HMM Summary Page: TIGR00641

AccessionTIGR00641
Nameacid_CoA_mut_N
Functionmethylmalonyl-CoA mutase N-terminal domain
Trusted Cutoff303.80
Domain Trusted Cutoff303.80
Noise Cutoff136.05
Domain Noise Cutoff136.05
Isology Typesubfamily_domain
EC Number5.4.99.-
HMM Length528
AuthorHaft DH
Entry DateOct 25 1999 11:40AM
Last ModifiedFeb 14 2011 3:27PM
CommentMethylmalonyl-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 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 5.4.99.2.
ReferencesA2 hmmalign DR ECOCYC; EG11444; sbm; RN [1] RM 97386818 RT Structure-based perspectives on B12-dependent enzymes. RA Ludwig ML, Matthews RG RL Annu Rev Biochem 1997;66:269-313 RN [2] RM 98165841 RN [3] RM 97022083
Genome PropertyGenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0284: cobalamin-utilizing enzymes (HMM)
GenProp0284: cobalamin-utilizing enzymes (HMM)
GenProp0284: cobalamin-utilizing enzymes (HMM)