| Accession | TIGR03081 |
| Name | metmalonyl_epim |
| Function | methylmalonyl-CoA epimerase |
| Gene Symbol | mce |
| Trusted Cutoff | 114.95 |
| Domain Trusted Cutoff | 114.95 |
| Noise Cutoff | 60.30 |
| Domain Noise Cutoff | 60.30 |
| Isology Type | equivalog |
| EC Number | 5.1.99.1 |
| HMM Length | 129 |
| Author | Haft DH |
| Entry Date | Sep 28 2006 8:13AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer. |
| References | RN [1]
RM PMID: 11481338
RT Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements. Implications for decoding the human genome.
RA Bobik TA, Rasche ME
RL J Biol Chem. 2001 Oct 5;276(40):37194-8.
RN [2]
RM PMID: 11470438
RT Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold.
RA McCarthy AA, Baker HM, Shewry SC, Patchett ML, Baker EN
RL Structure. 2001 Jul 3;9(7):637-46.
DR BRENDA; 5.1.99.1; Methylmalonyl-CoA epimerase
DR PFAM; PF00903; glyoxalase family protein |
| Genome Property | GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM) |
