U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 1 to 20 of 22

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:
2024-08-14
Family Accession:
NF019342.5
Method:
HMM
2.

CobB/CobQ-like glutamine amidotransferase domain

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Date:
2024-08-14
Family Accession:
NF019305.5
Method:
HMM
3.

SNO glutamine amidotransferase family

This family and its amidotransferase domain was first described in [1]. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of Pfam:PF01174 and Pfam:PF01680 [2]. [1]. 9159529. Sequence analysis of an exceptionally conserved operon suggests. enzymes for a new link between histidine and purine. biosynthesis.. Galperin MY, Koonin EV;. Mol Microbiol 1997;24:443-445.. [2]. 9791124. The highly conserved, coregulated SNO and SNZ gene families in. Saccharomyces cerevisiae respond to nutrient limitation.. Padilla PA, Fuge EK, Crawford ME, Errett A, Werner-Washburne M;. J Bacteriol 1998;180:5718-5726. (from Pfam)

GO Terms:
Molecular Function:
glutaminase activity (GO:0004359)
Biological Process:
vitamin B6 biosynthetic process (GO:0042819)
Biological Process:
pyridoxal phosphate biosynthetic process (GO:0042823)
Date:
2024-08-14
Family Accession:
NF013350.5
Method:
HMM
4.

Glutamine amidotransferase class-I

Date:
2024-08-14
Family Accession:
NF012345.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.
new record, indexing in progress
Family Accession:
17.

imidazole glycerol phosphate synthase subunit HisH

This HMM represents HisH, the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. IGPS catalyzes the conversion of phosphoribulosyl-formimino-5-aminoimidazole-4-carboxamide ribonucleotide phosphate and glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamide ribonucleotide, and glutamate during histidine biosynthesis.

Gene:
hisH
GO Terms:
Biological Process:
L-histidine biosynthetic process (GO:0000105)
Molecular Function:
imidazoleglycerol-phosphate synthase activity (GO:0000107)
Date:
2024-06-14
Family Accession:
TIGR01855.1
Method:
HMM
18.
new record, indexing in progress
Family Accession:
19.
new record, indexing in progress
Family Accession:
20.

imidazole glycerol phosphate synthase subunit HisH

imidazole glycerol phosphate synthase subunit HisH catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR

Date:
2023-02-27
Family Accession:
10793738
Method:
Sparcle
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center