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 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. DR SWISS-2DPAGE; P06715; -. 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 //