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Human Metabolome Database Version 2.5

 

Showing metabocard for S-Methylmalonyl-CoA (HMDB02310)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:47
Update Date 2009-05-05 20:59:14
Accession Number HMDB02310
Secondary Accession Numbers Not Available
Common Name S-Methylmalonyl-CoA
Description Methylmalonyl-CoA is an intermediate in the metabolism of Propanoate. It is a substrate for Malonyl-CoA decarboxylase (mitochondrial), Methylmalonyl-CoA mutase (mitochondrial) and Methylmalonyl-CoA epimerase (mitochondrial).
Synonyms
  1. (S)-Methylmalonyl-CoA
  2. (S)-Methylmalonyl-Coenzyme A
Chemical IUPAC Name (2S)-2-[2-[3-[[4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxy-2-hydroxy-3,3-dimethyl-butanoyl]amino]propanoylamino]ethylsulfanylcarbonyl]propanoic acid
Chemical Formula C25H40N7O19P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Short chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • secondary carboxylic acid amide
  • thiocarboxylic acid ester
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Lipid biosynthesis, Fatty acid transport
Application
—
Source
  • Endogenous
Average Molecular Weight 867.607
Monoisotopic Molecular Weight 867.131226
Isomeric SMILES C[C@@H](C(O)=O)C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12
Canonical SMILES CC(C(O)=O)C(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12
KEGG Compound ID C00683 Link Image
BioCyc ID D-METHYL-MALONYL-COA Link Image
BiGG ID 35689 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB02310 Link Image
Metagene Link HMDB02310 Link Image
METLIN ID 6609 Link Image
PubChem Compound 439291 Link Image
PubChem Substance 3952 Link Image
ChEBI ID Not Available
CAS Registry Number 73173-91-8
InChI Identifier InChI=1/C25H40N7O19P3S/c1-12(23(37)38)24(39)55-7-6-27-14(33)4-5-28-21(36)18(35)25(2,3)9-48-54(45,46)51-53(43,44)47-8-13-17(50-52(40,41)42)16(34)22(49-13)32-11-31-15-19(26)29-10-30-20(15)32/h10-13,16-18,22,34-35H,4-9H2,1-3H3,(H,27,33)(H,28,36)(H,37,38)(H,43,44)(H,45,46)(H2,26,29,30)(H2,40,41,42)/t12-,13?,16+,17+,18-,22?/m0/s1
Synthesis Reference Mutka, Sarah C.; Bondi, Shana M.; Carney, John R.; Da Silva, Nancy A.; Kealey, James T. Metabolic pathway engineering for complex polyketide biosynthesis in Saccharomyces cerevisiae .FEMS Yeast Research (2006), 6(1), 40-47.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.57 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -5
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.60 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • mitochondria
  • peroxisome
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Propanoate Metabolism SMP00016 Link Image map00640 Link Image
Threonine and 2-Oxobutanoate Degradation SMP00452 Link Image
General References Not Available
Metabolic Enzymes
  1. Methylmalonyl-CoA epimerase, mitochondrial precursor
  2. Propionyl-CoA carboxylase beta chain, mitochondrial precursor
  3. Hypothetical protein MCEE
  4. Propionyl-CoA carboxylase alpha subunit
Enzyme 1 [top]
Enzyme 1 ID 5488
Enzyme 1 Name Methylmalonyl-CoA epimerase, mitochondrial precursor
Enzyme 1 Synonyms
  1. DL-methylmalonyl-CoA racemase
Enzyme 1 Gene Name MCEE
Enzyme 1 Protein Sequence >Methylmalonyl-CoA epimerase, mitochondrial precursor 
MARVLKAAAANAVGLFSRLQAPIPTVRASSTSQPLDQVTGSVWNLGRLNHVAIAVPDLEK
AAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKNKAGGM
HHICIEVDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQA
Enzyme 1 Number of Residues 176
Enzyme 1 Molecular Weight 18749
Enzyme 1 Theoretical pI 9.68
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function (R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 14010614 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q96PE7 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name MCEE_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >531 bp 
ATGGCGCGGGTGCTGAAGGCTGCAGCCGCGAATGCCGTAGGGCTTTTTTCCAGACTTCAA
GCTCCCATTCCAACAGTAAGAGCTTCTTCCACATCACAGCCCTTGGATCAAGTGACAGGT
TCTGTGTGGAACCTGGGTCGACTCAACCATGTAGCCATAGCAGTGCCAGATTTGGAAAAG
GCTGCAGCATTTTATAAGAATATTCTGGGGGCCCAGGTAAGTGAAGCGGTCCCTCTTCCT
GAACATGGAGTATCTGTTGTTTTTGTCAACCTGGGAAATACCAAGATGGAACTGCTTCAT
CCATTGGGACGTGACAGTCCAATTGCAGGTTTTCTGCAGAAAAACAAGGCTGGAGGAATG
CATCACATCTGCATCGAGGTGGATAATATTAATGCAGCTGTGATGGATTTGAAAAAAAAG
AAGATCCGCAGTCTAAGTGAAGAGGTCAAAATAGGAGCACATGGAAAACCAGTGATTTTT
CTCCATCCTAAAGACTGTGGTGGAGTCCTTGTGGAACTGGAGCAAGCTTGA
Enzyme 1 GenBank Gene ID AF364547 Link Image
Enzyme 1 GeneCard ID MCEE Link Image
Enzyme 1 GenAtlas ID MCEE Link Image
Enzyme 1 HGNC ID HGNC:16732 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Bobik TA, Rasche ME: Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements. Implications for decoding the human genome. J Biol Chem. 2001 Oct 5;276(40):37194-8. Epub 2001 Jul 31. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5490
