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

Date:

2024-11-04

Catalyzes the formation of 4-amino-4-deoxychorismate from chorismate and glutamine in para-aminobenzoate synthesis

Date:

2020-10-26

aminodeoxychorismate synthase component II is part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate

Date:

2018-05-10

Aminodeoxychorismate synthase subunit PabA; with PabB catalyzes the formation of 4-amino-4-deoxychorismate from chorismate and glutamine in para-aminobenzoate synthesis

Gene:

pabA

Date:

2020-10-26

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