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 03-AUG-2022, entry version 209.
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; Proteobacteria; 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}.
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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_CP047127.1.
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; P06715; -.
DR PRIDE; P06715; -.
DR EnsemblBacteria; AAC76525; AAC76525; b3500.
DR EnsemblBacteria; BAE77794; BAE77794; BAE77794.
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 PhylomeDB; P06715; -.
DR BioCyc; EcoCyc:GLUTATHIONE-REDUCT-NADPH-MON; -.
DR BioCyc; MetaCyc:GLUTATHIONE-REDUCT-NADPH-MON; -.
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 (NADPH) 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; -; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR42737; PTHR42737; 1.
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; TIGR01421; gluta_reduc_1; 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
