ID   GSHR_STRTR              Reviewed;         450 AA.
AC   Q60151;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Glutathione reductase;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=gor;
OS   Streptococcus thermophilus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 368;
RX   PubMed=8525054; DOI=10.1016/0923-2508(96)80283-x;
RA   Pebay M., Holl A.-C., Simonet J.-M., Decaris B.;
RT   "Characterization of the gor gene of the lactic acid bacterium
RT   Streptococcus thermophilus CNRZ368.";
RL   Res. Microbiol. 146:371-383(1995).
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   -!- SUBUNIT: Homodimer. {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   EMBL; L27672; AAB00353.1; -; Genomic_DNA.
DR   EMBL; Z29494; CAA82630.1; -; Genomic_DNA.
DR   PIR; S41386; S41386.
DR   RefSeq; WP_011225543.1; NZ_RIJE01000061.1.
DR   AlphaFoldDB; Q60151; -.
DR   SMR; Q60151; -.
DR   GeneID; 66898325; -.
DR   KEGG; sths:AVT04_02840; -.
DR   eggNOG; COG1249; Bacteria.
DR   OMA; MSKHYDY; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR006322; Glutathione_Rdtase_euk/bac.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   NCBIfam; TIGR01421; gluta_reduc_1; 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   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..450
FT                   /note="Glutathione reductase"
FT                   /id="PRO_0000067979"
FT   ACT_SITE        439
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  48712 MW;  6A0DA46BEA828804 CRC64;
     MVKEYDYIVI GGGSGGIASA NRAAMHGAKV ILFEGKEVGG TCVNVGCVPK KVMWYGAQVA
     ETLHRYAGEY GFDVTINNFD FATLKANRQA YIDRIHGSFE RGFDSNGVER VYEYARFVDP
     HTVEVAGELY TAPHILIATG GHPLYPNIPG SEYGITSDGF FELDEVPKRT AVIGAGYIAV
     EVAGVLNALG SDTHLFVRKD RPLRTFDKDI IDVLVDEMAK SGPTLHMHAN ATEVVKNADD
     SLTISFDNEE TITVDCLIWA VGRAANTSGF GLEKTGVELT ERGNIYSDEF ENTSVPGIYA
     LGDVTGKLDL TPVAVKAGRQ LSERLFNNKV DAKLDYTDVA TVVFSHPAIG AIGLTEEKAI
     AKYGAENIKV YKSSFTPMYT ALGDNRQLST MKLVTLGEDE KIIGLHGIGY GVDEMIQGFS
     VAIKMGATKA DFDNTVAIHP TGSEEFVTMR
//