ID   GSHR_SPISP              Reviewed;          58 AA.
AC   P11804;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   08-NOV-2023, entry version 77.
DE   RecName: Full=Glutathione reductase;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
DE   Flags: Fragments;
OS   Spirulina sp.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Spirulinales; Spirulinaceae;
OC   Spirulina.
OX   NCBI_TaxID=1157;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BOND.
RX   PubMed=2499573; DOI=10.1093/oxfordjournals.jbchem.a122674;
RA   Cui J.-Y., Wakabayashi S., Wada K., Fukuyama K., Matsubara H.;
RT   "Isolation and sequence studies of cysteinyl peptides from Spirulina
RT   glutathione reductase: comparison of active site cysteine peptides with
RT   those of other flavoprotein disulfide oxidoreductases.";
RL   J. Biochem. 105:390-394(1989).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
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.
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   PIR; PX0017; PX0017.
DR   AlphaFoldDB; P11804; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   NADP; Oxidoreductase; Redox-active center.
FT   CHAIN           <1..>58
FT                   /note="Glutathione reductase"
FT                   /id="PRO_0000067978"
FT   BINDING         5..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..18
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:2499573"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000305"
FT   NON_CONS        43..44
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         58
SQ   SEQUENCE   58 AA;  5952 MW;  B2C2A050EF55B5EF CRC64;
     VAIAENSVVG GTCVIRGCVP KLTLTGDDTE PLIVDALLCA TGRTTQSNIF AVGDCTDR
//