTCCCAGAAGATGTTTATGACAAGGGTTGCGTGAAAGACGTAGATGAGGGC
TTGGAGGCAGCAGAAAGAATTGGTTTTCCATTGATGATCAAAGCTTCTGAAGGTGGCGGA
GGGAAGGGAATCCGGGAAACTGAGAGTGCGGAGGACTTCCCGATCCTTTTCAGACAAGTA
CAGAGTGAGATCCCAGGCTCGCCCATCTTTCTCATGAAGCTGGCCCAGCACGCCCGTCAC
CTGGAAGTTCAGATCCTCGCTGACCAGTATGGGAATGCTGTGTCTCTGTTTGGTCGCGAC
TGCTCCATCCAGCGGCGGCATCAGAAGATCGTTGAGGAAGCACCGGCCACCATCGCGCCG
CTGGCCATATTCGAGTTCATGGAGCAGTGTGCCATTCGCCTGGCCAAGACCGTGGGCTAT
GTGAGTGCAGGGACAGTGGAATACCTCTATAGTCAGGATGGTAGCTTCCACTTCTTGGAG
CTGAATCCTCGCTTGCAGGTGGAACATCCCTGCACAGAAATGATTGCTGACGTTAATCTG
CCGGCCGCCCAGCTACAGATCGCCATGGGTGCCCCACTGCACCGGCTGAAAGATATCCGG
CTTCTGTATGGAGAGTCACCCTGGGGAGACTCCCCAATTTCTTTTGAAAACTCAGCTCAT
CTCCCCTGCCCCCGAGGCCACGTCATTGCCACCAGAATCACCAGCGAAAACCCAGACGAG
GGTTTTAAGCCGAGCTCCGGGACTGTCCAGGAACTGAATTTCCGGAGCAGCAAGAACGTC
TGGGGTTACTTCACGGTGGCCGCTACTGGAGGCCTGCACGAGTTTGCGATTTCCCAGTTT
GGGCACTGCTTCTCCTGGGGAGAGAACCGGAAAGAGGCCATTTCGAACATGGTGGTGGCT
TTGAAGGAACTGTCCCTCCGAGGCGACTTTAGGACTACCGTGGAATACCTCATTAACCTC
CTGGAGACCGAGAGCTTCCAGAACAACTACATCGACACCGGGTGGTTGGACTACCTCATT
GCTGAGAAAGTGCAAAAGAAACCGAATATCATGCTTGGGGTGGTATGCGGGGCCCTTGAA
CGTGGAGATGCGATGTTCAGAACGTGCATGACAGATTTCTTACACTCCCTGGAAAGGGGC
CAGGTCCTCCCAGCGGATTCACTACTGAACCTCGTAGATGTGGAATTAATTTACGAGGGT
GTAAAGTACATTCTAAAGGTGACCCGGCAGTCTCTGACCATGTTCGTTCTCATCATGAAT
GGCTGCCACATCGAGATTGATGCCCACCGGCTGAATGATGGGGGGCTCCTGCTCTCCTAC
AATGGGAACAGCTACACCACCTACATGAAGGAAGAGGTTGACAGTTACCGTACCATCGGC
AATAAGACGTGTGTTTTTGAGAAGGAGAACGATCCTACAGTCCTGAGATCCCCCTCGGCT
GGGAAGCTGACACAGATCACAGTGGAGGATGGGGGCCACGTTGAGGCTGGGAGACGCTAC
GCTGAGATGGAGGTGATGAAGATGATCATGACCCTGAACGTTCAGGAAAGAGGCCGGGTG
AAGTACATCAAGCGTCCAGGTGCGGTGCTGGAAGCAGGCTGCGTGGTGGCCAGGCTGGAG
CTCGATGACCCTTCTAAAGTCCACCCGGCTGAACCGTTCACAGGAGAACTCCCTGCCCAG
CAGAACACTGCCGACCTCGGAAAGAAACTGCACAGGGTCTTCCACAGCGTCCTGGGAAGC
CTCACCAACGTCATGAGTGGCTTTTGTCTGCCAGAGCCGTTTTTTAGCATAAAGCTGAAG
GAGTGGGTGCAGAAGCTCATGATGACCCTCCGGCACCCGTCACTGCTGCTGGACGTGCAG
GAGATCATGACCAGTCGTGCAGGCCGCATCCCCCCCCCTGTTGAGAAGTCTGTCCGCAAG
GTGATGGCCCAGTATGCCAGCAACATCACCTCGGTGCTGTGCCAGTTCCCCAGCCAGCAG
ATAGCCACCATCCTGGACTGCCATGCAGCCACCCTGCAGCGGAAGGCTGATCGAGAGGTC
TTCTTCATCAACACCCAGAGCATGGTGCAGTTGGTCCAGAGGTACCGAAGTGGAATCCGC
GGTCATATGAAAACAGTGGTGATCGATCTCTTGAGAAGATACTTGCGTGTTGAGACCATT
TTCGGCAAGGCAAGAGATGCTGATGCCAACTCCAGTGGGATGGTGGGGGGCGTGAGGAGC
CTGAGCTTTACCTCTGTGTGGGTGGTTTTGTCTCCCCCAGCCCACTACGACAAGTGTGTG
ATAAACCTCAGGGAACAGTTCAAGCCAGACATGTCCCAGGTGCTGGACTGCATCTTCTCC
CACGCACAGGTGACCAAGAAGAACCAGCTGGTGATCATGTTGATCGATGAGCTGTGTGGC
CCAGACCCTTCCCTGTCGGACGAGCTGATCTCCATCCTCAACGAGCTCACTCAGCTGAGC
AAAAGCGAGCACTGCAAAGTGGCCCTCAGAGCCCGGCAGATCCTGATCGCCTCCCCCTCC
TACGAGCTGCGGCATAACCAGGTGGAGTCCATTTTCCTGTCTGCCATTGACATGTACGGC
CACCAGTTCTGCCCCGAGAACCTCCAGAAATTAATACTTTCGGAAACAACCATCTTCGAC
GTCCTGAATACTTTCTTCTATCACGCAAACAAAGTCGTGTGCATGGCGTCCTTGGAGGTT
TACGTGGGGGGGGCTTACATCGCCTATGTGTTAAACAGCCTGCAGCACCGGCAGCTCCCG
GACGGCACCTGCGTGGTAGAATTCCAGTTCATGCTGCCGTCCTCCCACCCAAACCGGATG
ACCGTGCCCATCAGCATCACCAACCCTGACCTGCTGAGGCACACGACAGAGCTCTTCATG
GACAGCGGCTTCTCCCCACTGTGCCAGCGCATGGGAGCCATGGTAGCCTTCAGGAGATTC
GAGGACTTCACCAGAAATTTTGATGAAGTCATCTCTTGCTTCGCCAACGTGCCGAAAGAC
CCCCCCCTCTTCAGCGAGGCCCGCACCTCCCTATACTCCGAGGATGACTGCAAGAGCCTC
AGAGAAGAGCCCATCCACATTCTGAATGTGTCCATCCAGTGTGCGGACCACCTGGAGGAT
GAGGCACTGGTGCCGATTTTACGTACATTCGTACAGTCCAAGAAAAATATCCTTGTGGAT
TATGGACTCCGACGAATCCCATTCTTGATTGCCCAAGAGAAAGAATTTCCCAAGTTTTTC
ACATTCAGAGCAAGAGATGAGTTTGCAGAAGATCGCATTTACCGTCACTTGGAACCTGCC
CTGGCTTTCCAGCTGGAACTCAACCGGATGCGTAACTTCGATCTGACCGCCGTGCCCTGT
GCCAACCACAAGATGCACCTTTACCTGGGTGCTGCCAAGGTGGAAGGAAGGTATGAAGTG
ACGGACCATAGGTTCTTCATCCGTGCCATCATCAGGCACTCTGACCTGATCACAAAGGAA
GCCTCCTTCGAATACCTGCAGAACGAGGGTGAGCGGCTGCTCCTGGAGGCCATGGACGAG
CTGGAGGTGGCGTTCAATAACACCAACGTGCGCACCGACTGCAACCACATCTTCCTCAAC
TTCGTGCCCACTGTCATCATGGACCCCAACAAGATCGAGGAGTCCGTGCGCTACATGGTT
ATGCGCTACGGCAGCCGGCTGTGGAAACTCCGTGTGCTACAGGCTGAGGTCAAGATCAAC
ATCCGCCAGACCACCACCGGCAGTGCCGTTCCCATCCGCCTGTTCATCACCAATGAGTCG
GGCTACTACCTGGACATCAGCCTCTACAAAGAAGTGACTGACTCCAGATCTGGAAATATC
ATGTTTCACTCCTTCGGCAACAAGCAAGGGCCCCAGCACGGGATGCTGATCAATACTCCC
TACGTCACCAAGGATCTGCTCCAGGCCAAGCGATTCCAGGCCCAGACCCTGGGAACCACC
TACATCTATGACTTCCCGGAAATGTTCAGGCAGGCTCTCTTTAAACTGTGGGGCTCCCCA
GACAAGTATCCCAAAGACATCCTGACATACACTGAATTAGTGTTGGACTCTCAGGGCCAG
CTGGTGGAGATGAACCGACTTCCTGGTGGAAATGAGGTGGGCATGGTGGCCTTCAAAATG
AGGTTTAAGACCCAGGAGTACCCGGAAGGACGGGATGTGATCGTCATCGGCAATGACATC
ACCTTTCGCATTGGATCCTTTGGCCCTGGAGAGGACCTTCTGTACCTGCGGGCATCCGAG
ATGGCCCGGGCAGAGGCGATTCCCAAAATTTACGTGGCAGCCAACAGTGGCGCCCGTATT
GGCATGGCAGAGGAGATCAAACACATGTTCCACGTGGCTTGGGTGGACCCAGAAGACCCC
CACAAAGGATTTAAATACCTGTACCTGACTCCCCAAGACTACACCAGAATCAGCTCCCTG
AACTCCGTCCACTGTAAACACATCGAGGAAGGAGGAGAGTCCAGATACATGATCACGGAT
ATCATCGGGAAGGATGATGGCTTGGGCGTGGAGAATCTGAGGGGCTCAGGCATGATTGCT
GGGGAGTCCTCTCTGGCTTACGAAGAGATCGTCACCATTAGCTTGGTGACCTGCCGAGCC
ATTGGGATTGGGGCCTACTTGGTGAGGCTGGGCCAGCGAGTGATCCAGGTGGAGAATTCC
CACATCATCCTCACAGGAGCAAGTGCTCTCAACAAGGTCCTGGGAAGAGAGGTCTACACA
TCCAACAACCAGCTGGGTGGCGTTCAGATCATGCATTACAATGGTGTCTCCCACATCACC
GTGCCAGATGACTTTGAGGGGGTTTATACCATCCTGGAGTGGCTGTCCTATATGCCAAAG
GATAATCACAGCCCTGTCCCTATCATCACACCCACTGACCCCATTGACAGAGAAATTGAA
TTCCTCCCATCCAGAGCTCCCTACGACCCCCGGTGGATGCTTGCAGGAAGGCCTCACCCA
ACTCTGAAGGGAACGTGGCAGAGCGGATTCTTTGACCACGGCAGTTTCAAGGAAATCATG
GCACCCTGGGCGCAGACCGTGGTGACAGGACGAGCAAGGCTTGGGGGGATTCCCGTGGGA
GTGATTGCTGTGGAGACACGGACTGTGGAGGTGGCAGTCCCTGCAGACCCTGCCAACCTG
GATTCTGAGGCCAAGATAATTCAGCAGGCAGGACAGGTGTGGTTCCCAGACTCAGCCTAC
AAAACCGCCCAGGCCATCAAGGACTTCAACCGGGAGAAGTTGCCCCTGATGATCTTTGCC
AACTGGAGGGGGTTCTCCGGTGGCATGAAAGACATGTATGACCAGGTGCTGAAGTTTGGA
GCCTACATCGTGGACGGCCTTAGACAATACAAACAGCCCATCCTGATCTATATCCGCCCT
ATGCGGGAGCTCCGGGGAGGCTCCTGGGTGGTCATAGATGCCACCATCAACCCGCTGTGC
ATAGAAATGTATGCAGACAAAGAGAGCAGGGGTGGTGTTCTGGAACCAGAGGGGACAGTG
GAGATTAAGTTCCGAAAGGAAGATCTGATAAAGTCCATGAGAAGGATCGATCCAGCTTAC
AAGAAGCTCATGGAACAGCTAGGGGAACCTGATCTCTCCGACAAGGACCGAAAGGACCTG
GAGGGCCGGCTAAAGGCTCGCGAGGACCTGCTGCTCCCCATCTACCACCAGGTGGCGGTG
CAGTTCGCCGACTTCCATGACACACCCGGCCGGATGCTGGAGAAGGGCGTCATATCTGAC
ATCCTGGAGTGGAAGACCGCACGCACCTTCCTGTATTGGCGTCTGCGCCGCCTCCTCCTG
GAGGACCAGGTCAAGCAGGAGATCCTGCAGGCCAGCGGGGAGCTGAGTCACGTGCATATC
CAGTCCATGCTGCGTCGCTGGTTCGTGGAGACGGAGGGGGCTGTCAAGGCCTACTTGTGG
GACAACAACCAGGTGGTTGTGCAGTGGCTGGAACAGCACTGGCAGGCAGGGGATGGCCCG
CGCTCCACCATCCGTGAGAACATCACGTACCTGAAGCACGACTCTGTCCTCAAGACCATC
CGAGGCCTGGTTGAAGAAAACCCCGAGGTGGCCGTGGACTGTGTGATATACCTGAGCCAG
CACATCAGCCCAGCTGAGCGGGCGCAGGTCGTTCACCTGCTGTCTACCATGGACAGCCCG
GCCTCCACCTGA
Enzyme 1 GenBank Gene ID U89344 Link Image
Enzyme 1 GeneCard ID ACACB Link Image
Enzyme 1 GenAtlas ID ACACB Link Image
Enzyme 1 HGNC ID HGNC:85 Link Image
Enzyme 1 Chromosome Location 12
Enzyme 1 Locus 12q24.11
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Abu-Elheiga L, Almarza-Ortega DB, Baldini A, Wakil SJ: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. J Biol Chem. 1997 Apr 18;272(16):10669-77. [PubMed Link Image]
  2. Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA: Identification of a second human acetyl-CoA carboxylase gene. Biochem J. 1996 Jun 15;316 ( Pt 3):915-22. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5248
Enzyme 2 Name Pyruvate carboxylase, mitochondrial precursor
Enzyme 2 Synonyms
  1. Pyruvic carboxylase
  2. PCB
Enzyme 2 Gene Name PC
Enzyme 2 Protein Sequence >Pyruvate carboxylase, mitochondrial precursor 
MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELG
IRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGF
LSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEA
HEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIE
KPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAK
QVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDL
GLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISP
HYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQF
IDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAG
FRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSK
LFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVF
KFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSL
QYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGV
AAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEG
ARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQM
LGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFP
EPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF
KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFEL
NGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVL
SAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE
