ID   GSHR_KLULA              Reviewed;         484 AA.
AC   Q6HA23; Q6CM03;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Glutathione reductase;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=GLR1; OrderedLocusNames=KLLA0E24112g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=15157744; DOI=10.1016/j.bbaexp.2004.03.004;
RA   Tarrio N., Diaz Prado S., Cerdan M.E., Gonzales Siso M.I.;
RT   "Isolation and characterization of two nuclear genes encoding glutathione
RT   and thioredoxin reductases from the yeast Kluyveromyces lactis.";
RL   Biochim. Biophys. Acta 1678:170-175(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ504414; CAD43213.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAH00123.1; -; Genomic_DNA.
DR   RefSeq; XP_455036.1; XM_455036.1.
DR   AlphaFoldDB; Q6HA23; -.
DR   SMR; Q6HA23; -.
DR   STRING; 284590.Q6HA23; -.
DR   PaxDb; 284590-Q6HA23; -.
DR   GeneID; 2894346; -.
DR   KEGG; kla:KLLA0_E24069g; -.
DR   eggNOG; KOG0405; Eukaryota.
DR   HOGENOM; CLU_016755_2_2_1; -.
DR   InParanoid; Q6HA23; -.
DR   OMA; MSKHYDY; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..484
FT                   /note="Glutathione reductase"
FT                   /id="PRO_0000067968"
FT   ACT_SITE        473
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         52..60
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..65
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   484 AA;  53378 MW;  CEE24F6377CC0ECB CRC64;
     MSIRNTINRI IIRRNMSDSI RHYDYLVIGG GSGGVASSRR AASYGAKTLL IEAKAMGGTC
     VNKGCVPKKV MWYASDLATR IGHAHSYNLF EDLPLTKENL TFNWPEFKKK RDAYIHRLNG
     IYERNLTKEG VDYVYGWASF TVDGKVQVKK ADNCTETYTA DHILVATGGK PIYPAKIPGY
     DYGVSSDEFF ELEDQPKKVV VVGAGYIGVE IAGVFNGLGS DSHLVIRGET VLRKFDDCIQ
     ETVTDTYIKE GVNIHKSSNV TKVEKDESTG KLNIQLDTGK NIDNVDSLIW TIGRRSLLGL
     GLENIGVKLD AKEQIVVDEY QNSSVKNVYS LGDVVGKVEL TPVAIAAGRK LSNRLFGPEK
     FKNQKQDYEN VPSVVFSHPE AGSIGLSERE AIEKFGKDNV KVYNSKFNAM YYAMMEEKDK
     TPTRYKLVCT GEEEKVVGLH IIGDSSAEIL QGFGVAIKMG ATKADFDSCV AIHPTSAEEL
     VTLT
//