Protein Family Models

These peptidases have gamma-glutamyl hydrolase activity; that is they catalyse the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to Pfam:PF00117, but contain extensions in four loops and at the C terminus [1]. [1]. 11953431. Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate. Li H, Ryan TJ, Chave KJ, Van Roey P;. J Biol Chem 2002;277:24522-24529. (from Pfam)

Date:

2024-10-16

This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate. [1]. 2199449. Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. Walter MR, Cook WJ, Cole LB, Short SA, Koszalka GW, Krenitsky TA, Ealick SE;. J Biol Chem 1990;265:14016-14022. (from Pfam)

Date:

2024-10-16

Date:

2024-11-04

This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate. [1]. 2199449. Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. Walter MR, Cook WJ, Cole LB, Short SA, Koszalka GW, Krenitsky TA, Ealick SE;. J Biol Chem 1990;265:14016-14022. (from Pfam)

Date:

2024-10-16

In many widely different species, including E. coli, Thermotoga maritima, and Archaeoglobus fulgidus, this enzymatic domain (anthranilate phosphoribosyltransferase) is found C-terminal to glutamine amidotransferase; the fusion protein is designated anthranilate synthase component II (EC 4.1.3.27)

Gene:

trpD

Date:

2021-04-27

bifunctional glutamine amidotransferase/anthranilate phosphoribosyltransferase plays a role in the biosynthesis of tryptophan

Date:

2017-02-03

This HMM describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the PFAM HMM GATase.

Date:

2021-04-27

Bifunctional anthranilate synthase II/anthranilate phosphoribosyltransferase; TrpD; forms a heterotetramer with Trp E and the complex catalyzes the formation of anthranilate from chorismate and glutamine; also catalyzes the formation of N-(5-phospho-D-ribosyl)-anthranilate from athranilate and 5-phospho-alpha-D-ribose 1-diphosphate; functions in tryptophan biosynthesis

Gene:

trpD

Date:

2021-11-04