GSHR_ASHGO
ID GSHR_ASHGO Reviewed; 480 AA.
AC Q74ZK4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glutathione reductase;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
GN Name=GLR1; OrderedLocusNames=AGR196W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54686.1; -; Genomic_DNA.
DR RefSeq; NP_986862.1; NM_211924.1.
DR AlphaFoldDB; Q74ZK4; -.
DR SMR; Q74ZK4; -.
DR STRING; 33169.AAS54686; -.
DR EnsemblFungi; AAS54686; AAS54686; AGOS_AGR196W.
DR GeneID; 4623164; -.
DR KEGG; ago:AGOS_AGR196W; -.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_2_1; -.
DR InParanoid; Q74ZK4; -.
DR OMA; GGATQRM; -.
DR Proteomes; UP000000591; Chromosome VII.
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 (NADPH) 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 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..480
FT /note="Glutathione reductase"
FT /id="PRO_0000067965"
FT ACT_SITE 469
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 51..59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 59..64
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 52649 MW; 8AF0C57EEA727BC9 CRC64;
MLRCREVYNI CKGAMSNEVK HYDYLVIGGG SGGVASSRRA ASYGAKTVLI EGKALGGTCV
NVGCVPKKVM WYASDLAHRL LHARDYGLLQ EVDISKEKLH FNWKEFAGKR NAYVERLNGI
YERNLAKEGV EYVHGWARFN SEGQVEVTRP DQTTEKYTAD HILIATGGEP VLPEGIPGAE
YGVDSDGFFR LEEQPKKVVI SGSGYIATEF AGVFNGLGTE THIVIRKDHV LTKFDPSIQE
IVTEHYEKEG VNIHKKESIQ RVEKDPNTGK LTVHLSGKII EDVDQLVWAI GRKSLLGIAP
ENVGVKLGET GHVVVDEYQN TSTKGIYALG DVVGNMELTP VAIAAGRKLA NRLFGPEQMR
AQKQDYDNVP SVVFSHPEAG SIGLTEPQAI ERYGKENIKI YQTKFTAMYY AMLEDKSPTK
YKLICAGPEE KVVGLHIVGD GSAEILQGFG VAIKMGATKA DFDSCVAIHP TSAEEIVTLK
