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Links from Protein

Items: 8

1.

gamma-glutamyl-gamma-aminobutyrate hydrolase family protein

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)

GO Terms:
Molecular Function:
hydrolase activity (GO:0016787)
Date:
2024-10-16
Family Accession:
NF019342.5
Method:
HMM
2.

glutamine amidotransferase-related protein

Date:
2024-11-04
Family Accession:
NF012345.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

aminodeoxychorismate/anthranilate synthase component II

aminodeoxychorismate/anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA), and anthranilate, an intermediate in the biosynthesis of L-tryptophan, respectively

Date:
2023-02-27
Family Accession:
10792604
Method:
Sparcle
8.

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase

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.

GO Terms:
Molecular Function:
carbon-nitrogen ligase activity, with glutamine as amido-N-donor (GO:0016884)
Date:
2021-04-27
Family Accession:
TIGR00566.1
Method:
HMM
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