HMM Summary Page: TIGR00640

Functionmethylmalonyl-CoA mutase C-terminal domain
Trusted Cutoff57.45
Domain Trusted Cutoff57.45
Noise Cutoff27.00
Domain Noise Cutoff27.00
Isology Typesubfamily_domain
HMM Length132
AuthorHaft DH
Entry DateOct 25 1999 11:40AM
Last ModifiedFeb 14 2011 3:27PM
CommentMethylmalonyl-CoA mutase (EC 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
ReferencesA2 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 PropertyGenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0284: cobalamin-utilizing enzymes (HMM)