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 family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95 Swiss:P08328, which is inhibited by serine [1]. Aspartokinase EC:2.7.2.4 Swiss:P53553, which is regulated by lysine. Acetolactate synthase small regulatory subunit Swiss:P00894, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1 Swiss:P00439, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51 Swiss:P21203. formyltetrahydrofolate deformylase EC:3.5.1.10, Swiss:P37051, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Swiss:P11585 [1]. 7719856. The allosteric ligand site in the Vmax-type cooperative enzyme. phosphoglycerate dehydrogenase.. Schuller DJ, Grant GA, Banaszak LJ;. Nat Struct Biol 1995;2:69-76.. Definition of the domain. [2]. 10222208. Gleaning non-trivial structural, functional and evolutionary. information about proteins by iterative database searches.. Aravind L, Koonin EV;. J Mol Biol 1999;287:1023-1040. (from Pfam)

Date:

2024-08-14

Members of this family belong to a large family of nucleotidyltransferases [1]. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug. [1]. 7482698. DNA polymerase beta belongs to an ancient nucleotidyltransferase. superfamily.. Holm L, Sander C;. Trends Biochem Sci 1995;20:345-347. (from Pfam)

Date:

2024-08-14

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

Catalyzes the uridylylation or deuridylylation of the PII nitrogen regulatory protein

Gene:

glnD

Date:

2024-05-02

Gene:

glnD

Date:

2020-10-26