ThiC_Rad_SAM

ThiC_Rad_SAM
PFAM accession number:PF01964
Interpro abstract (IPR002817):

This entry includes phosphomethylpyrimidine synthases, including thiC from prokaryotes and AtTHIC from Arabidopsis. thiC is found within the thiamin biosynthesis operon and is involved in thiamin biosynthesis [ (PUBMED:10382260) ]. ThiC catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction [ (PUBMED:18953358) (PUBMED:15326535) ].

AtTHIC is involved in pyrimidine synthesis in the thiamine biosynthesis pathway of Arabidopsis. Heterologous expression of AtTHIC could functionally complement the thiC knock-out mutant of E. coli [ (PUBMED:18332905) ].

This entry also includes 5-hydroxybenzimidazole synthase BzaA and BzaB. They are part of the bzaABCDE genes that are necessary and sufficient for the anaerobic biosynthesis of DMB (5,6-dimethylbenzimidazole), the "lower ligand" of vitamin B12 [ (PUBMED:26246619) ].

GO process:thiamine biosynthetic process (GO:0009228)
GO function:iron-sulfur cluster binding (GO:0051536)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ThiC_Rad_SAM