Enzyme 2 Name Propionyl-CoA carboxylase beta chain, mitochondrial precursor
Enzyme 2 Synonyms
  1. PCCase subunit beta
  2. Propanoyl-CoA:carbon dioxide ligase subunit beta
Enzyme 2 Gene Name PCCB
Enzyme 2 Protein Sequence >Propionyl-CoA carboxylase beta chain, mitochondrial precursor 
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHK
RGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVY
VFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIF
LRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVT
QEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVP
ELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPK
VASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFA
EATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVE
AAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
Enzyme 2 Number of Residues 539
Enzyme 2 Molecular Weight 58216
Enzyme 2 Theoretical pI 7.69
Enzyme 2 GO Classification
Function
  • catalytic activity
  • ligase activity
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-23
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 312812 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P05166 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PCCB_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID X73424 Link Image
Enzyme 2 GeneCard ID PCCB Link Image
Enzyme 2 GenAtlas ID PCCB Link Image
Enzyme 2 HGNC ID HGNC:8654 Link Image
Enzyme 2 Chromosome Location 3
Enzyme 2 Locus 3q21-q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8730
Enzyme 3 Name Hypothetical protein MCEE
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name MCEE
Enzyme 3 Protein Sequence >Hypothetical protein MCEE 
MARVLKAAAANAVGLFSRLQAPIPTVRASSTSQPLDQVTGSVWNLGRLNHVAIAVPDLEK
AAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKNKAGGM
HHICIEVDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQA
Enzyme 3 Number of Residues 176
Enzyme 3 Molecular Weight 18749
Enzyme 3 Theoretical pI 9.68
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals Not Available
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 62822199 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q53TP1 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q53TP1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >531 bp 
ATGGCGCGGGTGCTGAAGGCTGCAGCCGCGAATGCCGTAGGGCTTTTTTCCAGACTTCAA
GCTCCCATTCCAACAGTAAGAGCTTCTTCCACATCACAGCCCTTGGATCAAGTGACAGGT
TCTGTGTGGAACCTGGGTCGACTCAACCATGTAGCCATAGCAGTGCCAGATTTGGAAAAG
GCTGCAGCATTTTATAAGAATATTCTGGGGGCCCAGGTAAGTGAAGCGGTCCCTCTTCCT
GAACATGGAGTATCTGTTGTTTTTGTCAACCTGGGAAATACCAAGATGGAACTGCTTCAT
CCATTGGGACGTGACAGTCCAATTGCAGGTTTTCTGCAGAAAAACAAGGCTGGAGGAATG
CATCACATCTGCATCGAGGTGGATAATATTAATGCAGCTGTGATGGATTTGAAAAAAAAG
AAGATCCGCAGTCTAAGTGAAGAGGTCAAAATAGGAGCACATGGAAAACCAGTGATTTTT
CTCCATCCTAAAGACTGTGGTGGAGTCCTTGTGGAACTGGAGCAAGCTTGA
Enzyme 3 GenBank Gene ID AC007881 Link Image
Enzyme 3 GeneCard ID MCEE Link Image
Enzyme 3 GenAtlas ID MCEE Link Image
Enzyme 3 HGNC ID HGNC:16732 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13089
Enzyme 4 Name Propionyl-CoA carboxylase alpha subunit
Enzyme 4 Synonyms
  1. Propionyl Coenzyme A carboxylase, alpha polypeptide, isoform CRA_c
  2. Propionyl Coenzyme A carboxylase, alpha polypeptide
Enzyme 4 Gene Name PCCA
Enzyme 4 Protein Sequence >Propionyl-CoA carboxylase alpha subunit 
MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNE
KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKS
YLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIES
KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRD
GFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVV
EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPV
TECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQY
QEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTH
NIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRA
QHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLAS
PLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSS
VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGE
GDLLVELE
Enzyme 4 Number of Residues 728
Enzyme 4 Molecular Weight 80060
Enzyme 4 Theoretical pI 7.56
Enzyme 4 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 4 General Function Not Available
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 18252315 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8WXQ7 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q8WXQ7_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AF385926 Link Image
Enzyme 4 GeneCard ID Q8WXQ7 Link Image
Enzyme 4 GenAtlas ID PCCA Link Image
Enzyme 4 HGNC ID HGNC:8653 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 4 Metabolite References Not Available