Enzyme 2 Number of Residues 1178
Enzyme 2 Molecular Weight 129635
Enzyme 2 Theoretical pI 6.83
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-carbon bonds
  • nucleotide binding
  • purine nucleotide binding
  • pyruvate carboxylase activity
  • vitamin binding
Process
  • alcohol metabolism
  • cellular metabolism
  • gluconeogenesis
  • glucose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-21
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 458236 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P11498 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PYC_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3537 bp 
ATGCTGAAGTTCCGAACAGTCCATGGGGGCCTGAGGCTCCTGGGAATCCGCCGAACCTCC
ACCGCCCCCGCTGCCTCCCCAAATGTCCGGCGCCTGGAGTATAAGCCCATCAAGAAAGTC
ATGGTGGCCAACAGAGGTGAGATTGCCATCCGTGTGTTCCGGGCCTGCACGGAGCTGGGC
ATCCGCACCGTAGCCATCTACTCTGAGCAGGACACGGGCCAGATGCACCGGCAGAAAGCA
GATGAAGCCTATCTCATCGGCCGCGGCCTGGCCCCCGTGCAGGCCTACCTGCACATCCCA
GACATCATCAAGGTGGCCAAGGAGAACAACGTAGATGCAGTGCACCCTGGCTACGGGTTC
CTCTCTGAGCGAGCGGACTTCGCCCAGGCCTGCCAGGATGCAGGGGTCCGGTTTATTGGG
CCAAGCCCAGAAGTGGTCCGCAAGATGGGAGACAAGGTGGAGGCCCGGGCCATCGCCATT
GCTGCGGGTGTTCCCGTTGTCCCTGGCACAGATGCCCCCATCACGTCCCTGCATGAGGCC
CACGAGTTCTCCAACACCTACGGCTTCCCCATCATCTTCAAGGCGGCCTATGGGGGTGGA
GGGCGTGGCATGAGGGTGGTGCACAGCTACGAGGAGCTGGAGGAGAATTACACCCGGGCC
TACTCAGAGGCTCTGGCCGCCTTTGGGAATGGGGCGCTGTTTGTGGAGAAGTTCATCGAG
AAGCCACGGCACATCGAGGTGCAGATCTTGGGGGACCAGTATGGGAACATCCTGCACCTG
TACGAGCGAGACTGCTCCATCCAGCGGCGGCACCAGAAGGTGGTCGAGATTGCCCCCGCC
GCCCACCTGGACCCGCAGCTTCGGACTCGGCTCACCAGCGACTCTGTGAAACTCGCTAAA
CAGGTGGGCTACGAGAACGCAGGCACCGTGGAGTTCCTGGTGGACAGGCACGGCAAGCAC
TACTTCATCGAGGTCAACTCCCGCCTGCAGGTGGAGCACACGGTCACAGAGGAGATCACC
GACGTAGACCTGGTCCATGCTCAGATCCACGTGGCTGAGGGCAGGAGCCTACCCGACCTG
GGCCTGCGGCAGGAGAACATCCGCATCAACGGGTGTGCCATCCAGTGCCGGGTCACCACC
GAGGACCCCGCGCGCAGCTTCCAGCCGGACACCGGCCGCATTGAGGTGTTCCGGAGCGGA
GAGGGCATGGGCATCCGCCTGGATAATGCTTCCGCCTTCCAAGGAGCCGTCATCTCGCCC
CACTACGACTCCCTGCTGGTCAAAGTCATTGCCCACGGCAAAGACCACCCCACGGCCGCC
ACCAAGATGAGCAGGGCCCTTGCGGAGTTCCGCGTCCGAGGTGTGAAGACCAACATCGCC
TTCCTGCAGAATGTGCTCAACAACCAGCAGTTCCTGGCAGGCACTGTGGACACCCAGTTC
ATCGACGAGAACCCAGAGCTGTTCCAGCTGCGGCCTGCACAGAACCGGGCCCAAAAGCTG
TTGCACTACCTCGGCCATGTCATGGTAAACGGTCCAACCACCCCGATTCCCGTCAAGGCC
AGCCCCAGCCCCACGGACCCCGTTGTCCCTGCAGTGCCCATAGGCCCGCCCCCGGCTGGT
TTCAGAGACATCCTGCTGCGAGAGGGGCCTGAGGGCTTTGCTCGAGCTGTGCGGAACCAC
CCGGGGCTGCTGCTGATGGACACGACCTTCAGGGACGCCCACCAGTCACTGCTGGCCACT
CGTGTGCGCACCCACGATCTCAAAAAGATCGCCCCCTATGTTGCCCACAACTTCAGCAAG
CTCTTCAGCATGGAGAACTGGGGAGGAGCCACGTTTGACGTCGCCATGCGCTTCCTGTAT
GAGTGCCCCTGGCGGCGGCTGCAGGAGCTCCGGGAGCTCATCCCCAACATCCCTTTCCAG
ATGCTGCTGCGGGGGGCCAATGCTGTGGGCTACACCAACTACCCAGACAACGTGGTCTTC
AAGTTCTGTGAAGTGGCCAAAGAGAATGGCATGGATGTCTTCCGTGTGTTTGACTCCCTC
AACTACTTGCCCAACATGCTGCTGGGCATGGAGGCGGCAGGAAGTGCCGGAGGCGTGGTG
GAGGCTGCCATCTCATACACGGGCGACGTGGCCGACCCCAGCCGCACCAAGTACTCACTG
CAGTACTACATGGGCTTGGCCGAAGAGCTGGTGCGAGCTGGCACCCACATCCTGTGCATC
AAGGACATGGCCGGGCTGCTGAAGCCCACGGCCTGCACCATGCTGGTCAGCTCCCTCCGG
GACCGCTTCCCCGACCTCCCACTGCACATCCACACCCACGACACGTCAGGGGCAGGCGTG
GCAGCCATGCTGGCCTGTGCCCAGGCTGGAGCTGATGTGGTGGATGTGGCAGCTGATTCC
ATGTCTGGGATGACTTCACAGCCCAGCATGGGGGCCCTGGTGGCCTGTACCAGAGGGACT
CCCCTGGACACAGAGGTGCCCATGGAGCGCGTGTTTGACTACAGTGAGTACTGGGAGGGG
GCTCGGGGACTGTACGCGGCCTTCGACTGCACGGCCACCATGAAGTCTGGCAACTCGGAC
GTGTATGAAAATGAGATCCCAGGGGGCCAGTACACCAACCTGCACTTCCAGGCCCACAGC
ATGGGGCTTGGCTCCAAGTTCAAGGAGGTCAAGAAGGCCTATGTGGAGGCCAACCAGATG
CTGGGCGATCTCATCAAGGTGACGCCCTCCTCCAAGATCGTGGGGGACCTGGCCCAGTTT
ATGGTGCAGAATGGATTGAGCCGGGCAGAGGCCGAAGCTCAGGCGGAAGAGCTGTCCTTT
CCCCGCTCCGTGGTGGAGTTCCTGCAGGGCTACATCGGTGTCCCCCATGGGGGGTTCCCC
GAACCCTTTCGCTCTAAGGTACTGAAGGACCTGCCAAGGGTGGAGGGGCGGCCTGGAGCC
TCCCTCCCTCCCCTGGATCTGCAGGCACTGGAGAAGGAGCTGGTAGACCGGCATGGGGAG
GAGGTGACGCCGGAAGATGTGCTCTCAGCAGCTATGTACCCCGATGTGTTTGCCCACTTC
AAGGACTTCACTGCCACCTTTGGCCCCCTGGATAGCCTGAATACTCGCCTCTTCCTGCAG
GGACCCAAGATCGCAGAGGAGTTTGAGGTGGAGCTGGAGCGGGGCAAGACGCTGCACATC
AAAGCCCTGGCCGTGAGCGACCTGAACCGGGCCGGCCAGAGGCAGGTCTTCTTTGAGCTC
AATGGGCAGCTGCGGTCCATCTTGGTCAAGGACACCCAGGCCATGAAGGAGATGCACTTC
CACCCCAAGGCCCTAAAGGACGTGAAGGGCCAGATCGGGGCGCCCATGCCTGGGAAGGTG
ATAGACATCAAAGTGGTGGCAGGGGCCAAGGTGGCCAAGGGCCAGCCCCTGTGTGTGCTC
AGTGCCATGAAGATGGAGACTGTGGTGACCTCACCCATGGAGGGTACTGTCCGCAAGGTT
CATGTGACCAAGGACATGACACTGGAAGGTGACGACCTCATCCTGGAGATCGAGTGA
Enzyme 2 GenBank Gene ID U04641 Link Image
Enzyme 2 GeneCard ID PC Link Image
Enzyme 2 GenAtlas ID PC Link Image
Enzyme 2 HGNC ID HGNC:8636 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. Wexler ID, Du Y, Lisgaris MV, Mandal SK, Freytag SO, Yang BS, Liu TC, Kwon M, Patel MS, Kerr DS: Primary amino acid sequence and structure of human pyruvate carboxylase. Biochim Biophys Acta. 1994 Oct 21;1227(1-2):46-52. [PubMed Link Image]
  2. MacKay N, Rigat B, Douglas C, Chen HS, Robinson BH: cDNA cloning of human kidney pyruvate carboxylase. Biochem Biophys Res Commun. 1994 Jul 29;202(2):1009-14. [PubMed Link Image]
  3. Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed Link Image]
  4. Freytag SO, Collier KJ: Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J Biol Chem. 1984 Oct 25;259(20):12831-7. [PubMed Link Image]
  5. Carbone MA, MacKay N, Ling M, Cole DE, Douglas C, Rigat B, Feigenbaum A, Clarke JT, Haworth JC, Greenberg CR, Seargeant L, Robinson BH: Amerindian pyruvate carboxylase deficiency is associated with two distinct missense mutations. Am J Hum Genet. 1998 Jun;62(6):1312-9. [PubMed Link Image]
  6. Wexler ID, Kerr DS, Du Y, Kaung MM, Stephenson W, Lusk MM, Wappner RS, Higgins JJ: Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families. Pediatr Res. 1998 May;43(5):579-84. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5276
Enzyme 3 Name Acetyl-CoA carboxylase 1
Enzyme 3 Synonyms
  1. ACC-alpha[Includes: Biotin carboxylase
Enzyme 3 Gene Name ACACA
Enzyme 3 Protein Sequence >Acetyl-CoA carboxylase 1 
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLS
DLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK
VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG
GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL
GDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQA
AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV
QILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSA
GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY
GVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY
FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET
ESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQV
LPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDG
SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYA
EIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQ
STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQ
DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV
FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD
MNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALR
ARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH
SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM
SFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSP
PQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLV
DHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ
LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE
YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG
SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA
YGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQA
FLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVI
GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVD
PEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGS
GMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR
EVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPID
RIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG
IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL
MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSI
NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAE
RKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLR
RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTE
EDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILST
MDSPST
Enzyme 3 Number of Residues 2346
Enzyme 3 Molecular Weight 265557
Enzyme 3 Theoretical pI 6.32
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 849083 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q13085 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name COA1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >7041 bp 
