Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyCobT-like 8042890 3000212 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ADBI_PRTe1d0sA1 A: a/b three-layered sandwichesX: Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) (From Topology)H: Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) (From Topology)T: Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT)F: DBI_PRTECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF02277Phosphoribosyltransferase (DBI_PRT)PhosphoribosyltransferaseThis family of proteins represent the nicotinate-nucleotide- dimethylbenzimidazole phosphoribosyltransferase (NN:DBI PRT) enzymes involved in dimethylbenzimidazole synthesis. This function is essential to de novo cobalamin (vitamin B12) production in ...This family of proteins represent the nicotinate-nucleotide- dimethylbenzimidazole phosphoribosyltransferase (NN:DBI PRT) enzymes involved in dimethylbenzimidazole synthesis. This function is essential to de novo cobalamin (vitamin B12) production in bacteria. Nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole (DMB) phosphoribosyltransferase (CobT) from Salmonella enterica plays a central role in the synthesis of alpha-ribazole-5'-phosphate, an intermediate for the lower ligand of cobalamin [2].
Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase  M-CSA #79

Nicotinate mononucleotide:5,6- dimethylbenzimidazole (DMB) phosphoribosyltransferase (CobT) is crucial in the synthesis of alpha-ribose-5'-phosphate, a precursor to the lower ligand of colbamin. The biosynthesis of colbamin requires more than 25 committed enzymes, and the biosynthetic pathway has received much interest because of its complexity. Colbamin synthesis is also of interest in evolutionary biology because of its utilisation by early forms of bacteria and Archaea.

The enzyme has also been shown to act on benzimidazole, and the clostridial enzyme acts on adenine to form 7-alpha-D-ribosyladenine 5'-phosphate.

Defined by 2 residues: GLU:A-174GLU:A-317
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