|Function||methylmalonyl-CoA mutase N-terminal domain|
|Domain Trusted Cutoff||303.80|
|Domain Noise Cutoff||136.05|
|Entry Date||Oct 25 1999 11:40AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||Methylmalonyl-CoA mutase (EC 126.96.36.199) 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 abd 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 N-terminal domain subfamily. In a neighbor-joining tree, AF2215 branches with a bacterial isobutyryl-CoA mutase, which is also the same length. Scoring between the noise and trusted cutoffs are the non-catalytic, partially homologous beta chains from certain heterodimeric examples of 188.8.131.52.
DR ECOCYC; EG11444; sbm;
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)|
© J. Craig Venter Institute | Privacy Statement | Data Disclaimer