GSHR_CANGA
ID GSHR_CANGA Reviewed; 476 AA.
AC Q6FRV2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glutathione reductase;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
GN Name=GLR1; OrderedLocusNames=CAGL0H05665g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; CR380954; CAG59975.1; -; Genomic_DNA.
DR RefSeq; XP_447042.1; XM_447042.1.
DR AlphaFoldDB; Q6FRV2; -.
DR SMR; Q6FRV2; -.
DR STRING; 5478.XP_447042.1; -.
DR PRIDE; Q6FRV2; -.
DR EnsemblFungi; CAG59975; CAG59975; CAGL0H05665g.
DR GeneID; 2888553; -.
DR KEGG; cgr:CAGL0H05665g; -.
DR CGD; CAL0131774; GLR1.
DR VEuPathDB; FungiDB:CAGL0H05665g; -.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_2_1; -.
DR InParanoid; Q6FRV2; -.
DR OMA; MSKHYDY; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblFungi.
DR GO; GO:0036245; P:cellular response to menadione; IEA:EnsemblFungi.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:EnsemblFungi.
DR GO; GO:0010731; P:protein glutathionylation; IEA:EnsemblFungi.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006322; Glutathione_Rdtase_euk/bac.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR42737; PTHR42737; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01421; gluta_reduc_1; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..476
FT /note="Glutathione reductase"
FT /id="PRO_0000067966"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 46..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 54..59
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 476 AA; 52499 MW; BA4793D0F077D14D CRC64;
MIVKRLFRTM APVAKHFDYL VIGGGSGGVA SSRRAASYGA KTLLIEGKAL GGTCVNVGCV
PKKVMWYASD LATRLTHAHE YGLAQNVPLS KESITFNWPE FKKKRDAYIH RLNGIYENNL
KKEGVEVVFG WAKFNKDGNV EVTKHDNTTE VYSADRILVA TGGKPVYPEK VPGFELGTDS
DGFFRLEEQP KKVVVVGAGY IGIELAGVFH GLGSDSHLVI RGKTVLRKFD EIIQNTVTDY
YVEEGINVHK ETNVDKVEKD EKTGKLSVHL TNGQVLEDVD ELIWTMGRRS LLGIGLENVG
VKLNDKEQII TDEYQNTNVP NIYSLGDVSG RVELTPVAIA AGRKLSNRLF GPEQYRNDKL
DYTNVPSVVF SHPEAGSIGL TEDEAIKQYG KDNIKVYTSK FTAMYYAMLE HKSPTRYKII
CEGPNEKVVG LHIVGDSSAE ILQGFGVAIK MGATKADFDN CVAIHPTSAE ELVTMR