ATGGATGAACCATCTCCCTTGGCCCAACCTCTGGAGCTGAACCAGCACTCTCGATTCATA
ATAGGTTCTGTGTCAGAAGATAACTCAGAGGATGAGATCAGCAACCTGGTGAAGCTGGAC
CTACTGGAGGAGAAGGAGGGCTCCTTGTCACCTGCTTCTGTTGGCTCAGATACACTCTCT
GATTTGGGGATCTCTGCCCTACAGGATGGCTTGGCCTTGCACATAAGGTCCAGCTGGTCT
GGCTTGCACCTAGTAAAGCAGGGCGGAGACAGAAAGAAAATAGATTCTCAACGAGATTTC
ACTGTGGCTTCTCCAGCAGAATTTGTTACTCGCTTTGGGGGAAATAAAGTGATTGAGAAG
GTTCTCATCGCTAACAATGGCATTGCAGCAGTGAAATGCATGCGGTCTATCCGTAGGTGG
TCTTATGAAATGTTTCGAAATGAACGTGCAATTAGATTCGTTGTCATGGTCACACCTGAA
GACCTTAAAGCCAATGCAGAATACATTAAGATGGCAGATCACTATGTGCCGGTGCCTGGA
GGAGCAAACAACAACAACTATGCAAATGTGGAATTAATTCTTGATATTGCTAAAAGGATC
CCAGTGCAAGCAGTGTGGGCTGGCTGGGGTCATGCTTCTGAGAATCCCAAACTACCGGAA
CTTCTCTTGAAAAATGGCATTGCCTTCATGGGTCCTCCAAACCAGGCCATGTGGGCTTTA
GGGGATAAGATTGCATCTTCCATAGTGGCTCAAACTGCAGGTATCCCAACTCTTCCCTGG
AGCGGCAGTGGTCTTCGTGTGGACTGGCAGGAAAATGATTTTTCAAAACGTATCTTAAAT
GTTCCCCAGGAGCTATATGAAAAAGGTTATGTGAAAGATGTGGATGATGGGCTAAAGGCA
GCTGAGAAGGTTGGATATCCAGTAATGATCAAGGCCTCAGAGGGAGGAGGAGGGAAGGGA
ATTAGAAAAGTTAACAATGCAGATGACTTCCCTAATCTCTTCAGACAGGTTCAAGCTGAA
GTTCCTGGATCTCCCATATTTGTGATGAGACTAGCCAAACAATCTCGTCATCTGGAGGTG
CAGATCTTAGCGGACCAATATGGCAATGCTATCTCTTTGTTTGGTCGTGATTGCTCTGTA
CAACGCAGGCATCAGAAGATTATTGAAGAAGCACCTGCTACTATTGCTACTCCAGCAGTA
TTTGAACACATGGAACAGTGTGCGGTGAAACTTGCCAAAATGGTGGGTTATGTGAGTGCT
GGGACTGTGGAATACCTGTACAGCCAGGATGGCAGCTTCTACTTTCTAGAATTGAACCCT
CGGCTACAGGTTGAACAACCTTGTACAGAGATGGTGGCTGATGTCAATCTCCCCGCAGCA
CAGCTCCAGATTGCCATGGGGATTCCTCTATATAGAATCAAGGATATCCGTATGATGTAT
GGGGTATCTCCTTGGGGTGATTCTCCCATTGATTTTGAAAATTCTGCTCACGTTCCTTGT
CCAAGGGGCCATGTTATTGCTGCTCGGATCACTAGTGAAAATCCAGATGAGGGTTTTAAG
CCCAGCTCAGGAACAGTTCAGGAGCTAAATTTCCGCAGCAATAAGAATGTTTGGGGATAT
TTCAGTGTTGCTGCTGCAGGGGGACTTCATGAATTTGCTGGTTCTCAGTTTGGTCACTGC
TTTTCTTGGGGAGAAAACAGAGAAGAAGCAATTTCAAACATGGTGGTGGCATTGAAGGAG
CTGTCTATTCGGGGTGACTTTCGAACTACAGTTGAATACCTGATCAAATTGTTAGAGACT
GAAAGCTTTCAAATGAACAGAATTGATACTGGCTGGCTGGACAGACTGATAGCAGAAAAA
GTACGGGCTGAGCGTCCTGACACCATGTTGGGGGTTGTGTGTGGTGCCCTCCACGTCGGA
GATGTGAGCCTGCGAAATAGCGTCTCTAACTTCCTTCACTCCTTAGAAAGGGGTCAAGTC
CTTCCGGCTCATACACTTCTGAATACAGTAGATGTTGAACTTATCTATGAGGGAGTCAAG
TATGTACTTAAGGTGACTCGACAGTCCCCCAACTCCTATGTGGTGATCATGAATGGCTCA
TGTGTAGAAGTAGATGTACATCGGCTGAGTGACGGTGGACTGCTCTTGTCCTATGATGGC
AGCAGTTACACCACGTATATGAAGGAGGAAGTAGACAGATATCGCATCACAATTGGCAAT
AAAACCTGTGTGTTTGAGAAGGAAAATGACCCATCGGTGATGCGCTCACCTTCTGCTGGG
AAGTTAATCCAGTACATTGTAGAAGATGGAGGTCATGTGTTTGCCGGCCAGTGCTATGCA
GAGATTGAGGTAATGAAGATGGTAATGACTTTGACAGCTGTGGAGTCTGGCTGTATCCAT
TACGTCAAGCGTCCTGGAGCAGCTCTTGACCCTGGCTGTGTACTCGCCAAAATGCAACTG
GACAACCCCAGCAAGGTTCAGCAGGCTGAACTTCACACAGGTAGTCTGCCACGGATCCAG
AGCACCGCTCTCCGAGGCGAGAAGCTCCATCGAGTGTTCCACTATGTCCTGGATAATCTG
GTCAATGTAATGAATGGATACTGCCTTCCAGATCCTTTCTTTAGCAGCAAGGTAAAAGAC
TGGGTAGAACGATTGATGAAAACCCTCAGAGATCCCTCCCTGCCTCTCCTAGAATTGCAA
GATATTATGACCAGTGTGTCTGGCCGCATTCCCCCCAATGTGGAGAAGTCTATCAAGAAG
GAAATGGCTCAGTATGCTAGCAACATCACATCAGTCCTCTGTCAGTTTCCCAGCCAGCAG
ATTGCAAACATCCTAGATAGCCATGCAGCTACATTGAACCGGAAATCTGAACGGGAAGTC
TTCTTTATGAATACTCAGAGCATTGTCCAGCTGGTACAGAGGTACCGAAGTGGCATCCGA
GGCCACATGAAGGCTGTGGTGATGGATCTGCTCCGGCAGTACCTGCGAGTAGAGACACAA
TTCCAGAATGGTCACTATGACAAATGTGTATTCGCCCTTCGAGAAGAGAATAAGAGTGAC
ATGAACACTGTACTGAACTACATCTTCTCTCACGCTCAAGTCACCAAGAAGAATCTTCTG
GTCACAATGCTTATTGATCAGTTGTGTGGCCGGGACCCTACTCTAACTGATGAGCTGCTG
AGTATTCTCACAGAGCTAACTCAACTCAGTAAGACCACCAATGCCAAAGTAGCACTTCGA
GCACGCCAGGTTCTTATTGCCTCCCATTTGCCATCATATGACGTTCGCCATAACCAAGTA
GAGTCTATCTTCCTATCAGCTATTGACATGTATGGACATCAATTTTGCATTGAGAACCTG
CAGAAACTCATCCTATCAGAAACATCTATTTTTGATGTCCTACCAAACTTCTTCTATCAC
AGCAACCAAGTAGTGAGGATGGCAGCTCTGGAGGTGTACGTTCGAAGGGCTTATATTGCC
TATGAACTTAACAGCGTACAACACCGCCAGCTTAAGGACAACACCTGCGTGGTGGAATTC
CAGTTCATGCTGCCCACATCTCATCCAAACAGAGGGAACATCCCTACGCTAAACAGAATG
TCCTTCTCCTCCAACCTCAACCACTATGGCATGACCCATGTAGCTAGTGTCAGCGATGTT
CTGTTGGACAACGCCTTCACACCACCTTGTCAACGCATGGGCGGAATGGTCTCTTTTCGG
ACTTTTGAAGATTTTGTCAGGATCTTTGATGAAGTAATGGGCTGCTTCTGTGACTCCCCA
CCCCAGAGTCCCACATTCCCTGAGGCAGGTCACACGTCTCTTTATGATGAGGATAAGGTT
CCCAGGGATGAACCAATTCACATTCTCAATGTGGCTATCAAGACTGACGGTGATATTGAG
GATGACAGGCTGGCAGCTATGTTCAGAGAATTCACCCAGCAAAATAAAGCTACCCTGGCT
GACCATGGGATCCGGCGCCTGACTTTCCTGGTTGCACAAAAGGATTTCAGAAAGCAGGTC
AACTATGAGGTGGATCGGAGATTTCATAGAGAATTCCCTAAATTTTTTACATTCCGAGCA
AGGGATAAGTTTGAGGAGGATCGTATCTATCGTCATCTGGAGCCTGCTCTGGCTTTCCAG
TTAGAGCTGAACCGGATGAGAAATTTTGACCTCACTGCCATTCCATGTGCTAATCACAAG
ATGCACCTGTATCTCGGGGCAGCCAAGGTGGAAGTGGGCACAGAAGTGACAGACTACAGG
TTCTTTGTTCGTGCAATCATCAGGCATTCTGATCTGGTCACCAAGGAAGCTTCTTTTGAA
TATCTGCAAAGTGAAGGGGAGCGGCTACTCCTGGAAGCCATGGATGAGTTGGAAGTTGCT
TTTAACAATACAAATGTCCGCACTGACTGTAACCACATCCTCCTCAACTTTGTGCCCACG
GTTATCATGGACCCATCAAAGATTGAGGAATCCGTGCGGAGCATGGTAATGCGGTATGGA
AGTCGCCTGTGGAAATTGCGCGTCCTCCAGGCAGAACTGAAAATCAACATTCGCCTGACG
CCAACTGGAAAAGCAATTCCCATCCGCCTTTTCCTGACAAACGAGTCTGGCTATTACTTG
GATATCAGCCTATACAAGGAAGTGACTGACTCCAGGACAGCACAGATCATGTTTCAGGCA
TATGGAGACAAGCAGGGACCACTGCATGGAATGTTAATCAATACTCCATATGTGACCAAA
GACCTGCTGCAATCAAAGAGGTTCCAGGCACAATCCTTAGGGACAACGTACATATATGAT
ATCCCAGAGATGTTTCGGCAGTCCCTGATCAAACTCTGGGAGTCTATGTCAACTCAAGCA
TTTCTTCCATCTCCCCCTCTGCCTTCTGACATGCTGACTTACACTGAACTGGTACTGGAT
GATCAAGGTCAGCTGGTCCACATGAACAGGCTTCCAGGAGGAAATGAGATTGGCATGGTA
GCTTGGAAAATGAGCCTTAAAAGTCCTGAATATCCAGAAGGCCGAGATGTTATTGTTATT
GGCAATGACATTACATACCGAATTGGGTCCTTTGGGCCTCAAGAAGATTTGTTATTTCTC
AGAGCTTCCGAACTTGCTAGGGCCGAAGGCATTCCACGCATCTATGTATCAGCCAACAGT
GGAGCAAGAATCGGACTGGCAGAAGAAATTCGCCATATGTTTCATGTGGCCTGGGTAGAT
TCTGAGGATCCTTACAAGGGATACAGGTATTTATATCTGACTCCTCAAGATTATAAGAGA
GTCGGTGCTCTCAACTCTGTCCATTGTGAACACGTGGAAGATGAAGGAGAATCCAGGTAC
AAGATAACAGATATTATTGGGAAAGAAGAGGGAATTGGACCCGAGAACCTTCGAGGTTCT
GGAATGATCGCTGGAGAATCCTCATTGGCCTATAATGAGATCATTACCATCAGCCTGGTG
ACGTCCCGGGCCATTGGGATTGGGGCTTACCTTGTCCGGCTGGGACAGAGAACCATCCAG
GTTGAGAATTCTCACTTGATTCTAACAGGAGCTGGAGCCCTCAACAAAGTCCTCGGGCGG
GAAGTGTACACCTCCAATAACCAGCTGGGGGGCATCCAGATTACGCACAACAATGGGGTG
ACCCACTGCACTGTGTGTGACGGCTTTGAAGGGGTTTTCACTGTCCTGCACTGGCTGTCT
TACATGCCCAAGAGCGTACACAGTTCAGTTCCTCTTCTGAACTCAAAGGATCCTATAGAC
AGAATCATCGAGTTTGTTCCCACAAAGACCCCATATGATCCTCGATGGATGCTAGCAGGC
CGCCCTCACCCAACCCAAAAAGGTCAGTGGTTGAGTGGCTTTTTTGACTATGGATCTTTC
TCAGAGATTATGCAGCCCTGGGCACAGACGGTGGTGGTTGGTAGAGCCAGGTTAGGGGGA
ATACCTGTGGGAGTTGTTGCTGTAGAAACCCGGACAGTAGAACTAAGTGTACCAGCTGAT
CCAGCAAACCTGGATTCTGAAGCCAAGATAATCCAGCACGCCGGCCAAGTTTGGTTTCCG
GATTCTGCGTTTAAGACGTATCAGGCCATCAAGGACTTCAACCGGGAAGGGCTACCTCTA
ATGGTCTTTGCCAACTGGAGAGGCTTCTCTGGTGGAATGAAAGATATGTATCACCAAGTG
CTGAAGTTTGGTGCTTACATTGTGGATGGCTTGCGGGAATGTTCCCAGCCTGTGCTGGTC
TACATTCCTCCCCAGGCTGAGCTGCGGGGTGGCTCCTGGGTGGTGATCGACCCAACCATC
AATCCTCGGCACATGGAGATGTATGCTGACCGAGAAAGCAGGGGATCTGTTCTGGAGCCA
GAAGGGACGGTAGAAATCAAATTCCGCAGAAAGGATCTGGTGAAAACCATGCGTCGGGTG
GACCCAGTCTACATCCACTTGGCTGAGCGATTGGGGACCCCAGAGCTGAGCCCAACTGAG
CGGAAGGAGTTGGAGAGCAAGTTGAAGGAGCGGGAGGAATTCCTAATTCCAATTTACCAT
CAGGTAGCCGTGCAGTTTGCTGACTTGCACGACACTCCAGGCCGGATGCAGGAGAAGGGT
GTTATTAGCGATATCCTGGATTGGAAAACATCCCGTACCTTCTTCTACTGGCGACTGAGG
CGTCTTCTGCTGGAGGACCTGGTCAAGAAGAAAATCCACAGTGCCAACCCTGAGCTGACT
GATGGCCAGATTCAAGCCATGTTAAGACGCTGGTTTGTGGAAGTGGAAGGAACAGTGAAG
GCTTATGTTTGGGACAATAATAAGGATCTGGCGGAGTGGCTAGAGAAACAGCTGACAGAG
GAGGATGGTGTTCACTCGGTAATAGAGGAAAACATCAAATGCATCAGCAGAGACTACGTC
CTCAAGCAAATCCGCAGCTTGGTCCAGGCCAATCCAGAGGTTGCCATGGATTCCATCATC
CATATGACGCAGCACATATCACCCACTCAGCGGGCAGAAGTCATAAGGATCCTTTCCACT
ATGGACTCCCCTTCTACGTAG
Enzyme 3 GenBank Gene ID U19822 Link Image
Enzyme 3 GeneCard ID ACACA Link Image
Enzyme 3 GenAtlas ID ACACA Link Image
Enzyme 3 HGNC ID HGNC:84 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4011-5. [PubMed Link Image]
  2. Mao J, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7515-20. Epub 2003 Jun 16. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5490
Enzyme 4 Name Propionyl-CoA carboxylase beta chain, mitochondrial precursor
Enzyme 4 Synonyms
  1. PCCase subunit beta
  2. Propanoyl-CoA:carbon dioxide ligase subunit beta
Enzyme 4 Gene Name PCCB
Enzyme 4 Protein Sequence >Propionyl-CoA carboxylase beta chain, mitochondrial precursor 
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHK
RGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVY
VFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIF
LRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVT
QEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVP
ELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPK
VASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFA
EATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVE
AAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
Enzyme 4 Number of Residues 539
Enzyme 4 Molecular Weight 58216
Enzyme 4 Theoretical pI 7.69
Enzyme 4 GO Classification
Function
  • catalytic activity
  • ligase activity
Process
—
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-23
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 312812 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P05166 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PCCB_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1620 bp 
ATGGCGGCGGCATTACGGGTGGCGGCGGTCGGGGCAAGGCTCAGCGTTCTGGCGAGCGGT
CTCCGCGCCGCGGTCCGCAGCCTTTGCAGCCAGGCCACCTCTGTTAACGAACGCATCGAA
AACAAGCGCCGGACCGCGCTGCTGGGAGGGGGCCAACGCCGTATTGACGCGCAGCACAAG
CGAGGAAAGCTAACAGCCAGGGAGAGGATCAGTCTCTTGCTGGACCCTGGCAGCTTTGTT
GAGAGCGACATGTTTGTGGAACACAGATGTGCAGATTTTGGAATGGCTGCTGACAAGAAT
AAGTTTCCTGGAGACAGCGTGGTCACTGGACGAGGCCGAATCAATGGAAGATTGGTTTAT
GTCTTCAGTCAGGATTTTACAGTTTTTGGAGGCAGTCTGTCAGGAGCACATGCCCAAAAG
ATCTGCAAAATCATGGACCAGGCCATAACGGTGGGGGCTCCAGTGATTGGGCTGAATGAC
TCTGGGGGAGCACGGATCCAAGAAGGAGTGGAGTCTTTGGCTGGCTATGCAGACATCTTT
CTGAGGAATGTTACGGCATCCGGAGTCATCCCTCAGATTTCTCTGATCATGGGCCCATGT
GCTGGTGGGGCCGTCTACTCCCCAGCCCTAACAGACTTCACGTTCATGGTAAAGGACACC
TCCTACCTGTTCATCACTGGCCCTGATGTTGTGAAGTCTGTCACCAATGAGGATGTTACC
CAGGAGGAGCTCGGTGGTGCCAAGACCCACACCACCATGTCAGGTGTGGCCCACAGAGCT
TTTGAAAATGATGTTGATGCCTTGTGTAATCTCCGGGATTTCTTCAACTACCTGCCCCTG
AGCAGTCAGGACCCGGCTTCCGTCCGTGAGTGCCACGATCCCAGTGACCGTCTGGTTCCT
GAGCTTGACACAATTGTCCCTTTGGAATCAACCAAAGCCTACAACATGGTGGACATCATA
CACTCTGTTGTTGATGAGCGTGAATTTTTTGAGATCATGCCCAATTATGCCAAGAACATC
ATTGTTGGTTTTGCAAGAATGAATGGGAGGACTGTTGGAATTGTTGGCAACCAACCTAAG
GTGGCCTCAGGATGCTTGGATATTAATTCATCTGTGAAAGGGGCTCGTTTTGTCAGATTC
TGTGATGCATTCAATATTCCACTCATCACTTTTGTTGATGTCCCTGGCTTTCTACCTGGC
ACAGCACAGGAATACGGGGGCATCATCCGGCATGGTGCCAAGCTTCTCTACGCATTTGCT
GAGGCAACTGTACCCAAAGTCACAGTCATCACCAGGAAGGCCTATGGAGGTGCCTATGAT
GTCATGAGCTCTAAGCACCTTTGTGGTGATACCAACTATGCCTGGCCCACCGCAGAGATT
GCAGTCATGGGAGCAAAGGGCGCTGTGGAGATCATCTTCAAAGGGCATGAGAATGTGGAA
GCTGCTCAGGCAGAGTACATCGAGAAGTTTGCCAACCCTTTCCCTGCAGCAGTGCGAGGG
TTTGTGGATGACATCATCCAACCTTCTTCCACACGTGCCCGAATCTGCTGTGACCTGGAT
GTCTTGGCCAGCAAGAAGGTACAACGTCCTTGGAGAAAACATGCAAATATTCCATTGTAA
Enzyme 4 GenBank Gene ID X73424 Link Image
Enzyme 4 GeneCard ID PCCB Link Image
Enzyme 4 GenAtlas ID PCCB Link Image
Enzyme 4 HGNC ID HGNC:8654 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3q21-q22
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Lamhonwah AM, Leclerc D, Loyer M, Clarizio R, Gravel RA: Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. Genomics. 1994 Feb;19(3):500-5. [PubMed Link Image]
  2. Ohura T, Ogasawara M, Ikeda H, Narisawa K, Tada K: The molecular defect in propionic acidemia: exon skipping caused by an 8-bp deletion from an intron in the PCCB allele. Hum Genet. 1993 Oct;92(4):397-402. [PubMed Link Image]
  3. Rodriguez-Pombo P, Hoenicka J, Muro S, Perez B, Perez-Cerda C, Richard E, Desviat LR, Ugarte M: Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients. Am J Hum Genet. 1998 Aug;63(2):360-9. [PubMed Link Image]
  4. Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed Link Image]
  5. Tahara T, Kraus JP, Rosenberg LE: An unusual insertion/deletion in the gene encoding the beta-subunit of propionyl-CoA carboxylase is a frequent mutation in Caucasian propionic acidemia. Proc Natl Acad Sci U S A. 1990 Feb;87(4):1372-6. [PubMed Link Image]
  6. Tahara T, Kraus JP, Ohura T, Rosenberg LE, Fenton WA: Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia. J Inherit Metab Dis. 1993;16(2):353-60. [PubMed Link Image]
  7. Muro S, Rodriguez-Pombo P, Perez B, Perez-Cerda C, Desviat LR, Sperl W, Skladal D, Sass JO, Ugarte M: Identification of novel mutations in the PCCB gene in European propionic acidemia patients. Mutation in brief no. 253. Online. Hum Mutat. 1999;14(1):89-90. [PubMed Link Image]
  8. Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed Link Image]
  9. Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5491
Enzyme 5 Name Propionyl-CoA carboxylase alpha chain, mitochondrial precursor
Enzyme 5 Synonyms
  1. PCCase subunit alpha
  2. Propanoyl-CoA:carbon dioxide ligase subunit alpha
Enzyme 5 Gene Name PCCA
Enzyme 5 Protein Sequence >Propionyl-CoA carboxylase alpha chain, mitochondrial precursor 
MLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKM
GIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGF
LSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEA
VRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFID
NPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALAR
AVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHK
QADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPLHLPGVRVDSGIQPGSDISIYY
DPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLS
DVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRAQHFQENSRMPVIKPDIANWELSVKL
HDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLSVSVDGTQRTVQCLSREAGGNM
SIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQ
EICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE
Enzyme 5 Number of Residues 703
Enzyme 5 Molecular Weight 77355
Enzyme 5 Theoretical pI 7.07
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 296366 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P05165 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PCCA_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2112 bp 
ATGCTGAGCGCGGCGCTGCGGACCCTGAAGCATGTTCTGTACTATTCAAGACAGTGCTTA
ATGGTGTCCCGTAATCTTGGTTCAGTGGGATATGATCCTAATGAAAAAACTTTTGATAAA
ATTCTTGTTGCTAATAGAGGAGAAATTGCATGTCGGGTTATTAGAACTTGCAAGAAGATG
GGCATTAAGACAGTTGCCATCCACAGTGATGTTGATGCTAGTTCTGTTCATGTGAAAATG
GCGGATGAGGCTGTCTGTGTTGGCCCAGCTCCCACCAGTAAAAGCTACCTCAACATGGAT
GCCATCATGGAAGCCATTAAGAAAACCAGGGCCCAAGCTGTACATCCAGGTTATGGATTC
CTTTCAGAAAACAAAGAATTTGCCAGATGTTTGGCAGCAGAAGATGTCGTTTTCATTGGA
CCTGACACACATGCTATTCAAGCCATGGGCGACAAGATTGAAAGCAAATTATTAGCTAAG
AAAGCAGAGGTTAATACAATCCCTGGCTTTGATGGAGTAGTCAAGGATGCAGAAGAAGCT
GTCAGAATTGCAAGGGAAATTGGCTACCCTGTCATGATCAAGGCCTCAGCAGGTGGTGGT
GGGAAAGGCATGCGCATTGCTTGGGATGATGAAGAGACCAGGGATGGTTTTAGATTGTCA
TCTCAAGAAGCTGCTTCTAGTTTTGGCGATGATAGACTACTAATAGAAAAATTTATTGAT
AATCCTCGTCATATAGAAATCCAGGTTCTAGGTGATAAACATGGGAATGCTTTATGGCTT
AATGAAAGAGAGTGCTCAATTCAGAGAAGAAATCAGAAGGTGGTGGAGGAAGCACCAAGC
ATTTTTTTGGATGCGGAGACTCGAAGAGCGATGGGAGAACAAGCTGTAGCTCTTGCCAGA
GCAGTAAAATATTCCTCTGCTGGGACCGTGGAGTTCCTTGTGGACTCTAAGAAGAATTTT
TATTTCTTGGAAATGAATACAAGACTCCAGGTTGAGCATCCTGTCACAGAATGCATTACT
GGCCTGGACCTAGTCCAGGAAATGATCCGTGTTGCTAAGGGCTACCCTCTCAGGCACAAA
CAAGCTGATATTCGCATCAACGGCTGGGCAGTTGAATGTCGGGTTTATGCTGAGGACCCC
TACAAGTCTTTTGGTTTACCATCTATTGGGAGATTGTCTCAGTACCAAGAACCGTTACAT
CTACCTGGTGTCCGAGTGGACAGTGGCATCCAACCAGGAAGTGATATTAGCATTTATTAT
GATCCTATGATTTCAAAACTAATCACATATGGCTCTGATAGAACTGAGGCACTGAAGAGA
ATGGCAGATGCACTGGATAACTATGTTATTCGAGGTGTTACACATAATATTGCATTACTT
CGAGAGGTGATAATCAACTCACGCTTTGTAAAAGGAGACATCAGCACTAAATTTCTCTCC
GATGTGTATCCTGATGGCTTCAAAGGACACATGCTAACCAAGAGTGAGAAGAACCAGTTA
TTGGCAATAGCATCATCATTGTTTGTGGCATTCCAGTTAAGAGCACAACATTTTCAAGAA
AATTCAAGAATGCCTGTTATTAAACCAGACATAGCCAACTGGGAGCTCTCAGTAAAATTG
CATGATAAAGTTCATACCGTAGTAGCATCAAACAATGGGTCAGTGTTCTCGGTGGAAGTT
GATGGGTCGAAACTAAATGTGACCAGCACGTGGAACCTGGCTTCGCCCTTATTGTCTGTC
AGCGTTGATGGCACTCAGAGGACTGTCCAGTGTCTTTCTCGAGAAGCAGGTGGAAACATG
AGCATTCAGTTTCTTGGTACAGTGTACAAGGTGAATATCTTAACCAGACTTGCCGCAGAA
TTGAACAAATTTATGCTGGAAAAAGTGACTGAGGACACAAGCAGTGTTCTGCGTTCCCCG
ATGCCCGGAGTGGTGGTGGCCGTCTCTGTCAAGCCTGGAGACGCGGTAGCAGAAGGTCAA
GAAATTTGTGTGATTGAAGCCATGAAAATGCAGAATAGTATGACAGCTGGGAAAACTGGC
ACGGTGAAATCTGTGCACTGTCAAGCTGGAGACACAGTTGGAGAAGGGGATCTGCTCGTG
GAGCTGGAATGA
Enzyme 5 GenBank Gene ID X14608 Link Image
Enzyme 5 GeneCard ID PCCA Link Image
Enzyme 5 GenAtlas ID PCCA Link Image
Enzyme 5 HGNC ID HGNC:8653 Link Image
Enzyme 5 Chromosome Location 13
Enzyme 5 Locus 13q32
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Lamhonwah AM, Mahuran D, Gravel RA: Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro- and mature alpha chains in the deduced primary sequence of a full-length cDNA. Nucleic Acids Res. 1989 Jun 12;17(11):4396. [PubMed Link Image]
  2. Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed Link Image]
  3. Stankovics J, Ledley FD: Cloning of functional alpha propionyl CoA carboxylase and correction of enzyme deficiency in pccA fibroblasts. Am J Hum Genet. 1993 Jan;52(1):144-51. [PubMed Link Image]
