ID   GSHR_YARLI              Reviewed;         470 AA.
AC   Q6C5H4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Glutathione reductase;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=GLR1; OrderedLocusNames=YALI0E18029g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382131; CAG79681.1; -; Genomic_DNA.
DR   RefSeq; XP_504088.1; XM_504088.1.
DR   AlphaFoldDB; Q6C5H4; -.
DR   SMR; Q6C5H4; -.
DR   STRING; 284591.Q6C5H4; -.
DR   EnsemblFungi; CAG79681; CAG79681; YALI0_E18029g.
DR   GeneID; 2911696; -.
DR   KEGG; yli:YALI0E18029g; -.
DR   VEuPathDB; FungiDB:YALI0_E18029g; -.
DR   HOGENOM; CLU_016755_2_2_1; -.
DR   InParanoid; Q6C5H4; -.
DR   OMA; MSKHYDY; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   NCBIfam; TIGR01421; gluta_reduc_1; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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..470
FT                   /note="Glutathione reductase"
FT                   /id="PRO_0000067971"
FT   ACT_SITE        459
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..49
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   470 AA;  51302 MW;  B9E4760F181DD143 CRC64;
     MASIPHYDYL VIGGGSGGVA SARRAASYGA KTLLIEGKAL GGTCVNVGCV PKKVMWNASD
     LAGRIRQAKE YGFPDVDPKY ADNFDWSGFK AKRDAYVKRL NGIYERNLQK EGVEYVFGWA
     TLYKQEGQEF PLVHVKSDDG NTKLYSAKKI MIATGGKPRL PDVPGAEYGI DSDGFFALET
     QPKRVAVVGG GYIGVELAGV FHGLNSETTL FCRGQTVLRA FDIMIQDTIT DYYVKEGINV
     LKGSGVKKIV KKDNGELLVT YEQDGAEKDI TLDSLIWTIG REPLKDTLNL GEFGIKTNKR
     GYIEVDEYQR SSVDNIYSLG DVCGKVELTP MAIAAGRKLS NRLFGPTEFK NQKQDYTDVP
     SAVFSHPEVG SIGITEAAAK EQYGEENVKV YTSKFVAMYY AMLEEKAPTA YKLVCAGKDE
     KVVGLHIVGA DSAEILQGFG VAIRMGATKA DFDNVVAIHP TSAEELVTMR
//