Q6FRV2 (GSHR_CANGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	GLR1
Ordered Locus Names:	CAGL0H05665g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces › Candida glabrata

Protein attributes

Sequence length	476 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
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide 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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380954 Genomic DNA. Translation: CAG59975.1.
RefSeq	XP_447042.1. XM_447042.1.
3D structure databases
ProteinModelPortal	Q6FRV2.
SMR	Q6FRV2. Positions 15-476.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2888553.
KEGG	cgr:CAGL0H05665g.
Phylogenomic databases
HOGENOM	HOG000276712.
KO	K00383.
OMA	VTSHRQP.
OrthoDB	EOG415KNX.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glutathione_Rdtase_euk/bac. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
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:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program