ThiC_Rad_SAM |
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PFAM accession number: | PF01964 |
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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