GSHR_NOSS1
ID GSHR_NOSS1 Reviewed; 459 AA.
AC P48638;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutathione reductase;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
GN Name=gor; OrderedLocusNames=all4968;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7559423; DOI=10.1074/jbc.270.39.23143;
RA Jiang F., Hellman U., Sroga G.E., Bergman B., Mannervik B.;
RT "Cloning, sequencing, and regulation of the glutathione reductase gene from
RT the cyanobacterium Anabaena PCC 7120.";
RL J. Biol. Chem. 270:22882-22889(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X89712; CAA61856.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB76667.1; -; Genomic_DNA.
DR PIR; AH2426; AH2426.
DR PIR; I39477; I39477.
DR RefSeq; WP_010999094.1; NZ_RSCN01000018.1.
DR AlphaFoldDB; P48638; -.
DR SMR; P48638; -.
DR STRING; 103690.17134106; -.
DR EnsemblBacteria; BAB76667; BAB76667; BAB76667.
DR KEGG; ana:all4968; -.
DR eggNOG; COG1249; Bacteria.
DR OMA; MSKHYDY; -.
DR OrthoDB; 267896at2; -.
DR Proteomes; UP000002483; 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: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; -; 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; 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 TIGRFAMs; TIGR01424; gluta_reduc_2; 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..459
FT /note="Glutathione reductase"
FT /id="PRO_0000067973"
FT ACT_SITE 448
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"
FT CONFLICT 234
FT /note="E -> Q (in Ref. 1; CAA61856)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="R -> L (in Ref. 1; CAA61856)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="V -> L (in Ref. 1; CAA61856)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="L -> H (in Ref. 1; CAA61856)"
FT /evidence="ECO:0000305"
FT CONFLICT 381..383
FT /note="RTR -> AP (in Ref. 1; CAA61856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 49478 MW; 29C1F06CE2195888 CRC64;
MTFDYDLFVI GAGSGGLAAS KRAASYGAKV AIAENDLVGG TCVIRGCVPK KLMVYGSHFP
ALFEDAAGYG WQVGKAELNW EHFITSIDKE VRRLSQLHIS FLEKAGVELI SGRATLVDNH
TVEVGERKFT ADKILIAVGG RPIKPELPGM EYGITSNEIF HLKTQPKHIA IIGSGYIGTE
FAGIMRGLGS QVTQITRGDK ILKGFDEDIR TEIQEGMTNH GIRIIPKNVV TAIEQVPEGL
KISLSGEDQE PIIADVFLVA TGRVPNVDGL GLENAGVDVV DSSIEGPGYS TMNAIAVNEY
SQTSQPNIYA VGDVTDRLNL TPVAIGEGRA FADSEFGNNR REFSHETIAT AVFSNPQAST
VGLTEAEARA KLGDDAVTIY RTRFRPMYHS FTGKQERIMM KLVVDTKTDK VLGAHMVGEN
AAEIIQGVAI AVKMGATKKD FDATVGIHPS SAEEFVTMR
