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Database: UniProt
Entry: A0A251TFF4_HELAN
LinkDB: A0A251TFF4_HELAN
Original site: A0A251TFF4_HELAN 
ID   A0A251TFF4_HELAN        Unreviewed;       567 AA.
AC   A0A251TFF4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-NOV-2023, entry version 27.
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   Name=GSHRP {ECO:0000313|EMBL:OTG09887.1};
GN   ORFNames=HannXRQ_Chr10g0281451 {ECO:0000313|EMBL:OTG09887.1},
GN   HanXRQr2_Chr10g0423181 {ECO:0000313|EMBL:KAF5784981.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG09887.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5784981.1, ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5784981.1};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
RN   [2] {ECO:0000313|EMBL:OTG09887.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTG09887.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5784981.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5784981.1};
RA   Gouzy J., Langlade N., Munos S.;
RT   "Helianthus annuus Genome sequencing and assembly Release 2.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
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; MNCJ02000325; KAF5784981.1; -; Genomic_DNA.
DR   EMBL; CM007899; OTG09887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251TFF4; -.
DR   STRING; 4232.A0A251TFF4; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr10g0423181; mRNA:HanXRQr2_Chr10g0423181; HanXRQr2_Chr10g0423181.
DR   Gramene; mRNA:HanXRQr2_Chr10g0423181; mRNA:HanXRQr2_Chr10g0423181; HanXRQr2_Chr10g0423181.
DR   InParanoid; A0A251TFF4; -.
DR   OMA; MSKHYDY; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000215914; Chromosome 10.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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:UP000215914}.
FT   DOMAIN          91..413
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          433..541
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   REGION          546..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   567 AA;  60848 MW;  ABE74756BC2D7EC8 CRC64;
     MATSLSTPKL GTTLSSSTLQ TFIFRHKLSI LNRSPFLITS QSPSSYSCYT PTLNLSKKAL
     GFLSDSNRKC RRFSTRAEST NGAELRSYDF DLFTIGAGSG GVRASRFAAN FGASVAVCEL
     PFATISSETT GGVGGTCVLR GCVPKKLLVY ASKYSHEFEE SLGFGWSYNS EPTHDWSTLM
     ANKNAELQRL TGIYKNILNN AGVKLIEGRG KIVDPHTVDV DGKLYTARNI LVSVGGRPFI
     PDIPGREYVI DSDAALDLPS KPTKIAIVGG GYIALEFAGI FNGLQSDVHV FIRQKQVLRG
     FDEEVRDFVA EQMSLKGIEF HTEESPQAVI KSADGSLSLK TNKGTVDGFS HVMFATGRKP
     NTKNLGLETV GVKLDKNGAI LVDEYSRTSV PSIWAVGDVT DRMNLTPVAL MEGGALAKTL
     FANEPTKPDF SAVPSAVFSQ PPIGQVGVSE QQAIEEYGDI DVYTANFRPL KATLSGLPDR
     VFMKLIVSAK TNQVVGLHMC GEDSAEVVQG FAVAIKAGLT KAQFDSTVGV HPTSAEEFVT
     MRTPTRKIRN SSSGGKTDSE AKAAAGV
//
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