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ACT domain-containing protein
This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95 Swiss:P08328, which is inhibited by serine [1]. Aspartokinase EC:2.7.2.4 Swiss:P53553, which is regulated by lysine. Acetolactate synthase small regulatory subunit Swiss:P00894, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1 Swiss:P00439, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51 Swiss:P21203. formyltetrahydrofolate deformylase EC:3.5.1.10, Swiss:P37051, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Swiss:P11585 [1]. 7719856. The allosteric ligand site in the Vmax-type cooperative enzyme. phosphoglycerate dehydrogenase.. Schuller DJ, Grant GA, Banaszak LJ;. Nat Struct Biol 1995;2:69-76.. Definition of the domain. [2]. 10222208. Gleaning non-trivial structural, functional and evolutionary. information about proteins by iterative database searches.. Aravind L, Koonin EV;. J Mol Biol 1999;287:1023-1040. (from Pfam)
formyltransferase family protein
Many but not all members of this family are formyltransferases or deformylases, including hosphoribosylglycinamide formyltransferase 1 (EC 2.1.2.2), methionyl-tRNA formyltransferase (EC 2.1.2.9), and formyltetrahydrofolate deformylase (EC 3.5.1.1).
formyltetrahydrofolate deformylase
formyltetrahydrofolate deformylase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to tetrahydrofolate (FH4) and formate
Produces formate from formyl-tetrahydrofolate which is the major source of formate for PurT in de novo purine nucleotide biosynthesis; has a role in one-carbon metabolism; forms a homohexamer; activated by methionine and inhibited by glycine
This HMM describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region.
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