Reviewed, UniProtKB/Swiss-Prot Q6BPI1 (GSHR_DEBHA)

Names and origin

Protein names

Recommended name:
    Glutathione reductase
      Short name=GRase
      Short name=GR
    EC=1.8.1.7

Gene names

Name:	GLR1
Ordered Locus Names:	DEHA2E13442g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Maintains high levels of reduced glutathione in the cytosol By similarity.
Catalytic activity	2 glutathione + NADP+ = glutathione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond By similarity.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 490	490	Glutathione reductase		PRO_0000067967
Regions
	Nucleotide binding	39 – 49	11	FAD By similarity
Sites
	Active site	479	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	49 ↔ 54		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BPI1-1 [UniParc]. Last modified December 16, 2008. Version 3. Checksum: 1076F6EDB4389EAE	FASTA	490	53,520
	10 20 30 40 50 60 MAPLQAIRKY DYLVIGGGSG GVASARRAAS YGAKVLLIES KFNKMGGTCV NVGCVPKKVM 70 80 90 100 110 120 WYAGDLAEKR HHLKSYGLST TDDKVKYGDF DWSTFKDKRD AYVKRLNGIY ERNLKNEGVD 130 140 150 160 170 180 YIYGFAHFAN SNGDVEVTLT GDQELSFLEE GKEFKKDEKL VFAGSKTLIA TGGYAINPPN 190 200 210 220 230 240 VEGHELGTTS DGFFELQKQP KSVAVVGAGY IGVELSGIFK ALGSETHLVI RGDTVLRSFD 250 260 270 280 290 300 ESIQNSITDY YTDKLGVNII KQSGSVSKVE KIDGDRKKIT LGNGQVLEVD ELIWTMGRKS 310 320 330 340 350 360 LINIGLDKVG VTLNDKQQVD VDQFQQTANP NIFSLGDVIG KVELTPVAIA AGRRLSNRLF 370 380 390 400 410 420 SGDKAFENDH LDYSNVPSVI FSHPEAGSIG LSCKEAKEKY GEDQIKIYKS KFNAMYYAMM 430 440 450 460 470 480 EDDSLKSPTS YKVVCAGEDE KVVGLHIVGD SSAEILQGFG VAIKMGATKK DFDSCVAIHP 490 TSAEELVTMK

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382137 Genomic DNA. Translation: CAG88130.2. Different initiation.
RefSeq	XP_459889.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2902393.
GenomeReviews	Gene locus DEHA2E13442g in contig CR382137_GR.
KEGG	dha:DEHA0E14014g.
Phylogenomic databases
eggNOG	fuNOG07682.
HOGENOM	HBG515043.
OrthoDB	EOG9M3BRT.
Enzyme and pathway databases
BRENDA	1.8.1.7. 74267.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glutathione_Rdtase_animal/bac. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
TIGRFAMs	TIGR01421. gluta_reduc_1. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHR_DEBHA

Accession

Primary (citable) accession number: Q6BPI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 44 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)