  4. Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed Link Image]
  5. Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed Link Image]
  6. Richard E, Desviat LR, Perez B, Perez-Cerda C, Ugarte M: Genetic heterogeneity in propionic acidemia patients with alpha-subunit defects. Identification of five novel mutations, one of them causing instability of the protein. Biochim Biophys Acta. 1999 Mar 30;1453(3):351-8. [PubMed Link Image]
  7. Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed Link Image]
  8. Campeau E, Dupuis L, Leon-Del-Rio A, Gravel R: Coding sequence mutations in the alpha subunit of propionyl-CoA carboxylase in patients with propionic acidemia. Mol Genet Metab. 1999 May;67(1):11-22. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5755
Enzyme 6 Name Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor
Enzyme 6 Synonyms
  1. 3-methylcrotonyl-CoA carboxylase 2
  2. MCCase subunit beta
  3. 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
  4. 3- methylcrotonyl-CoA carboxylase non-biotin-containing subunit
Enzyme 6 Gene Name MCCC2
Enzyme 6 Protein Sequence >Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor 
MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERV
EHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGII
TGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPR
QADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIF
LAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKL
DVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFA
RIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAK
DGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAAN
VLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLV
LGLSFSAALNAPIEKTDFGIFRM
Enzyme 6 Number of Residues 563
Enzyme 6 Molecular Weight 61334
Enzyme 6 Theoretical pI 7.75
Enzyme 6 GO Classification
Function
  • catalytic activity
  • ligase activity
Process
—
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 6 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 6 Reactions
  • ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-15
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 10934059 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9HCC0 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name MCCC2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1692 bp 
ATGTGGGCCGTCCTGAGGTTAGCCCTGCGGCCGTGTGCCCGCGCCTCTCCCGCCGGGCCG
CGCGCCTATCACGGGGACTCGGTGGCCTCGCTGGGCACCCAGCCGGACTTGGGCTCTGCC
CTCTACCAGGAGAACTACAAGCAGATGAAAGCACTAGTAAATCAGCTCCATGAACGAGTG
GAGCATATAAAACTAGGAGGTGGTGAGAAAGCCCGAGCACTTCACATATCAAGAGGAAAA
CTATTGCCCAGAGAAAGAATTGACAATCTCATAGACCCAGGGTCTCCATTTCTGGAATTA
TCCCAGTTTGCAGGTTACCAGTTATATGACAATGAGGAGGTGCCAGGAGGTGGCATTATT
ACAGGCATTGGAAGAGTATCAGGAGTAGAATGCATGATTATTGCCAATGATGCCACCGTC
AAAGGAGGTGCCTACTACCCAGTGACTGTGAAAAAACAATTACGGGCCCAAGAAATTGCC
ATGCAAAACAGGCTCCCCTGCATCTACTTAGTTGATTCGGGAGGAGCATACTTACCTCGA
CAAGCAGATGTGTTTCCAGATCGAGACCACTTTGGCCGTACATTCTATAATCAGGCAATT
ATGTCTTCTAAAAATATTGCACAGATCGCAGTGGTCATGGGCTCCTGCACCGCAGGAGGA
GCCTATGTGCCTGCCATGGCTGATGAAAACATCATTGTACGCAAGCAGGGTACCATTTTC
TTGGCAGGACCCCCCTTGGTTAAAGCGGCAACTGGGGAAGAAGTATCTGCTGAGGATCTT
GGAGGTGCTGATCTTCATTGCAGAAAGTCTGGAGTAAGTGACCACTGGGCTTTGGATGAT
CATCATGCCCTTCACTTAACTAGGAAGGTTGTGAGGAATCTAAATTATCAGAAGAAATTG
GATGTCACCATTGAACCTTCTGAAGAGCCTTTATTTCCTGCTGATGAATTGTATGGAATA
GTTGGTGCTAACCTTAAGAGGAGCTTTGATGTCCGAGAGGTCATTGCTAGAATCGTGGAT
GGAAGCAGATTCACTGAGTTCAAAGCCTTTTATGGAGACACATTAGTTACAGGATTTGCT
CGAATATTTGGGTACCCAGTAGGTATCGTTGGAAACAACGGAGTTCTCTTTTCTGAATCT
GCAAAAAAGGGTACTCACTTTGTCCAGTTATGCTGCCAAAGAAATATTCCTCTGCTGTTC
CTTCAAAACATTACTGGATTTATGGTTGGTAGAGAGTATGAAGCTGAAGGAATTGCCAAG
GATGGTGCCAAGATGGTGGCCGCTGTGGCCTGTGCCCAAGTGCCTAAGATAACCCTCATC
ATTGGGGGCTCCTATGGAGCCGGAAACTATGGGATGTGTGGCAGAGCGTATAGCCCAAGA
TTTCTCTACATTTGGCCAAATGCTCGTATCTCAGTGATGGGAGGAGAGCAGGCAGCCAAT
GTGTTGGCCACGATAACAAAGGACCAAAGAGCCCGGGAAGGAAAGCAGTTCTCCAGTGCT
GATGAAGCGGCTTTAAAAGAGCCCATCATTAAGAAGTTTGAAGAGGAAGGAAACCCTTAC
TATTCCAGCGCAAGGGTATGGGATGATGGGATCATTGATCCAGCAGACACCAGACTGGTC
TTGGGTCTCAGTTTTAGTGCAGCCCTCAACGCACCAATAGAGAAGACTGACTTCGGTATC
TTCAGGATGTAA
Enzyme 6 GenBank Gene ID AB050049 Link Image
Enzyme 6 GeneCard ID MCCC2 Link Image
Enzyme 6 GenAtlas ID MCCC2 Link Image
Enzyme 6 HGNC ID HGNC:6937 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. Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed Link Image]
  2. Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5756
Enzyme 7 Name Biotin--protein ligase
Enzyme 7 Synonyms
  1. Biotin apo-protein ligase[Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
  2. Holocarboxylase synthetase
  3. HCS
  4. Biotin-- [methylcrotonoyl-CoA-carboxylase] ligase
Enzyme 7 Gene Name HLCS
Enzyme 7 Protein Sequence >Biotin--protein ligase 
MEDRLHMDNGLVPQKIVSVHLQDSTLKEVKDQVSNKQAQILEPKPEPSLEIKPEQDGMEH
VGRDDPKALGEEPKQRRGSASGSEPAGDSDRGGGPVEHYHLHLSSCHECLELENSTIESV
KFASAENIPDLPYDYSSSLESVADETSPEREGRRVNLTGKAPNILLYVGSDSQEALGRFH
EVRSVLADCVDIDSYILYHLLEDSALRDPWTDNCLLLVIATRESIPEDLYQKFMAYLSQG
GKVLGLSSSFTFGGFQVTSKGALHKTVQNLVFSKADQSEVKLSVLSSGCRYQEGPVRLSP
GRLQGHLENEDKDRMIVHVPFGTRGGEAVLCQVHLELPPSSNIVQTPEDFNLLKSSNFRR
YEVLREILTTLGLSCDMKQVPALTPLYLLSAAEEIRDPLMQWLGKHVDSEGEIKSGQLSL
RFVSSYVSEVEITPSCIPVVTNMEAFSSEHFNLEIYRQNLQTKQLGKVILFAEVTPTTMR
LLDGLMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPF
VQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGC
GFNVTNSNPTICINDLITEYNKQHKAELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVL
PLYYRYWVHSGQQVHLGSAEGPKVSIVGLDDSGFLQVHQEGGEVVTVHPDGNSFDMLRNL
ILPKRR
Enzyme 7 Number of Residues 726
Enzyme 7 Molecular Weight 80761
Enzyme 7 Theoretical pI 5.34
Enzyme 7 GO Classification
Function
  • biotin-[acetyl-CoA-carboxylase] ligase activity
  • biotin-protein ligase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
Component
—
Enzyme 7 General Function Coenzyme transport and metabolism
Enzyme 7 Specific Function Posttranslational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 577625 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P50747 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name BPL1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2181 bp 
ATGGAAGATAGACTCCACATGGATAATGGACTGGTACCCCAAAAGATTGTGTCGGTGCAC
TTGCAGGACTCCACTCTGAAGGAAGTTAAGGATCAGGTCTCAAACAAGCAAGCCCAGATC
CTAGAGCCGAAGCCTGAACCTTCTCTTGAGATTAAGCCTGAGCAGGACGGTATGGAGCAT
GTTGGCAGAGATGACCCAAAGGCTCTTGGTGAAGAACCCAAACAAAGGAGAGGCAGTGCC
TCTGGGAGTGAGCCTGCTGGGGACAGTGACAGGGGAGGGGGCCCCGTTGAGCATTATCAC
CTCCATCTGTCTAGTTGCCACGAGTGTCTGGAACTTGAGAACAGCACCATTGAGTCAGTC
AAGTTTGCGTCTGCCGAGAACATTCCAGACCTTCCCTACGATTATAGCAGCAGTTTGGAG
AGTGTTGCTGATGAGACCTCCCCCGAAAGAGAAGGGAGGAGAGTCAACCTCACGGGAAAG
GCACCCAACATCCTCCTCTATGTGGGCTCCGACTCCCAGGAAGCCCTCGGCCGGTTCCAC
GAGGTCCGGTCTGTGCTGGCCGACTGTGTGGACATTGACAGTTATATTCTCTACCACCTG
CTGGAGGACAGTGCTCTCAGAGACCCGTGGACGGACAACTGTCTGCTGTTGGTCATTGCT
ACCAGGGAGTCCATTCCCGAAGACCTGTACCAGAAGTTCATGGCCTATCTTTCTCAGGGA
GGGAAGGTGTTGGGCCTGTCTTCATCCTTCACCTTTGGTGGCTTTCAGGTGACAAGCAAG
GGTGCACTGCACAAGACAGTCCAGAACTTGGTTTTCTCCAAGGCTGACCAGAGCGAGGTG
AAGCTCAGCGTCTTGAGCAGTGGCTGCAGGTACCAGGAAGGCCCCGTCCGGCTCAGCCCC
GGCAGGCTCCAGGGCCACCTGGAGAATGAGGACAAGGACAGGATGATTGTGCATGTGCCT
TTTGGAACTCGCGGGGGAGAAGCTGTTCTTTGCCAGGTGCACTTAGAACTACCTCCCAGC
TCCAACATAGTGCAAACTCCAGAAGATTTTAACTTGCTCAAGTCAAGCAATTTTAGAAGA
TACGAAGTCCTTAGAGAGATTCTGACAACCCTTGGCCTCAGCTGTGACATGAAACAAGTT
CCTGCCTTAACTCCTCTTTACTTGCTGTCAGCTGCGGAGGAAATCAGGGATCCTCTTATG
CAGTGGCTTGGGAAACATGTGGACTCCGAGGGAGAAATAAAATCCGGCCAGCTCTCTCTT
AGATTTGTTTCATCCTACGTGTCTGAAGTAGAAATAACCCCATCTTGTATACCTGTGGTG
ACCAACATGGAGGCCTTCTCATCAGAACATTTCAACTTAGAGATCTATCGCCAAAATCTG
CAGACCAAGCAGTTGGGGAAAGTAATTTTGTTTGCCGAAGTGACCCCCACAACGATGCGT
CTCCTGGATGGGCTGATGTTTCAGACACCGCAGGAAATGGGCTTAATAGTGATCGCGGCC
CGGCAGACCGAGGGCAAAGGACGGGGAGGGAATGTGTGGCTGAGCCCTGTGGGATGTGCT
CTTTCTACTCTGCTCATCTCCATTCCACTGAGATCCCAGCTGGGACAGAGGATCCCGTTT
GTCCAGCATCTGATGTCCGTGGCTGTCGTGGAAGCAGTGAGGTCCATTCCCGAGTATCAG
GATATCAACTTACGAGTGAAGTGGCCCAACGATATTTATTACAGTGACCTCATGAAGATC
GGCGGAGTTCTGGTTAACTCAACACTCATGGGAGAAACATTTTATATACTTATTGGCTGT
GGATTTAATGTGACTAACAGTAACCCTACCATCTGCATCAACGACCTCATCACAGAATAC
AATAAACAACACAAGGCAGAACTGAAGCCCTTAAGAGCCGATTATCTCATCGCCAGAGTC
GTGACTGTGCTGGAGAAACTGATCAAAGAGTTTCAGGACAAAGGGCCCAACAGCGTCCTT
CCCCTTTATTACCGATACTGGGTCCACAGTGGTCAGCAAGTCCATCTGGGCAGCGCAGAG
GGACCAAAGGTGTCCATCGTTGGCCTGGACGATTCTGGCTTCCTCCAGGTTCACCAGGAG
