GSHR_PSEAE
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 03-AUG-2022, entry version 153.
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; Proteobacteria; 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 / 1C /
RC 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; 287.DR97_5822; -.
DR PaxDb; P23189; -.
DR PRIDE; P23189; -.
DR EnsemblBacteria; AAG05413; AAG05413; 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 OMA; MSKHYDY; -.
DR PhylomeDB; P23189; -.
DR BioCyc; PAER208964:G1FZ6-2063-MON; -.
DR Proteomes; UP000002438; Chromosome.
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 (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase 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; -; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 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
