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Human Metabolome Database Version 2.5

 

Showing metabocard for R-Methylmalonyl-CoA (HMDB02255)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:44
Update Date 2009-05-05 20:59:19
Accession Number HMDB02255
Secondary Accession Numbers Not Available
Common Name R-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 Not Available
Chemical IUPAC Name (2R)-3-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethylsulfanyl]-2-methyl-3-oxopropanoic 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(O)C1OP(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 C01213 Link Image
BioCyc ID METHYL-MALONYL-COA Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB02255 Link Image
Metagene Link HMDB02255 Link Image
METLIN ID 6577 Link Image
PubChem Compound 449534 Link Image
PubChem Substance 4435 Link Image
ChEBI ID Not Available
CAS Registry Number 73173-92-9
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?/m1/s1
Synthesis Reference Not Available
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]; -6.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Propanoate Metabolism SMP00016 Link Image map00640 Link Image
Threonine and 2-Oxobutanoate Degradation SMP00452 Link Image
General References
  1. Michenfelder M, Hull WE, Retey J: Quantitative measurement of the error in the cryptic stereospecificity of methylmalonyl-CoA mutase. Eur J Biochem. 1987 Nov 2;168(3):659-67. [PubMed Link Image]
Metabolic Enzymes
  1. Methylmalonyl-CoA epimerase, mitochondrial precursor
  2. Methylmalonyl-CoA mutase, mitochondrial precursor
  3. Hypothetical protein MCEE
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 5489
Enzyme 2 Name Methylmalonyl-CoA mutase, mitochondrial precursor
Enzyme 2 Synonyms
  1. MCM
  2. Methylmalonyl-CoA isomerase
Enzyme 2 Gene Name MUT
Enzyme 2 Protein Sequence >Methylmalonyl-CoA mutase, mitochondrial precursor 
MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLI
WHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESN
KFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLE
KMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMK
IIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDE
FAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTE
QDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPK
VADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARID
SGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTEC
AASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSA
IKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQ
AVDADVHAVGVSTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSN
VFGPGTRIPKAAVQVLDDIEKCLEKKQQSV
Enzyme 2 Number of Residues 750
Enzyme 2 Molecular Weight 83121
Enzyme 2 Theoretical pI 6.92
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cobalt ion binding
  • intramolecular transferase activity
  • ion binding
  • isomerase activity
  • methylmalonyl-CoA mutase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Involved in the degradation of several amino acids, odd- chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (R)-methylmalonyl-CoA = succinyl-CoA
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 187452 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P22033 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name MUTA_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2253 bp 
ATGTTAAGAGCTAAGAATCAGCTTTTTTTACTTTCACCTCATTACCTGAGGCAGGTAAAA
GAATCATCAGGCTCCAGGCTCATACAGCAACGACTTCTACACCAGCAACAGCCCCTTCAC
CCAGAATGGGCTGCCCTGGCTAAAAAGCAGCTGAAAGGCAAAAACCCAGAAGACCTAATA
TGGCACACCCCGGAAGGGATCTCTATAAAACCCTTGTATTCCAAGAGAGATACTATGGAC
TTACCTGAAGAACTTCCAGGAGTGAAGCCATTCACACGTGGACCATATCCTACCATGTAT
ACCTTTAGGCCCTGGACCATCCGCCAGTATGCTGGTTTTAGTACTGTGGAAGAAAGCAAT
AAGTTCTATAAGGACAACATTAAGGCTGGTCAGCAGGGATTATCAGTTGCCTTTGATCTG
GCGACACATCGTGGCTATGATTCAGACAACCCTCGAGTTCGTGGTGATGTTGGAATGGCT
GGAGTTGCTATTGACACTGTGGAAGATACCAAAATTCTTTTTGATGGAATTCCTTTAGAA
AAAATGTCAGTTTCCATGACTATGAATGGAGCAGTTATTCCAGTTCTTGCAAATTTTATA
