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dihydropteroate synthase
This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) Swiss:Q46389 that catalyses a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin [2]. [1]. 9187658. Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase. Achari A, Somers DO, Champness JN, Bryant PK, Rosemond J, Stammers DK. Nat Struct Biol 1997;4:490-497. This paper shows similarity by sequence of DHPS and MetH enzymes. [2]. 10997901. Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase. Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW;. Structure Fold Des 2000;8:817-830. (from Pfam)
This HMM represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (PF00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of PF00809 and COG0294 are represented by HMM TIGR00284.
dihydropteroate synthase catalyzes the formation of 7,8-dihydropteroate from para-aminobenzoic acid and 6-hydroxymethyl-7,8-dihydropterin-pyrophosphate, a key step in the folate biosynthetic pathway
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