GenomeNet

Database: UniProt
Entry: GSHR_ECOLI
LinkDB: GSHR_ECOLI
Original site: GSHR_ECOLI 
ID   GSHR_ECOLI              Reviewed;         450 AA.
AC   P06715; Q2M7G2;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   24-JAN-2024, entry version 216.
DE   RecName: Full=Glutathione reductase;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
GN   Name=gor; OrderedLocusNames=b3500, JW3467;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3521741; DOI=10.1021/bi00357a069;
RA   Greer S., Perham R.N.;
RT   "Glutathione reductase from Escherichia coli: cloning and sequence analysis
RT   of the gene and relationship to other flavoprotein disulfide
RT   oxidoreductases.";
RL   Biochemistry 25:2736-2742(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=2006135; DOI=10.1002/prot.340090303;
RA   Ermler U., Schulz G.E.;
RT   "The three-dimensional structure of glutathione reductase from Escherichia
RT   coli at 3.0-A resolution.";
RL   Proteins 9:174-179(1991).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), AND DISULFIDE BOND.
RX   PubMed=8061609; DOI=10.1002/pro.5560030509;
RA   Mittl P.R.E., Schulz G.E.;
RT   "Structure of glutathione reductase from Escherichia coli at 1.86-A
RT   resolution: comparison with the enzyme from human erythrocytes.";
RL   Protein Sci. 3:799-809(1994).
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;
CC       Note=Binds 1 FAD per subunit.;
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}.
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; M13141; AAA23926.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18476.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76525.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77794.1; -; Genomic_DNA.
DR   PIR; A24409; RDECU.
DR   RefSeq; NP_417957.1; NC_000913.3.
DR   RefSeq; WP_000160816.1; NZ_JACEFS010000052.1.
DR   PDB; 1GER; X-ray; 1.86 A; A/B=1-450.
DR   PDB; 1GES; X-ray; 1.74 A; A/B=1-450.
DR   PDB; 1GET; X-ray; 2.00 A; A/B=1-450.
DR   PDB; 1GEU; X-ray; 2.20 A; A/B=1-450.
DR   PDBsum; 1GER; -.
DR   PDBsum; 1GES; -.
DR   PDBsum; 1GET; -.
DR   PDBsum; 1GEU; -.
DR   AlphaFoldDB; P06715; -.
DR   SMR; P06715; -.
DR   BioGRID; 4261324; 39.
DR   IntAct; P06715; 3.
DR   STRING; 511145.b3500; -.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
DR   DrugBank; DB00336; Nitrofural.
DR   SWISS-2DPAGE; P06715; -.
DR   jPOST; P06715; -.
DR   PaxDb; 511145-b3500; -.
DR   EnsemblBacteria; AAC76525; AAC76525; b3500.
DR   GeneID; 948014; -.
DR   KEGG; ecj:JW3467; -.
DR   KEGG; eco:b3500; -.
DR   PATRIC; fig|1411691.4.peg.3222; -.
DR   EchoBASE; EB0407; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_2_2_6; -.
DR   InParanoid; P06715; -.
DR   OMA; MSKHYDY; -.
DR   OrthoDB; 9800167at2; -.
DR   PhylomeDB; P06715; -.
DR   BioCyc; EcoCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER; -.
DR   BioCyc; MetaCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER; -.
DR   SABIO-RK; P06715; -.
DR   EvolutionaryTrace; P06715; -.
DR   PRO; PR:P06715; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IDA:EcoCyc.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; 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; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Glutathione reductase"
FT                   /id="PRO_0000067975"
FT   ACT_SITE        439
FT                   /note="Proton acceptor"
FT   BINDING         34..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:8061609"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           14..24
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           47..64
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          72..79
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           81..105
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          128..137
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           157..162
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          168..173
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           177..188
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          192..196
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          198..203
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           208..221
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          224..226
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          231..236
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          251..259
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          263..266
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:1GET"
FT   HELIX           272..275
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          298..300
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           303..305
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           311..326
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          341..343
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          349..353
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           356..363
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           365..367
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          368..376
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           378..381
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          383..385
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          388..396
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   TURN            397..400
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   STRAND          401..409
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           412..424
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           429..433
FT                   /evidence="ECO:0007829|PDB:1GES"
FT   HELIX           443..447
FT                   /evidence="ECO:0007829|PDB:1GES"
SQ   SEQUENCE   450 AA;  48773 MW;  3C8652AFE4E4ABF6 CRC64;
     MTKHYDYIAI GGGSGGIASI NRAAMYGQKC ALIEAKELGG TCVNVGCVPK KVMWHAAQIR
     EAIHMYGPDY GFDTTINKFN WETLIASRTA YIDRIHTSYE NVLGKNNVDV IKGFARFVDA
     KTLEVNGETI TADHILIATG GRPSHPDIPG VEYGIDSDGF FALPALPERV AVVGAGYIAV
     ELAGVINGLG AKTHLFVRKH APLRSFDPMI SETLVEVMNA EGPQLHTNAI PKAVVKNTDG
     SLTLELEDGR SETVDCLIWA IGREPANDNI NLEAAGVKTN EKGYIVVDKY QNTNIEGIYA
     VGDNTGAVEL TPVAVAAGRR LSERLFNNKP DEHLDYSNIP TVVFSHPPIG TVGLTEPQAR
     EQYGDDQVKV YKSSFTAMYT AVTTHRQPCR MKLVCVGSEE KIVGIHGIGF GMDEMLQGFA
     VALKMGATKK DFDNTVAIHP TAAEEFVTMR
//
DBGET integrated database retrieval system