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Database: UniProt
Entry: A0A0D2SD30_GOSRA
LinkDB: A0A0D2SD30_GOSRA
Original site: A0A0D2SD30_GOSRA 
ID   A0A0D2SD30_GOSRA        Unreviewed;       577 AA.
AC   A0A0D2SD30;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Glutathione reductase {ECO:0000256|RuleBase:RU365040};
DE            Short=GRase {ECO:0000256|RuleBase:RU365040};
DE            EC=1.8.1.7 {ECO:0000256|RuleBase:RU365040};
GN   ORFNames=B456_007G142200 {ECO:0000313|EMBL:KJB42209.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB42209.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB42209.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione.
CC       {ECO:0000256|RuleBase:RU365040}.
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:0000256|RuleBase:RU365040};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU365040};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; CM001746; KJB42209.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2SD30; -.
DR   STRING; 29730.A0A0D2SD30; -.
DR   EnsemblPlants; KJB42209; KJB42209; B456_007G142200.
DR   Gramene; KJB42209; KJB42209; B456_007G142200.
DR   eggNOG; KOG0405; Eukaryota.
DR   Proteomes; UP000032304; Chromosome 7.
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; IPR006324; GSHR.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   NCBIfam; TIGR01424; gluta_reduc_2; 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   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   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; NADP {ECO:0000256|RuleBase:RU365040};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT   DOMAIN          83..405
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          425..533
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   577 AA;  63072 MW;  4F0C1978F4DEB57C CRC64;
     MATTSFTAPK LSSPTFQTLC RNLPLSLPIP KTLSSFSFHL SPFLSRFHLH HHHPTPRFHP
     RRLFAVRAES ENGAEPLRHY DFDLFTIGAG SGGVRASRFA ANFGASVAVC ELPFSTISSE
     TTGGVGGTCV LRGCVPKKLM VYASKYSHEF DESNGFGWKY DTEPKHDWST LMANKNAELQ
     RLTGIYKNIL NKAGVTLIEG RGKIVDPHTV DVDGKLYTAR HILISVGGRP FIPDIPGSEY
     AIDSDAALDL PSKPEKVAIV GGGYIALEFA GIFNGLTSEV HVFIRQKKVL RGFDEEIRDF
     VGEQMALRGI QFHTEESPQA IVKSADGSLS LKTNKGTTEG FSHIMFATGR RPNTKNLGLE
     SVGVKINKNG AIEVDEYSRT TVPSIWAVGD VTDRINLTPV ALMEGAALAK TLFQNEPTKP
     DYRAVPSAVF SQPPIGQVGL TEEQAIKEYG DIDVYTANFR PLKATLSGLP DRIFMKLIVC
     AKTNKVIGLH MCGEDSAEIA QGFAVAVKAG LTKVDFDATV GIHPTSAEEF VTMRTPTRKI
     RQSSESQVYH SFSVLCIDTC SLICLIFSNL ITENHWS
//
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