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InterPro: IPR020593 Gamma-glutamyl phosphate reductase GPR, conserved site

Protein matches Help

UniProtKB

Matches:

1468 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

IPR020593 G-glutamylP_reductase_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS01223	PROA	1468
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000965 Gamma-glutamyl phosphate reductase GPR
IPR005766 Delta l-pyrroline-5-carboxylate synthetase
IPR012134 Glutamate-5-semialdehyde dehydrogenase
IPR015590 Aldehyde dehydrogenase
IPR016161 Aldehyde/histidinol dehydrogenase
IPR016163 Aldehyde dehydrogenase, C-terminal

GO Term annotation Help

Process

GO:0006561 proline biosynthetic process

Function

GO:0004350 glutamate-5-semialdehyde dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

Gamma-glutamyl phosphate reductase (EC:1.2.1.41) (GPR) is the enzyme that catalyzes the second step in the biosynthesis of proline from glutamate, the NADP-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. In bacteria (gene proA) and yeast [1] (gene PRO2), GPR is a monofunctional protein, while in plants and mammals, it is a bifunctional enzyme (P5CS) [2] that consists of two domains, an N-terminal glutamate 5-kinase domain (EC:2.7.2.11) and a C-terminal GPR domain.

This signature pattern covers a conserved region that contains two histidine residues. This region is located in the last third of GPR.

Structural links Help

PDB - click here

SCOP: c.82.1.1

CATH: 3.40.309.10

Database links Help

Enzyme: EC:1.2.1.41

CluSTr: ALLvsALL:30911:107.2

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR020593

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P54885 Gamma-glutamyl phosphate reductase

P54886 Delta-1-pyrroline-5-carboxylate synthetase

P54887 Delta-1-pyrroline-5-carboxylate synthetase A

P54889 Probable delta-1-pyrroline-5-carboxylate synthetase

Q9Z110 Delta-1-pyrroline-5-carboxylate synthetase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005715	Glutamate 5-kinase, ProB-related
IPR000965	Gamma-glutamyl phosphate reductase GPR
IPR016163	Aldehyde dehydrogenase, C-terminal
IPR016162	Aldehyde dehydrogenase, N-terminal
IPR016161	Aldehyde/histidinol dehydrogenase
IPR019797	Glutamate 5-kinase, conserved site
IPR005766	Delta l-pyrroline-5-carboxylate synthetase
IPR020593	Gamma-glutamyl phosphate reductase GPR, conserved site
IPR012134	Glutamate-5-semialdehyde dehydrogenase
IPR001057	Glutamate 5-kinase
IPR001048	Aspartate/glutamate/uridylate kinase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Pearson BM, Hernando Y, Payne J, Wolf SS, Kalogeropoulos A, Schweizer M. Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII. Yeast 12 1021-31 1996 [PubMed: 8896266] http://dx.doi.org/10.1002/(SICI)1097-0061(199609)12:10B<1021::AID-YEA981>3.3.CO;2-Z
2.	Hu CA, Delauney AJ, Verma DP. A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants. Proc. Natl. Acad. Sci. U.S.A. 89 9354-8 1992 [PubMed: 1384052] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1384052

Additional Reading Help

Page R, Nelson MS, von Delft F, Elsliger MA, Canaves JM, Brinen LS, Dai X, Deacon AM, Floyd R, Godzik A, Grittini C, Grzechnik SK, Jaroszewski L, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Robb A, Rodrigues K, Schwarzenbacher R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Hodgson KO, Wooley J, Wilson IA.
Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution.
Proteins 54 2004 157-61 [PubMed: 14705032]
http://dx.doi.org/10.1002/prot.10562

InterPro 23.1