GGCGGCGAGGTTGTGACTGTGCACCCGGACGGCAACTCCTTCGACATGCTGAGAAACCTC
ATCCTCCCCAAACGGCGGTAA
Enzyme 7 GenBank Gene ID D23672 Link Image
Enzyme 7 GeneCard ID HLCS Link Image
Enzyme 7 GenAtlas ID HLCS Link Image
Enzyme 7 HGNC ID HGNC:4976 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Suzuki Y, Aoki Y, Ishida Y, Chiba Y, Iwamatsu A, Kishino T, Niikawa N, Matsubara Y, Narisawa K: Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA. Nat Genet. 1994 Oct;8(2):122-8. [PubMed Link Image]
  2. Yang X, Aoki Y, Li X, Sakamoto O, Hiratsuka M, Kure S, Taheri S, Christensen E, Inui K, Kubota M, Ohira M, Ohki M, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Minoshima S, Shimizu N, Narisawa K, Matsubara Y, Suzuki Y: Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiency. Hum Genet. 2001 Nov;109(5):526-34. Epub 2001 Oct 5. [PubMed Link Image]
  3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  4. Dahmane N, Ghezala GA, Gosset P, Chamoun Z, Dufresne-Zacharia MC, Lopes C, Rabatel N, Gassanova-Maugenre S, Chettouh Z, Abramowski V, Fayet E, Yaspo ML, Korn B, Blouin JL, Lehrach H, Poutska A, Antonarakis SE, Sinet PM, Creau N, Delabar JM: Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome. Genomics. 1998 Feb 15;48(1):12-23. [PubMed Link Image]
  5. Aoki Y, Suzuki Y, Sakamoto O, Li X, Takahashi K, Ohtake A, Sakuta R, Ohura T, Miyabayashi S, Narisawa K: Molecular analysis of holocarboxylase synthetase deficiency: a missense mutation and a single base deletion are predominant in Japanese patients. Biochim Biophys Acta. 1995 Dec 12;1272(3):168-74. [PubMed Link Image]
  6. Dupuis L, Leon-Del-Rio A, Leclerc D, Campeau E, Sweetman L, Saudubray JM, Herman G, Gibson KM, Gravel RA: Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. Hum Mol Genet. 1996 Jul;5(7):1011-6. [PubMed Link Image]
  7. Aoki Y, Suzuki Y, Li X, Sakamoto O, Chikaoka H, Takita S, Narisawa K: Characterization of mutant holocarboxylase synthetase (HCS): a Km for biotin was not elevated in a patient with HCS deficiency. Pediatr Res. 1997 Dec;42(6):849-54. [PubMed Link Image]
  8. Aoki Y, Li X, Sakamoto O, Hiratsuka M, Akaishi H, Xu L, Briones P, Suormala T, Baumgartner ER, Suzuki Y, Narisawa K: Identification and characterization of mutations in patients with holocarboxylase synthetase deficiency. Hum Genet. 1999 Feb;104(2):143-8. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5757
Enzyme 8 Name Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor
Enzyme 8 Synonyms
  1. 3-methylcrotonyl-CoA carboxylase 1
  2. MCCase subunit alpha
  3. 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha
  4. 3- methylcrotonyl-CoA carboxylase biotin-containing subunit
Enzyme 8 Gene Name MCCC1
Enzyme 8 Protein Sequence >Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor 
MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEI
ACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTS
AAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEG
YHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFN
DDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRK
KLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQL
RIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGV
RQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFE
AGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSS
SGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKC
SVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKV
FVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESD
KRESE
Enzyme 8 Number of Residues 725
Enzyme 8 Molecular Weight 80474
Enzyme 8 Theoretical pI 7.86
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 8 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 8 Reactions
  • ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-14
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 12382296 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q96RQ3 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name MCCA_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2178 bp 
ATGGCGGCGGCCTCTGCGGTGTCGGTGCTGCTGGTGGCGGCGGAGAGGAACCGGTGGCAT
CGTCTCCCGAGCCTGCTCCTGCCGCCGAGGACATGGGTGTGGAGGCAAAGAACCATGAAG
TACACAACAGCCACAGGAAGAAACATTACCAAGGTCCTCATTGCAAACAGAGGAGAAATT
GCCTGCAGGGTGATGCGCACAGCCAAAAAACTGGGTGTACAGACTGTGGCGGTTTATAGT
GAGGCTGACAGAAATTCCATGCATGTAGATATGGCAGATGAAGCATATTCCATCGGCCCC
GCTCCCTCCCAGCAGAGCTACCTATCTATGGAGAAAATCATTCAAGTGGCCAAGACCTCT
GCTGCACAGGCTATCCATCCAGGATGCGGTTTTCTTTCAGAAAACATGGAATTTGCTGAA
CTTTGTAAGCAAGAAGGAATTATTTTTATAGGCCCTCCTCCATCTGCAATTAGAGACATG
GGTATAAAGAGCACATCCAAATCCATAATGGCTGCTGCTGGAGTACCTGTTGTGGAGGGT
TATCATGGTGAGGACCAATCAGACCAGTGCCTGAAGGAACACGCCAGGAGAATTGGCTAT
CCTGTCATGATTAAAGCCGTCCGGGGTGGAGGAGGAAAAGGAATGAGGATTGTTAGATCA
GAACAAGAATTTCAAGAACAGTTAGAGTCAGCACGGAGAGAAGCTAAGAAGTCTTTCAAT
GATGATGCTATGCTGATCGAGAAGTTTGTAGACACACCGAGGCATGTAGAAGTCCAGGTG
TTTGGTGATCACCATGGCAATGCTGTGTACTTGTTTGAAAGAGACTGTAGTGTGCAGAGG
CGACATCAGAAGATCATTGAGGAGGCCCCAGCGCCTGGTATTAAATCTGAAGTAAGAAAA
AAGCTGGGAGAAGCTGCAGTCAGAGCTGCTAAAGCTGTAAATTATGTTGGAGCAGGGACT
GTGGAGTTTATTATGGACTCAAAACATAATTTCTGTTTCATGGAGATGAATACAAGGCTG
CAAGTGGAACATCCTGTTACTGAGATGATCACAGGAACTGACTTGGTGGAGTGGCAGCTT
AGAATTGCAGCAGGAGAGAAGATTCCTTTGAGCCAGGAAGAAATAACTCTGCAGGGCCAT
GCCTTCGAAGCTAGAATATATGCAGAAGATCCTAGCAATAACTTCATGCCTGTGGCAGGC
CCATTAGTGCACCTCTCTACTCCTCGAGCAGACCCTTCCACCAGGATTGAAACTGGAGTA
CGGCAAGGAGACGAAGTTTCCGTGCATTATGACCCCATGATTGCGAAGCTGGTCGTGTGG
GCAGCAGATCGCCAGGCGGCATTGACAAAACTGAGGTACAGCCTTCGTCAGTACAATATT
GTTGGACTGCACACCAACATTGACTTCTTACTCAACCTGTCTGGCCACCCAGAGTTTGAA
GCTGGGAACGTGCACACTGATTTCATCCCTCAACACCACAAACAGTTGTTGCTCAGTCGG
AAGGCTGCAGCCAAAGAGTCTTTATGCCAGGCAGCCCTGGGTCTCATCCTCAAGGAGAAA
GCCATGACCGACACTTTCACTCTTCAGGCACATGATCAATTCTCTCCATTTTCGTCTAGC
AGTGGAAGAAGACTGAATATCTCGTATACCAGAAACATGACTCTTAAAGATGGTAAAAAC
AATGTAGCCATAGCTGTAACGTATAACCATGATGGGTCTTATAGCATGCAGATTGAAGAT
AAAACTTTCCAAGTCCTTGGTAATCTTTACAGCGAGGGAGACTGCACTTACCTGAAATGT
TCTGTTAATGGAGTTGCTAGTAAAGCGAAGCTGATTATCCTGGAAAACACTATTTACCTA
TTTTCCAAGGAAGGAAGTATTGAGATTGACATTCCAGTCCCCAAATACTTATCTTCTGTG
AGCTCACAAGAAACTCAGGGCGGCCCCTTAGCTCCTATGACTGGAACCATTGAAAAGGTG
TTTGTCAAAGCTGGAGACAAAGTGAAAGCGGGAGATTCCCTCATGGTTATGATCGCCATG
AAGATGGAGCATACCATAAAGTCTCCAAAGGATGGCACAGTAAAGAAAGTGTTCTACAGA
GAAGGTGCTCAGGCCAACAGACACACTCCTTTAGTCGAGTTTGAGGAGGAAGAATCAGAC
AAAAGGGAATCGGAATAA
Enzyme 8 GenBank Gene ID AF310972 Link Image
Enzyme 8 GeneCard ID MCCC1 Link Image
Enzyme 8 GenAtlas ID MCCC1 Link Image
Enzyme 8 HGNC ID HGNC:6936 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3q27
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Obata K, Fukuda T, Morishita R, Abe S, Asakawa S, Yamaguchi S, Yoshino M, Ihara K, Murayama K, Shigemoto K, Shimizu N, Kondo I: Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase gene (MCCA): cDNA sequence, genomic organization, localization to chromosomal band 3q27, and expression. Genomics. 2001 Mar 1;72(2):145-52. [PubMed Link Image]
  2. Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed Link Image]
  3. Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5817
Enzyme 9 Name Biotinidase precursor
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name BTD
Enzyme 9 Protein Sequence >Biotinidase precursor 
MSGARSKLALFLCGCYVVALGAHTGEESVADHHEAEYYVAAVYEHPSILSLNPLALISRQ
EALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPSPQVVRW
NPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVF
SNNGTLVDRYRKHNLYFEAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRD
YKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAANVHHPVLGMTGSGIHTPLESF
WYHDMENPKSHLIIAQVAKNPVGLIGAENATGETDPSHSKFLKILSGDPYCEKDAQEVHC
DEATKWNVNAPPTFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYERPTLSKELYAL
GVFDGLHTVHGTYYIQVCALVRCGGLGFDTCGQEITEATGIFEFHLWGNFSTSYIFPLFL
TSGMTLEVPDQLGWENDHYFLRKSRLSSGLVTAALYGRLYERD
Enzyme 9 Number of Residues 523
Enzyme 9 Molecular Weight 58914
Enzyme 9 Theoretical pI 5.72
Enzyme 9 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation
Enzyme 9 Pathways
Enzyme 9 Reactions
  • biotin amide + H2O = biotin + NH3
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-21
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 468824 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P43251 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name BTD_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1632 bp 
ATGGCGCATGCGCATATTCAGGGCGGAAGGCGCGCTAAGAGCAGATTTGTGGTCTGCATT
