Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
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. uridylyltr. TRUNCATED at 1650 bytes (from Pfam)
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)
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
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on