Conserved Protein Domain Family
Pterin_binding

?
cl00219: Pterin_binding Superfamily (this model, PSSM-Id:412232 is obsolete and has been replaced by 444759)
Click on image for an interactive view with Cn3D
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.
Links
?
Taxonomy: root
PubMed: 5 links
Protein: Related Protein
Related Structure
Statistics
?
Accession: cl00219
PSSM Id: 412232
Name: Pterin_binding
Created: 8-Feb-2008
Updated: 24-Nov-2020
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap