Protein Family Models

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)

Date:

2024-08-14

HD domains are metal dependent phosphohydrolases. [1]. 9868367. The HD domain defines a new superfamily of metal-dependent. phosphohydrolases.. Aravind L, Koonin EV;. Trends Biochem Sci 1998;23:469-472. (from Pfam)

Date:

2024-08-14

This HMM describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family.

Gene:

glnD

Date:

2021-04-27

bifunctional uridylyltransferase/uridylyl-removing enzyme modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell

Date:

2018-03-01