GSHR_KLULA
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 03-AUG-2022, entry version 117.
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 / 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}.
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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; 28985.XP_455036.1; -.
DR EnsemblFungi; CAH00123; CAH00123; KLLA0_E24069g.
DR GeneID; 2894346; -.
DR KEGG; kla:KLLA0_E24069g; -.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_2_1; -.
DR InParanoid; Q6HA23; -.
DR OMA; GGATQRM; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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 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
