HMM Summary Page: TIGR00636

FunctionATP:cob(I)alamin adenosyltransferase
Trusted Cutoff108.45
Domain Trusted Cutoff108.45
Noise Cutoff53.90
Domain Noise Cutoff53.90
Isology Typeequivalog_domain
EC Number2.5.1.17
HMM Length171
Mainrole CategoryBiosynthesis of cofactors, prosthetic groups, and carriers
Subrole CategoryHeme, porphyrin, and cobalamin
Gene Ontology TermGO:0008817: cob(I)yrinic acid a,c-diamide adenosyltransferase activity molecular_function
GO:0009236: cobalamin biosynthetic process biological_process
AuthorHaft DH
Entry DateOct 25 1999 11:40AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis HMM represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens.
ReferencesRN [1] RM 11160088 RT Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene. RA Johnson CL, Pechonick E, Park SD, Havemann GD, Leal NA, Bobik TA. RL J Bacteriol 2001 Mar;183(5):1577-84 RN [2] RM PMID: 15687219 RT Identification of genes involved in the glyoxylate regeneration cycle in Methylobacterium extorquens AM1, including two new genes, meaC and meaD. RA Korotkova N, Lidstrom ME, Chistoserdova L RL J Bacteriol. 2005 Feb;187(4):1523-6.
Genome PropertyGenProp0269: coenzyme B12 biosynthesis from cob(II)yrinate diamide (HMM)