EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR010043 Protein-PII uridylyltransferase

Protein matches Help

UniProtKB

Matches:

782 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR010043 GlnD_Uridyltrans

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00277	GlnD_Uridyltrans	537
PIRSF	PIRSF006288	PII_uridyltransf	688
PANTHER	PTHR13734:SF1	GlnD_Uridyltrans	777
TIGRFAMs	TIGR01693	UTase_glnD	673
Signatures in BioMart

InterPro Relationships Help

Contains

IPR002912 Amino acid-binding ACT
IPR002934 Nucleotidyltransferase
IPR003607 Metal-dependent phosphohydrolase, HD domain
IPR006674 Metal-dependent phosphohydrolase, HD subdomain
IPR013546 PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase

GO Term annotation Help

Process

GO:0006807 nitrogen compound metabolic process

Function

GO:0008773 [protein-PII] uridylyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for signal-transduction protein PII, and acts as the sensory component of the nitrogen regulation (ntr) system [1]. The ntr system modulates nitrogen metabolism in response to the prevailing nitrogen source and the requirements of the cell. During nitrogen fixation, ammonia and 2-oxoglutarate can be used to produce glutamate. The activity of the PII protein is stimulated by glutamine and inhibited by 2-oxoglutarate. Under glutamate-limiting conditions, PII is uridylylated by GlnD leading to the activation of glutamate synthetase and to the stimulation of NtrC-dependent promoters. Under high concentrations of fixed nitrogen, PII is de-uridylylated leading to the inactivation of the glutamate synthetase pathway and switching off NtrC-dependent promoters [2].

Not all homologues of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see IPR002332), but the modification site is preserved in the PII homologue of all species with a member of this family.

Database links Help

Enzyme: EC:2.7.7.59

CluSTr: ALLvsALL:34877:40.6

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR010043

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A1A7L1 [Protein-PII] uridylyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002912	Amino acid-binding ACT
IPR006674	Metal-dependent phosphohydrolase, HD subdomain
IPR002934	Nucleotidyltransferase
IPR010043	Protein-PII uridylyltransferase
IPR013546	PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase
IPR003607	Metal-dependent phosphohydrolase, HD domain
	SWISS-MODEL

Publications Open in usermanual
1.	Van Dommelen A, Keijers V, Somers E, Vanderleyden J. Cloning and characterisation of the Azospirillum brasilense glnD gene and analysis of a glnD mutant. Mol. Genet. Genomics 266 813-20 2002 [PubMed: 11810255] http://dx.doi.org/10.1007/s00438-001-0598-5
2.	Schluter A, Nohlen M, Kramer M, Defez R, Priefer UB. The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation. Microbiology (Reading, Engl.) 146 ( Pt 11) 2987-96 2000 [PubMed: 11065377]

InterPro 23.1