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: 8

1.

GlnD PII-uridylyltransferase

This is a family of bifunctional uridylyl-removing enzymes/uridylyltransferases (UR/UTases, GlnD) that are responsible for the modification (EC:2.7.7.59) of the regulatory protein P-II, or GlnB (e.g. Swiss:P05826, Pfam:PF00543). In response to nitrogen limitation, these transferases (e.g. Swiss:P27249) catalyse the uridylylation of the PII protein, which in turn stimulates deadenylylation of glutamine synthetase (GlnA). Deadenylylated glutamine synthetase is the more active form of the enzyme [1]. Moreover, uridylylated PII can act together with NtrB and NtrC to increase transcription of genes in the sigma54 regulon, which include glnA and other nitrogen-level controlled genes [2]. It has also been suggested that the product of the glnD gene is involved in other physiological functions such as control of iron metabolism in certain species [2]. The region described in this family is found in many of its members to be C-terminal to a nucleotidyltransferase domain (Pfam:PF01909), and N-terminal to an HD domain (Pfam:PF01966) and two ACT domains (Pfam:PF01842) [3]. [1]. 8412694. The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. van Heeswijk WC, Rabenberg M, Westerhoff HV, Kahn D;. Mol Microbiol 1993;9:443-457. [2]. 10931314. Novel effects of a transposon insertion in the Vibrio fischeri glnD gene: defects in iron uptake and symbiotic persistence in addition to nitrogen utilization. Graf J, Ruby EG;. Mol Microbiol 2000;37:168-179. [3]. 12384297. Isolation and characterization of the glnD gene of Gluconacetobacter diazotrophicus, encoding a putative uridylyltransferase. TRUNCATED at 1650 bytes (from Pfam)

GO Terms:
Molecular Function:
nucleotidyltransferase activity (GO:0016779)
Date:
2024-10-16
Family Accession:
NF019935.5
Method:
HMM
2.

Glutamate-ammonia ligase adenylyltransferase

Conserved repeated domain found in GlnE proteins. These proteins adenylate and deadenylate glutamine synthases: ATP + {L-Glutamate:ammonia ligase (ADP-forming)} = Diphosphate + Adenylyl-{L-Glutamate:Ammonia ligase (ADP-forming)}. The family is related to the Pfam:PF01909 domain. (from Pfam)

GO Terms:
Molecular Function:
[glutamate-ammonia-ligase] adenylyltransferase activity (GO:0008882)
Date:
2024-08-14
Family Accession:
NF015655.5
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.

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase catalyzes the adenylylation and deadenylylation of glutamine synthetase (GS)

Date:
2023-08-14
Family Accession:
11485184
Method:
Sparcle
8.

bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase

Catalyzes the ATP-dependent addition of AMP to a subunit of glutamine synthetase; also Catalyzes the reverse reaction - deadenylation

Gene:
glnE
GO Terms:
Molecular Function:
[glutamate-ammonia-ligase] adenylyltransferase activity (GO:0008882)
Date:
2021-07-23
Family Accession:
NF008292.0
Method:
HMM
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