ATGTCTGGAGCCAGAAGTAAGCTTGCTCTTTTCCTCTGCGGCTGTTACGTGGTTGCCCTG
GGAGCCCACACCGGGGAGGAGAGCGTGGCTGACCATCACGAGGCTGAATATTATGTGGCT
GCCGTGTATGAGCATCCATCCATCCTGAGTCTGAACCCTCTGGCTCTCATCAGCCGCCAA
GAGGCCTTGGAGCTCATGAACCAGAACCTTGACATCTATGAACAGCAAGTGATGACTGCA
GCCCAAAAGGATGTACAGATTATAGTGTTTCCAGAAGATGGCATTCATGGATTCAACTTT
ACAAGAACATCCATTTATCCATTTTTGGACTTCATGCCGTCTCCCCAGGTGGTCAGGTGG
AACCCATGCCTGGAGCCTCACCGCTTCAATGACACAGAGGTGCTCCAGCGCCTGAGTTGT
ATGGCCATCAGGGGAGATATGTTCTTGGTGGCCAATCTTGGGACAAAGGAGCCTTGTCAT
AGCAGTGACCCAAGGTGCCCAAAAGATGGGAGATACCAGTTCAACACAAATGTCGTGTTC
AGCAATAATGGAACCCTTGTTGACCGCTACCGTAAACACAACCTCTACTTTGAGGCAGCA
TTCGATGTTCCTCTTAAAGTGGATCTCATCACCTTTGATACCCCCTTTGCTGGCAGGTTT
GGCATCTTCACATGCTTTGATATATTGTTCTTTGACCCTGCCATCAGAGTCCTCAGAGAC
TACAAGGTGAAGCATGTTGTGTACCCAACTGCCTGGATGAACCAGCTCCCACTCTTGGCA
GCAATTGAGATTCAGAAAGCTTTTGCTGTTGCCTTTGGCATCAACGTTCTGGCAGCTAAT
GTCCACCACCCAGTTCTGGGGATGACAGGAAGTGGCATACACACCCCTCTGGAGTCCTTT
TGGTACCATGACATGGAAAATCCCAAAAGTCACCTTATAATTGCCCAGGTGGCCAAAAAT
CCAGTGGGTCTCATTGGTGCAGAGAATGCAACAGGTGAAACGGACCCATCCCATAGTAAG
TTTTTAAAAATTTTGTCAGGCGATCCGTACTGTGAGAAGGATGCTCAGGAAGTCCACTGT
GATGAGGCCACCAAGTGGAACGTGAATGCTCCTCCCACATTTCACTCTGAGATGATGTAT
GACAATTTCACCCTGGTCCCTGTCTGGGGAAAGGAAGGCTATCTCCACGTCTGTTCCAAT
GGCCTCTGCTGTTATTTACTTTACGAGAGGCCCACCTTATCCAAAGAGCTGTATGCCCTG
GGGGTCTTTGATGGGCTTCACACAGTACATGGCACTTACTACATCCAAGTGTGTGCCCTG
GTCAGGTGTGGGGGTCTTGGCTTCGACACCTGCGGACAGGAAATCACAGAGGCCACGGGG
ATATTTGAGTTTCACCTGTGGGGCAACTTCAGTACTTCCTATATCTTTCCTTTGTTTCTG
ACCTCAGGGATGACCCTAGAAGTCCCTGACCAGCTTGGCTGGGAGAATGACCACTATTTC
CTGAGGAAAAGTAGGCTGTCCTCTGGGCTGGTGACGGCGGCTCTCTATGGGCGCTTGTAT
GAGAGGGACTAG
Enzyme 9 GenBank Gene ID U03274 Link Image
Enzyme 9 GeneCard ID BTD Link Image
Enzyme 9 GenAtlas ID BTD Link Image
Enzyme 9 HGNC ID HGNC:1122 Link Image
Enzyme 9 Chromosome Location 3
Enzyme 9 Locus 3p25
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Cole H, Reynolds TR, Lockyer JM, Buck GA, Denson T, Spence JE, Hymes J, Wolf B: Human serum biotinidase. cDNA cloning, sequence, and characterization. J Biol Chem. 1994 Mar 4;269(9):6566-70. [PubMed Link Image]
  2. Knight HC, Reynolds TR, Meyers GA, Pomponio RJ, Buck GA, Wolf B: Structure of the human biotinidase gene. Mamm Genome. 1998 Apr;9(4):327-30. [PubMed Link Image]
  3. Pomponio RJ, Norrgard KJ, Hymes J, Reynolds TR, Buck GA, Baumgartner R, Suormala T, Wolf B: Arg538 to Cys mutation in a CpG dinucleotide of the human biotinidase gene is the second most common cause of profound biotinidase deficiency in symptomatic children. Hum Genet. 1997 Apr;99(4):506-12. [PubMed Link Image]
  4. Swango KL, Demirkol M, Huner G, Pronicka E, Sykut-Cegielska J, Schulze A, Mayatepek E, Wolf B: Partial biotinidase deficiency is usually due to the D444H mutation in the biotinidase gene. Hum Genet. 1998 May;102(5):571-5. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8120
Enzyme 10 Name Sodium-dependent multivitamin transporter
Enzyme 10 Synonyms
  1. Na(+-dependent multivitamin transporter
Enzyme 10 Gene Name SLC5A6
Enzyme 10 Protein Sequence >Sodium-dependent multivitamin transporter 
MSVGVSTSAPLSPTSGTSVGMSTFSIMDYVVFVLLLVLSLAIGLYHACRGWGRHTVGELL
MADRKMGCLPVALSLLATFQSAVAILGVPSEIYRFGTQYWFLGCCYFLGLLIPAHIFIPV
FYRLHLTSAYEYLELRFNKTVRVCGTVTFIFQMVIYMGVVLYAPSLALNAVTGFDLWLSV
LALGIVCTVYTALGGLKAVIWTDVFQTLVMFLGQLAVIIVGSAKVGGLGRVWAVASQHGR
ISGFELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSRTEKAAVLSCYAVFPF
QQVSLCVGCLIGLVMFAYYQEYPMSIQQAQAAPDQFVLYFVMDLLKGLPGLPGLFIACLF
SGSLSTISSAFNSLATVTMEDLIRPWFPEFSEARAIMLSRGLAFGYGLLCLGMAYISSQM
GPVLQAAISIFGMVGGPLLGLFCLGMFFPCANPPGAVVGLLAGLVMAFWIGIGSIVTSMG
FSMPPSPSNGSSFSLPTNLTVATVTTLMPLTTFSKPTGLQRFYSLSYLWYSAHNSTTVIV
VGLIVSLLTGRMRGRSLNPATIYPVLPKLLSLLPLSCQKRLHCRSYGQDHLDTGLFPEKP
RNGVLGDSRDKEAMALDGTAYQGSSSTCILQETSL
Enzyme 10 Number of Residues 635
Enzyme 10 Molecular Weight 68703
Enzyme 10 Theoretical pI 8.32
Enzyme 10 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 10 General Function Amino acid transport and metabolism
Enzyme 10 Specific Function Transports pantothenate, biotin and lipoate in the presence of sodium
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 24-44 68-88 101-121 143-163 176-196 199-219 256-276 297-317 336-356 396-416 428-448 456-476 528-548
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 5006439 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9Y289 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name SC5A6_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1908 bp 
ATGAGTGTAGGGGTGAGCACCTCAGCCCCTCTTTCCCCAACCTCGGGCACAAGCGTGGGC
ATGTCTACCTTCTCCATCATGGACTATGTGGTGTTCGTCCTGCTGCTGGTTCTCTCTCTT
GCCATTGGGCTCTACCATGCTTGTCGTGGCTGGGGCCGGCATACTGTTGGTGAGCTGCTG
ATGGCGGACCGCAAAATGGGCTGCCTTCCGGTGGCACTGTCCCTGCTGGCCACCTTCCAG
TCAGCCGTGGCCATCCTGGGTGTGCCGTCAGAGATCTACCGATTTGGGACCCAATATTGG
TTCCTGGGCTGCTGCTACTTTCTGGGGCTGCTGATACCTGCACACATCTTCATCCCCGTT
TTCTACCGCCTGCATCTCACCAGTGCCTATGAGTACCTGGAGCTTCGATTCAATAAAACT
GTGCGAGTGTGTGGAACTGTGACCTTCATCTTTCAGATGGTGATCTACATGGGAGTTGTG
CTCTATGCTCCGTCATTGGCTCTCAATGCAGTGACTGGCTTTGATCTGTGGCTGTCCGTG
CTGGCCCTGGGCATTGTCTGTACCGTCTATACAGCTCTGGGTGGGCTGAAGGCCGTCATC
TGGACAGATGTGTTCCAGACACTGGTCATGTTCCTCGGGCAGCTGGCAGTTATCATCGTG
GGGTCAGCCAAGGTGGGCGGCTTGGGGCGTGTGTGGGCCGTGGCTTCCCAGCACGGCCGC
ATCTCTGGGTTTGAGCTGGATCCAGACCCCTTTGTGCGGCACACCTTCTGGACCTTGGCC
TTCGGGGGTGTCTTCATGATGCTCTCCTTATACGGGGTGAACCAGGCTCAGGTGCAGCGG
TACCTCAGTTCCCGCACGGAGAAGGCTGCTGTGCTCTCCTGTTATGCAGTGTTCCCCTTC
CAGCAGGTGTCCCTCTGCGTGGGCTGCCTCATTGGCCTGGTCATGTTCGCGTATTACCAG
GAGTATCCCATGAGCATTCAGCAGGCTCAGGCAGCCCCAGACCAGTTCGTCCTGTACTTT
GTGATGGATCTCCTGAAGGGCCTGCCAGGCCTGCCAGGGCTCTTCATTGCCTGCCTCTTC
AGCGGCTCTCTCAGCACTATATCCTCTGCTTTTAATTCATTGGCAACTGTTACGATGGAA
GACCTGATTCGACCTTGGTTCCCTGAGTTCTCTGAAGCCCGGGCCATCATGCTTTCCAGA
GGCCTTGCCTTTGGCTATGGGCTGCTTTGTCTAGGAATGGCCTATATTTCCTCCCAGATG
GGACCTGTGCTGCAGGCAGCAATCAGCATCTTTGGCATGGTTGGGGGACCGCTGCTGGGA
CTCTTCTGCCTTGGAATGTTCTTTCCATGTGCTAACCCTCCTGGTGCTGTTGTGGGCCTG
TTGGCTGGGCTCGTCATGGCCTTCTGGATTGGCATCGGGAGCATCGTGACCAGCATGGGC
TTCAGCATGCCACCCTCTCCCTCTAATGGGTCCAGCTTCTCCCTGCCCACCAATCTAACC
GTTGCCACTGTGACCACACTGATGCCCTTGACTACCTTCTCCAAGCCCACAGGGCTGCAG
CGGTTCTATTCCTTGTCTTACTTATGGTACAGTGCTCACAACTCCACCACAGTGATTGTG
GTGGGCCTGATTGTCAGTCTACTCACTGGGAGAATGCGAGGCCGGTCCCTGAACCCTGCA
ACCATTTACCCAGTGTTGCCAAAGCTCCTGTCCCTCCTTCCGTTGTCCTGTCAGAAGCGG
CTCCACTGCAGGAGCTACGGCCAGGACCACCTCGACACTGGCCTGTTTCCTGAGAAGCCG
AGGAATGGTGTGCTGGGGGACAGCAGAGACAAGGAGGCCATGGCCCTGGATGGCACAGCC
TATCAGGGGAGCAGCTCCACCTGCATCCTCCAGGAGACCTCCCTGTGA
Enzyme 10 GenBank Gene ID AF116241 Link Image
Enzyme 10 GeneCard ID SLC5A6 Link Image
Enzyme 10 GenAtlas ID SLC5A6 Link Image
Enzyme 10 HGNC ID HGNC:11041 Link Image
Enzyme 10 Chromosome Location 2
Enzyme 10 Locus 2p23
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Wang H, Huang W, Fei YJ, Xia H, Yang-Feng TL, Leibach FH, Devoe LD, Ganapathy V, Prasad PD: Human placental Na+-dependent multivitamin transporter. Cloning, functional expression, gene structure, and chromosomal localization. J Biol Chem. 1999 May 21;274(21):14875-83. [PubMed Link Image]
  2. Prasad PD, Wang H, Huang W, Fei YJ, Leibach FH, Devoe LD, Ganapathy V: Molecular and functional characterization of the intestinal Na+-dependent multivitamin transporter. Arch Biochem Biophys. 1999 Jun 1;366(1):95-106. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 13089
Enzyme 11 Name Propionyl-CoA carboxylase alpha subunit
Enzyme 11 Synonyms
  1. Propionyl Coenzyme A carboxylase, alpha polypeptide, isoform CRA_c
  2. Propionyl Coenzyme A carboxylase, alpha polypeptide
Enzyme 11 Gene Name PCCA
Enzyme 11 Protein Sequence >Propionyl-CoA carboxylase alpha subunit 
MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNE
KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKS
YLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIES
KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRD
GFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVV
EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPV
TECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQY
QEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTH
NIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRA
QHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLAS
PLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSS
VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGE
GDLLVELE
Enzyme 11 Number of Residues 728
Enzyme 11 Molecular Weight 80060
Enzyme 11 Theoretical pI 7.56
