Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06715

- GSHR_ECOLI

UniProt

P06715 - GSHR_ECOLI

Protein

Glutathione reductase

Gene

gor

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Maintains high levels of reduced glutathione in the cytosol.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei439 – 4391Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi34 – 418FAD

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. glutathione-disulfide reductase activity Source: EcoCyc
    3. NADP binding Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. glutathione metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
    ECOL316407:JW3467-MONOMER.
    MetaCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
    SABIO-RKP06715.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Gene namesi
    Name:gor
    Ordered Locus Names:b3500, JW3467
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10412. gor.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Glutathione reductasePRO_0000067975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 47Redox-active1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP06715.
    PRIDEiP06715.

    2D gel databases

    SWISS-2DPAGEP06715.

    Expressioni

    Gene expression databases

    GenevestigatoriP06715.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP06715. 3 interactions.
    STRINGi511145.b3500.

    Structurei

    Secondary structure

    1
    450
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Helixi14 – 2411
    Turni25 – 273
    Beta strandi30 – 367
    Helixi40 – 456
    Helixi47 – 6418
    Helixi67 – 704
    Beta strandi72 – 798
    Helixi81 – 10525
    Beta strandi109 – 1135
    Beta strandi116 – 1194
    Beta strandi122 – 1254
    Beta strandi128 – 13710
    Beta strandi141 – 1433
    Helixi151 – 1533
    Helixi157 – 1626
    Beta strandi168 – 1736
    Helixi177 – 18812
    Beta strandi192 – 1965
    Beta strandi198 – 2036
    Helixi208 – 22114
    Beta strandi224 – 2263
    Beta strandi231 – 2366
    Beta strandi242 – 2465
    Beta strandi251 – 2599
    Beta strandi263 – 2664
    Helixi268 – 2703
    Helixi272 – 2754
    Beta strandi298 – 3003
    Helixi303 – 3053
    Helixi311 – 32616
    Beta strandi341 – 3433
    Beta strandi349 – 3535
    Helixi356 – 3638
    Helixi365 – 3673
    Beta strandi368 – 3769
    Helixi378 – 3814
    Beta strandi383 – 3853
    Beta strandi388 – 3969
    Turni397 – 4004
    Beta strandi401 – 4099
    Helixi412 – 42413
    Helixi429 – 4335
    Helixi443 – 4475

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GERX-ray1.86A/B1-450[»]
    1GESX-ray1.74A/B1-450[»]
    1GETX-ray2.00A/B1-450[»]
    1GEUX-ray2.20A/B1-450[»]
    ProteinModelPortaliP06715.
    SMRiP06715. Positions 2-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06715.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    KOiK00383.
    OMAiHRQPCKM.
    OrthoDBiEOG6QCD6D.
    PhylomeDBiP06715.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06715-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKHYDYIAI GGGSGGIASI NRAAMYGQKC ALIEAKELGG TCVNVGCVPK    50
    KVMWHAAQIR EAIHMYGPDY GFDTTINKFN WETLIASRTA YIDRIHTSYE 100
    NVLGKNNVDV IKGFARFVDA KTLEVNGETI TADHILIATG GRPSHPDIPG 150
    VEYGIDSDGF FALPALPERV AVVGAGYIAV ELAGVINGLG AKTHLFVRKH 200
    APLRSFDPMI SETLVEVMNA EGPQLHTNAI PKAVVKNTDG SLTLELEDGR 250
    SETVDCLIWA IGREPANDNI NLEAAGVKTN EKGYIVVDKY QNTNIEGIYA 300
    VGDNTGAVEL TPVAVAAGRR LSERLFNNKP DEHLDYSNIP TVVFSHPPIG 350
    TVGLTEPQAR EQYGDDQVKV YKSSFTAMYT AVTTHRQPCR MKLVCVGSEE 400
    KIVGIHGIGF GMDEMLQGFA VALKMGATKK DFDNTVAIHP TAAEEFVTMR 450
    Length:450
    Mass (Da):48,773
    Last modified:January 1, 1988 - v1
    Checksum:i3C8652AFE4E4ABF6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13141 Genomic DNA. Translation: AAA23926.1.
    U00039 Genomic DNA. Translation: AAB18476.1.
    U00096 Genomic DNA. Translation: AAC76525.1.
    AP009048 Genomic DNA. Translation: BAE77794.1.
    PIRiA24409. RDECU.
    RefSeqiNP_417957.1. NC_000913.3.
    YP_491935.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76525; AAC76525; b3500.
    BAE77794; BAE77794; BAE77794.
    GeneIDi12932330.
    948014.
    KEGGiecj:Y75_p3677.
    eco:b3500.
    PATRICi32122450. VBIEscCol129921_3602.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13141 Genomic DNA. Translation: AAA23926.1 .
    U00039 Genomic DNA. Translation: AAB18476.1 .
    U00096 Genomic DNA. Translation: AAC76525.1 .
    AP009048 Genomic DNA. Translation: BAE77794.1 .
    PIRi A24409. RDECU.
    RefSeqi NP_417957.1. NC_000913.3.
    YP_491935.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GER X-ray 1.86 A/B 1-450 [» ]
    1GES X-ray 1.74 A/B 1-450 [» ]
    1GET X-ray 2.00 A/B 1-450 [» ]
    1GEU X-ray 2.20 A/B 1-450 [» ]
    ProteinModelPortali P06715.
    SMRi P06715. Positions 2-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P06715. 3 interactions.
    STRINGi 511145.b3500.

    Chemistry

    DrugBanki DB00336. Nitrofurazone.

    2D gel databases

    SWISS-2DPAGE P06715.

    Proteomic databases

    PaxDbi P06715.
    PRIDEi P06715.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76525 ; AAC76525 ; b3500 .
    BAE77794 ; BAE77794 ; BAE77794 .
    GeneIDi 12932330.
    948014.
    KEGGi ecj:Y75_p3677.
    eco:b3500.
    PATRICi 32122450. VBIEscCol129921_3602.

    Organism-specific databases

    EchoBASEi EB0407.
    EcoGenei EG10412. gor.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi HRQPCKM.
    OrthoDBi EOG6QCD6D.
    PhylomeDBi P06715.

    Enzyme and pathway databases

    BioCyci EcoCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
    ECOL316407:JW3467-MONOMER.
    MetaCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
    SABIO-RK P06715.

    Miscellaneous databases

    EvolutionaryTracei P06715.
    PROi P06715.

    Gene expression databases

    Genevestigatori P06715.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01421. gluta_reduc_1. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases."
      Greer S., Perham R.N.
      Biochemistry 25:2736-2742(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    6. "The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0-A resolution."
      Ermler U., Schulz G.E.
      Proteins 9:174-179(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    7. "Structure of glutathione reductase from Escherichia coli at 1.86-A resolution: comparison with the enzyme from human erythrocytes."
      Mittl P.R.E., Schulz G.E.
      Protein Sci. 3:799-809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), DISULFIDE BOND.

    Entry informationi

    Entry nameiGSHR_ECOLI
    AccessioniPrimary (citable) accession number: P06715
    Secondary accession number(s): Q2M7G2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 156 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3