Reviewed, UniProtKB/Swiss-Prot Q6FRV2 (GSHR_CANGA)

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:	CAGL0H05665g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 – 476	476	Glutathione reductase		PRO_0000067966
Regions
	Nucleotide binding	46 – 54	9	FAD By similarity
Sites
	Active site	465	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	54 ↔ 59		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FRV2-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: BA4793D0F077D14D	FASTA	476	52,499
	10 20 30 40 50 60 MIVKRLFRTM APVAKHFDYL VIGGGSGGVA SSRRAASYGA KTLLIEGKAL GGTCVNVGCV 70 80 90 100 110 120 PKKVMWYASD LATRLTHAHE YGLAQNVPLS KESITFNWPE FKKKRDAYIH RLNGIYENNL 130 140 150 160 170 180 KKEGVEVVFG WAKFNKDGNV EVTKHDNTTE VYSADRILVA TGGKPVYPEK VPGFELGTDS 190 200 210 220 230 240 DGFFRLEEQP KKVVVVGAGY IGIELAGVFH GLGSDSHLVI RGKTVLRKFD EIIQNTVTDY 250 260 270 280 290 300 YVEEGINVHK ETNVDKVEKD EKTGKLSVHL TNGQVLEDVD ELIWTMGRRS LLGIGLENVG 310 320 330 340 350 360 VKLNDKEQII TDEYQNTNVP NIYSLGDVSG RVELTPVAIA AGRKLSNRLF GPEQYRNDKL 370 380 390 400 410 420 DYTNVPSVVF SHPEAGSIGL TEDEAIKQYG KDNIKVYTSK FTAMYYAMLE HKSPTRYKII 430 440 450 460 470 CEGPNEKVVG LHIVGDSSAE ILQGFGVAIK MGATKADFDN CVAIHPTSAE ELVTMR

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 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380954 Genomic DNA. Translation: CAG59975.1.
RefSeq	XP_447042.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2888553.
KEGG	cgr:CAGL0H05665g.
Phylogenomic databases
HOGENOM	Q6FRV2.
OMA	Q6FRV2. HRQPCKM.
Enzyme and pathway databases
BRENDA	1.8.1.7. 189220.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glut_reduct_1. IPR000815. Hg_reductase. 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. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01421. gluta_reduc_1. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHR_CANGA

Accession

Primary (citable) accession number: Q6FRV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)