Enzyme 11 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 18252315 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q8WXQ7 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q8WXQ7_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AF385926 Link Image
Enzyme 11 GeneCard ID Q8WXQ7 Link Image
Enzyme 11 GenAtlas ID PCCA Link Image
Enzyme 11 HGNC ID HGNC:8653 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Campeau E, Desviat LR, Leclerc D, Wu X, Perez B, Ugarte M, Gravel RA: Structure of the PCCA gene and distribution of mutations causing propionic acidemia. Mol Genet Metab. 2001 Sep-Oct;74(1-2):238-47. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16426
Enzyme 12 Name cDNA, FLJ93758, Homo sapiens biotinidase (BTD), mRNA (Biotinidase, isoform CRA_a)
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name BTD
Enzyme 12 Protein Sequence >cDNA, FLJ93758, Homo sapiens biotinidase (BTD), mRNA (Biotinidase, isoform CRA_a) 
MAHAHIQGGRRAKSRFVVCIMSGARSKLALFLCGCYVVALGAHTGEESVADHHEAEYYVA
AVYEHPSILSLNPLALISRQEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNF
TRTSIYPFLDFMPSPQVVRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCH
SSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYFEAAFDVPLKVDLITFDTPFAGRF
GIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN
VHHPVLGMTGSGIHTPLESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETDPSHSK
FLKILSGDPYCEKDAQEVHCDEATKWNVNAPPTFHSEMMYDNFTLVPVWGKEGYLHVCSN
GLCCYLLYERPTLSKELYALGVFDGLHTVHGTYYIQVCALVRCGGLGFDTCGQEITEATG
IFEFHLWGNFSTSYIFPLFLTSGMTLEVPDQLGWENDHYFLRKSRLSSGLVTAALYGRLY
ERD
Enzyme 12 Number of Residues 543
Enzyme 12 Molecular Weight 61134
Enzyme 12 Theoretical pI 6.22
Enzyme 12 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID B2R865 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B2R865_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK313252 Link Image
Enzyme 12 GeneCard ID B2R865 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 17058
Enzyme 13 Name cDNA, FLJ96567, highly similar to Homo sapiens propionyl Coenzyme A carboxylase, alpha polypeptide(PCCA), mRNA
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >cDNA, FLJ96567, highly similar to Homo sapiens propionyl Coenzyme A carboxylase, alpha polypeptide(PCCA), mRNA 
MLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKM
GIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGF
LSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEA
VRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFID
NPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALAR
AVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHK
QADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPLHLPGVRVDSGIQPGSDISIYY
DPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLF
DVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRAQHFQENSRMPVIKPDIANWELSVKL
HDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLSVSVDGTQRTVQCLSREAGGNM
SIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQ
EICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE
Enzyme 13 Number of Residues 703
Enzyme 13 Molecular Weight 77415
Enzyme 13 Theoretical pI 7.07
Enzyme 13 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B2RDE0 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B2RDE0_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK315503 Link Image
Enzyme 13 GeneCard ID B2RDE0 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 17059
Enzyme 14 Name Putative uncharacterized protein ACACB
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name ACACB
Enzyme 14 Protein Sequence >Putative uncharacterized protein ACACB 
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLQDTQPGRASLPQRPQRGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGT
QGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAG
SSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHRDF
TVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPE
DLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKLPE
LLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGKRI
SVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQS
EIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLA
IFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPA
AQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDEGF
KPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALK
ELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGALNV
ADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIMNG
CHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSA
GKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVARLE
LDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIKLK
EWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFPSQ
QIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRVEI
FSKARDADANTSGMVGGVRSLSFTSVWVLSPPAHYDKCVINLREQFKPDMSQVLDCIFSH
AQVAKKNQLVIMLIDELCGPDPSLSDELISILNELTQLSKSEHCKVALRARQILIASHLP
SYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLE
VYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLRHSTELF
MDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLFSEARTSLYSEDDCKS
LREEPIHILNVSIQCADHLEDEALVPILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKF
FTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVE
VTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFL
NFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNE
SGYYLDISLYKEVTDSRSGNIMFHSFGNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGT
TYIYDFPEMFRQALFKLWGSPDKYPKDILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFK
MRFKTQEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEGIPKIYVAANSGAR
IGMAEEIKHMFHVAWVDPEDPHKGFKYLYLTPQDYTRISSLNSVHCKHIEEGGESRYMIT
DIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVEN
SHIILTGASALNKVLGREVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMP
KDNHSPVPIITPTDPIDREIEFLPSRAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEI
MAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSA
YKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIP
PYAELRGGSWVVIDATINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPA
YKKLMEQLGEPDLSDKDRKDLEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVIS
DILEWKTARTFLYWRLRRLLLEDQVKQEILQASGELSHVHIQSMLRRWFVETEGAVKAYL
WDNNQVVVQWLEQHWQAGDGPRSTIRENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLS
QHISPAERAQVVHLLSTMDSPAST
Enzyme 14 Number of Residues 2484
Enzyme 14 Molecular Weight 279292
Enzyme 14 Theoretical pI 6.47
Enzyme 14 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 14 General Function Lipid transport and metabolism
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID A6NLM9 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A6NLM9_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AC007637 Link Image
Enzyme 14 GeneCard ID A6NLM9 Link Image
Enzyme 14 GenAtlas ID ACACB Link Image
Enzyme 14 HGNC ID HGNC:85 Link Image
Enzyme 14 Chromosome Location 12
Enzyme 14 Locus 12q24.11
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 17060
Enzyme 15 Name Putative uncharacterized protein DKFZp686B20267
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name DKFZp686B20267
Enzyme 15 Protein Sequence >Putative uncharacterized protein DKFZp686B20267 
MEKIIQVAKTSAAQHIQSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGG
GGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVY
LFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHN
FCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAED
PSNNFMPVAGPLVHLSTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTK
LRYSLRQYNIVGLPTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAAKESLCQ
AALGLILKEKAMTDTFTLQAHDQFSPFSSSSGRRLNISYTRNMTLKDGKNNVAIAVTYNH
DGSYSMQIEDKTFQVLGNLYSEGDCTYLKCSVNGVASKAKLIILENTIYLFSKEGSIEID
IPVPKYLSSVSSQETQGGPLAPMTGTIEKVFVKAGDKVKAGDSLMVMIAMKMEHTIKSPK
DGTVKKVFYREGAQANRHTPLVEFEEEESDKRESE
Enzyme 15 Number of Residues 575
Enzyme 15 Molecular Weight 63968
Enzyme 15 Theoretical pI 6.86
Enzyme 15 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
—
Component
—
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q68D27 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q68D27_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID CR749608 Link Image
Enzyme 15 GeneCard ID Q68D27 Link Image
Enzyme 15 GenAtlas ID DKFZp686B20267 Link Image
Enzyme 15 HGNC ID HGNC:6936 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available