ID   GSHR_PSEAE              Reviewed;         451 AA.
AC   P23189;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Glutathione reductase;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=gor; OrderedLocusNames=PA2025;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAO8;
RX   PubMed=1849605; DOI=10.1111/j.1365-2958.1991.tb01837.x;
RA   Perry A.C.F., Ni Bhriain N., Brown N.L., Rouch D.A.;
RT   "Molecular characterization of the gor gene encoding glutathione reductase
RT   from Pseudomonas aeruginosa: determinants of substrate specificity among
RT   pyridine nucleotide-disulphide oxidoreductases.";
RL   Mol. Microbiol. 5:163-171(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   -!- SUBUNIT: Homodimer.
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; X54201; CAA38122.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG05413.1; -; Genomic_DNA.
DR   PIR; S15236; S15236.
DR   RefSeq; NP_250715.1; NC_002516.2.
DR   RefSeq; WP_003100366.1; NZ_QZGE01000026.1.
DR   AlphaFoldDB; P23189; -.
DR   SMR; P23189; -.
DR   STRING; 208964.PA2025; -.
DR   PaxDb; 208964-PA2025; -.
DR   GeneID; 878570; -.
DR   KEGG; pae:PA2025; -.
DR   PATRIC; fig|208964.12.peg.2110; -.
DR   PseudoCAP; PA2025; -.
DR   HOGENOM; CLU_016755_2_1_6; -.
DR   InParanoid; P23189; -.
DR   OrthoDB; 9800167at2; -.
DR   PhylomeDB; P23189; -.
DR   BioCyc; PAER208964:G1FZ6-2063-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
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:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; 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   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; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Glutathione reductase"
FT                   /id="PRO_0000067977"
FT   ACT_SITE        436
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   451 AA;  49237 MW;  2924599996DB98EA CRC64;
     MSFDFDLFVI GAGSGGVRAA RFAAGFGARV AVAESRYLGG TCVNVGCVPK KLLVYGAHFS
     EDFEQARAYG WSAGEAQFDW ATLIGNKNRE IQRLNGIYRN LLVNSGVTLL EGHARLLDAH
     SVEVDGQRFS AKHILVATGG WPQVPDIPGK EHAITSNEAF FLERLPRRVL VVGGGYIAVE
     FASIFNGLGA ETTLLYRRDL FLRGFDRSVR EHLRDELGKK GLDLQFNSDI ARIDKQADGS
     LAATLKDGRV LEADCVFYAT GRRPMLDDLG LENTAVKLTD KGFIAVDEHY QTSEPSILAL
     GDVIGRVQLT PVALAEGMAV ARRLFKPEEY RPVDYKLIPT AVFSLPNIGT VGLTEEEALS
     AGHKVKIFES RFRPMKLTLT DDQEKTLMKL VVDAHDDRVL GCHMVGAEAG EILQGIAVAM
     KAGATKQAFD ETIGIHPTAA EEFVTLRTPT R
//