GSHR_DICDI
ID GSHR_DICDI Reviewed; 465 AA.
AC Q8T137; Q558X7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glutathione reductase {ECO:0000303|PubMed:16678813};
DE Short=GR;
DE Short=GRase;
DE Short=GSR {ECO:0000303|PubMed:16678813};
DE EC=1.8.1.7 {ECO:0000269|PubMed:16678813};
GN Name=gsr; ORFNames=DDB_G0272754;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16678813; DOI=10.1016/j.ydbio.2006.03.038;
RA Choi C.-H., Kim B.-J., Jeong S.-Y., Lee C.-H., Kim J.-S., Park S.-J.,
RA Yim H.-S., Kang S.-O.;
RT "Reduced glutathione levels affect the culmination and cell fate decision
RT in Dictyostelium discoideum.";
RL Dev. Biol. 295:523-533(2006).
CC -!- FUNCTION: Maintains high levels of reduced glutathione (GSH) in the
CC cytosol by reducing glutathione disulfide (oxidized glutathione or
CC GSSG) (PubMed:16678813). The amount of GSH may affect the determination
CC of cell fate (PubMed:16678813). {ECO:0000269|PubMed:16678813,
CC ECO:0000303|PubMed:16678813}.
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 Evidence={ECO:0000269|PubMed:16678813};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11742;
CC Evidence={ECO:0000269|PubMed:16678813};
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 -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AAFI02000008; EAL71014.1; -; Genomic_DNA.
DR RefSeq; XP_644939.1; XM_639847.1.
DR AlphaFoldDB; Q8T137; -.
DR SMR; Q8T137; -.
DR STRING; 44689.DDB0231410; -.
DR PaxDb; Q8T137; -.
DR EnsemblProtists; EAL71014; EAL71014; DDB_G0272754.
DR GeneID; 8618618; -.
DR KEGG; ddi:DDB_G0272754; -.
DR dictyBase; DDB_G0272754; gsr.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_2_1; -.
DR InParanoid; Q8T137; -.
DR OMA; MSKHYDY; -.
DR PhylomeDB; Q8T137; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DDI-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-DDI-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:Q8T137; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0043295; F:glutathione binding; IDA:dictyBase.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IMP:dictyBase.
DR GO; GO:0050661; F:NADP binding; IDA:dictyBase.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:dictyBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:dictyBase.
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..465
FT /note="Glutathione reductase"
FT /id="PRO_0000327610"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 42..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 50..55
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 50483 MW; E89CAF09AEA6A771 CRC64;
MSSTNHFTYL VLGAGSGGIA SARRAAKHLN AKGNGDRIGI VEVTRPGGTC VNVGCVPKKV
MWNTSFIKEM INAAPSYGFD FGGQQVKFNW PTIKKARDEY IKRLNGIYDS NLAKDNIVRI
NGYGRFSGPK EIQVNGANGE KYTADHILIA AGGRPTVPDV PGKELGITSD GFFELEDLPK
STLVVGAGYI AVELAGVLHS LGSETTMVIR QKQFLRTFDE MLHTTLLKQM TDDGVKFVTE
ASIKSLERDV DGKRIIATTN AGVKLPPVEC VIWAIGRVPN TDDLGIDKAG IQLTEQSGFI
KVDEFQNTNV PGVHAVGDIC GNFLLTPVAI AAGRRLSERL FNGKSDLKFE YENVATVVFS
HPPIGTVGLT EQEAITKYGT ENIKCYNTSF INMFYSVQVH KVRTSMKLVC LGKEEKVIGL
HIIGDGCDEI IQGFAVAVKM GCTKWDLDNT CAIHPTSAEE LVTMV
