HMM Summary Page: TIGR01140

Functionthreonine-phosphate decarboxylase
Trusted Cutoff290.55
Domain Trusted Cutoff290.55
Noise Cutoff276.85
Domain Noise Cutoff276.85
Isology Typeequivalog
EC Number4.1.1.81
HMM Length331
Mainrole CategoryBiosynthesis of cofactors, prosthetic groups, and carriers
Subrole CategoryHeme, porphyrin, and cobalamin
Gene Ontology TermGO:0005737: cytoplasm cellular_component
GO:0009236: cobalamin biosynthetic process biological_process
GO:0048472: threonine-phosphate decarboxylase activity molecular_function
AuthorHaft DH
Entry DateJan 31 2001 10:10AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis family contains pyridoxal phosphate-binding class II aminotransferases (see PFAM:PF00222) closely related to, yet distinct from, histidinol-phosphate aminotransferase (HisC). It is found in cobalamin biosynthesis operons in Salmonella typhimurium and Bacillus halodurans (each of which also has HisC) and has been shown to have L-threonine-O-3-phosphate decarboxylase activity in Salmonella. Although the gene symbol cobD was assigned in Salmonella, cobD in other contexts refers to a different cobalamin biosynthesis enzyme, modeled by PF03186 and called cbiB in Salmonella.
ReferencesRN [1] RM 98112812 RT CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. RA Brushaber KR, O'Toole GA, Escalante-Semerena JC RL J Biol Chem 1998 Jan 30;273(5):2684-91 RN [2] RM PMID: 12119022 RT Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes. RA Cheong CG, Escalante-Semerena JC, Rayment I RL Biochemistry. 2002 Jul 23;41(29):9079-89.
Genome PropertyGenProp0269: coenzyme B12 biosynthesis from cob(II)yrinate diamide (HMM)