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InterPro: IPR006322 Glutathione reductase, animal/bacterial

Protein matches Help

UniProtKB

Matches:

543 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

IPR006322 Glutathione_Rdtase_animal/bac

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01421	gluta_reduc_1	543
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000815 Mercuric reductase

Contains

IPR001327 Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
IPR004099 Pyridine nucleotide-disulphide oxidoreductase, dimerisation
IPR012999 Pyridine nucleotide-disulphide oxidoreductase, class I, active site
IPR013027 FAD-dependent pyridine nucleotide-disulphide oxidoreductase

GO Term annotation Help

Process

GO:0006749 glutathione metabolic process
GO:0055114 oxidation reduction

Function

GO:0004362 glutathione-disulfide reductase activity
GO:0050660 FAD binding
GO:0050661 NADP or NADPH binding

InterPro annotation

Entry Details in BioMart

Abstract

These sequences represent one of two closely related subfamilies of glutathione reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione reductases of animals, yeast, and a number of animal-resident bacteria.

Structural links Help

PDB - click here

SCOP: c.3.1.5 , d.87.1.1 , j.61.1.1

CATH: 3.30.390.30 , 3.50.50.60

Database links Help

Enzyme: EC:1.8.1.7

CluSTr: ALLvsALL:28906:113.9

PRIAM: PRI002867

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006322

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2TIL1 Glutathione reductase, mitochondrial

P00390 Glutathione reductase, mitochondrial

P06715 Glutathione reductase

P41921 Glutathione reductase

P47791 Glutathione reductase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation
IPR016156	FAD/NAD-linked reductase, dimerisation
IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site
IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
IPR000815	Mercuric reductase
IPR006322	Glutathione reductase, animal/bacterial
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Savvides SN, Scheiwein M, Bohme CC, Arteel GE, Karplus PA, Becker K, Schirmer RH. Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite. J. Biol. Chem. 277 2002 2779-84 [PubMed: 11705998] http://dx.doi.org/10.1074/jbc.M108190200
	Urig S, Fritz-Wolf K, Reau R, Herold-Mende C, Toth K, Davioud-Charvet E, Becker K. Undressing of phosphine gold(I) complexes as irreversible inhibitors of human disulfide reductases. Angew. Chem. Int. Ed. Engl. 45 2006 1881-6 [PubMed: 16493712] http://dx.doi.org/10.1002/anie.200502756
	Bauer H, Fritz-Wolf K, Winzer A, Kuhner S, Little S, Yardley V, Vezin H, Palfey B, Schirmer RH, Davioud-Charvet E. A fluoro analogue of the menadione derivative 6-[2'-(3'-methyl)-1',4'-naphthoquinolyl]hexanoic acid is a suicide substrate of glutathione reductase. Crystal structure of the alkylated human enzyme. J. Am. Chem. Soc. 128 2006 10784-94 [PubMed: 16910673] http://dx.doi.org/10.1021/ja061155v
	Gallwitz H, Bonse S, Martinez-Cruz A, Schlichting I, Schumacher K, Krauth-Siegel RL. Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies. J. Med. Chem. 42 1999 364-72 [PubMed: 9986706] http://dx.doi.org/10.1021/jm980471k
	Yu J, Zhou CZ. Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae. Proteins 68 2007 972-9 [PubMed: 17554778] http://dx.doi.org/10.1002/prot.21354

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