GTAACTGGAGAAGAACAAGGTGTACCTAAAGAGAAACTTACTGGTACCATCCAAAATGAT
ATACTAAAGGAATTTATGGTTCGAAATACATACATTTTTCCTCCAGAACCATCCATGAAA
ATTATTGCTGACATATTTGAATATACAGCAAAGCACATGCCAAAATTTAATTCAATTTCA
ATTAGTGGATACCATATGCAGGAAGCAGGGGCTGATGCCATTCTGGAGCTGGCCTATACT
TTAGCAGATGGATTGGAGTACTCTAGAACTGGACTCCAGGCTGGCCTGACAATTGATGAA
TTTGCACCAAGGTTGTCTTTCTTCTGGGGAATTGGAATGAATTTCTATATGGAAATAGCA
AAGATGAGAGCTGGTAGAAGACTCTGGGCTCACTTAATAGAGAAAATGTTTCAGCCTAAA
AACTCAAAATCTCTTCTTCTAAGAGCACACTGTCAGACATCTGGATGGTCACTTACTGAG
CAGGATCCCTACAATAATATTGTCCGTACTGCAATAGAAGCAATGGCAGCAGTATTTGGA
GGGACTCAGTCTTTGCACACAAATTCTTTTGATGAAGCTTTGGGTTTGCCAACTGTGAAA
AGTGCTCGAATTGCCAGGAACACACAAATCATCATTCAAGAAGAATCTGGGATTCCCAAA
GTGGCTGATCCTTGGGGAGGTTCTTACATGATGGAATGTCTCACAAATGATGTTTATGAT
GCTGCTTTAAAGCTCATTAATGAAATTGAAGAAATGGGTGGAATGGCCAAAGCTGTAGCT
GAGGGAATACCTAAACTTCGAATTGAAGAATGTGCTGCCCGAAGACAAGCTAGAATAGAT
TCTGGTTCTGAAGTAATTGTTGGAGTAAATAAGTACCAGTTGGAAAAAGAAGACGCTGTA
GAAGTTCTGGCAATTGATAATACTTCAGTGCGAAACAGGCAGATTGAAAAACTTAAGAAG
ATCAAATCCAGCAGGGATCAAGCTTTGGCTGAACATTGTCTTGCTGCACTAACCGAATGT
GCTGCTAGCGGAGATGGAAATATCCTGGCTCTTGCAGTGGATGCATCTCGGGCAAGATGT
ACAGTGGGAGAAATCACAGATGCCCTGAAAAAGGTATTTGGTGAACATAAAGCGAATGAT
CGAATGGTGAGTGGAGCATATCGCCAGGAATTTGGAGAAAGTAAAGAGATAACATCTGCT
ATCAAGAGGGTTCATAAATTCATGGAACGTGAAGGTCGCAGACCTCGTCTTCTTGTAGCA
AAAATGGGACAAGATGGCCATGACAGAGGAGCAAAAGTTATTGCTACAGGATTTGCTGAT
CTTGGTTTTGATGTGGACATAGGCCCTCTTTTCCAGACTCCTCGTGAAGTGGCCCAGCAG
GCTGTGGATGCGGATGTGCATGCTGTGGGCGTAAGCACCCTCGCTGCTGGTCATAAAACC
CTAGTTCCTGAACTCATCAAAGAACTTAACTCCCTTGGACGGCCAGATATTCTTGTCATG
TGTGGAGGGGTGATACCACCTCAGGATTATGAATTTCTGTTTGAAGTTGGTGTTTCCAAT
GTATTTGGTCCTGGGACTCGAATTCCAAAGGCTGCCGTTCAGGTGCTTGATGATATTGAG
AAGTGTTTGGAAAAGAAGCAGCAATCTGTATAA
Enzyme 2 GenBank Gene ID M65131 Link Image
Enzyme 2 GeneCard ID MUT Link Image
Enzyme 2 GenAtlas ID MUT Link Image
Enzyme 2 HGNC ID HGNC:7526 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6p21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Jansen R, Kalousek F, Fenton WA, Rosenberg LE, Ledley FD: Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction. Genomics. 1989 Feb;4(2):198-205. [PubMed Link Image]
  2. Nham SU, Wilkemeyer MF, Ledley FD: Structure of the human methylmalonyl-CoA mutase (MUT) locus. Genomics. 1990 Dec;8(4):710-6. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Crane AM, Ledley FD: Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia. Am J Hum Genet. 1994 Jul;55(1):42-50. [PubMed Link Image]
  5. Ledley FD, Rosenblatt DS: Mutations in mut methylmalonic acidemia: clinical and enzymatic correlations. Hum Mutat. 1997;9(1):1-6. [PubMed Link Image]
  6. Raff ML, Crane AM, Jansen R, Ledley FD, Rosenblatt DS: Genetic characterization of a MUT locus mutation discriminating heterogeneity in mut0 and mut- methylmalonic aciduria by interallelic complementation. J Clin Invest. 1991 Jan;87(1):203-7. [PubMed Link Image]
  7. Jansen R, Ledley FD: Heterozygous mutations at the mut locus in fibroblasts with mut0 methylmalonic acidemia identified by polymerase-chain-reaction cDNA cloning. Am J Hum Genet. 1990 Nov;47(5):808-14. [PubMed Link Image]
  8. Crane AM, Jansen R, Andrews ER, Ledley FD: Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria. J Clin Invest. 1992 Feb;89(2):385-91. [PubMed Link Image]
  9. Crane AM, Martin LS, Valle D, Ledley FD: Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase. Hum Genet. 1992 May;89(3):259-64. [PubMed Link Image]
  10. Qureshi AA, Crane AM, Matiaszuk NV, Rezvani I, Ledley FD, Rosenblatt DS: Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria. J Clin Invest. 1994 Apr;93(4):1812-9. [PubMed Link Image]
  11. Adjalla CE, Hosack AR, Matiaszuk NV, Rosenblatt DS: A common mutation among blacks with mut- methylmalonic aciduria. Hum Mutat. 1998;Suppl 1:S248-50. [PubMed Link Image]
  12. Adjalla CE, Hosack AR, Gilfix BM, Lamothe E, Sun S, Chan A, Evans S, Matiaszuk NV, Rosenblatt DS: Seven novel mutations in mut methylmalonic aciduria. Hum Mutat. 1998;11(4):270-4. [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