Accession | TIGR00640 |
Name | acid_CoA_mut_C |
Function | methylmalonyl-CoA mutase C-terminal domain |
Trusted Cutoff | 57.45 |
Domain Trusted Cutoff | 57.45 |
Noise Cutoff | 27.00 |
Domain Noise Cutoff | 27.00 |
Isology Type | subfamily_domain |
HMM Length | 132 |
Author | Haft DH |
Entry Date | Oct 25 1999 11:40AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a reversible isomerization between L-methylmalonyl-CoA and succinyl-CoA. The enzyme uses an adenosylcobalamin cofactor. It may be a homodimer, as in mitochondrion, or a heterodimer with partially homologous beta chain that does not bind the adenosylcobalamin cofactor, as in Propionibacterium freudenreichii. The most similar archaeal sequences are separate chains, such as AF2215 and AF2219 of Archaeoglobus fulgidus, that correspond roughly to the first 500 and last 130 residues, respectively of known methylmalonyl-CoA mutases. This HMM describes the C-terminal domain subfamily. In a neighbor-joining tree (methylaspartate mutase S chain as the outgroup), AF2219 branches with a coenzyme B12-dependent enzyme known not to be 5.4.99.2. |
References | A2 hmmalign
RM 97386818
RT Structure-based perspectives on B12-dependent enzymes.
RA Ludwig ML, Matthews RG
RL Annu Rev Biochem 1997;66:269-313 |
Genome Property | GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM) |
| GenProp0284: cobalamin-utilizing enzymes (HMM) |