Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione reductase

Gene

gor

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADNote: 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. mercury (II) reductase activity Source: InterPro
  4. mercury ion binding Source: InterPro
  5. NADP binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. detoxification of mercury ion Source: InterPro
  3. glutathione metabolic process Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP06715.
KOiK00383.
OMAiSFDPMII.
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

        10         20         30         40         50
MTKHYDYIAI GGGSGGIASI NRAAMYGQKC ALIEAKELGG TCVNVGCVPK
60 70 80 90 100
KVMWHAAQIR EAIHMYGPDY GFDTTINKFN WETLIASRTA YIDRIHTSYE
110 120 130 140 150
NVLGKNNVDV IKGFARFVDA KTLEVNGETI TADHILIATG GRPSHPDIPG
160 170 180 190 200
VEYGIDSDGF FALPALPERV AVVGAGYIAV ELAGVINGLG AKTHLFVRKH
210 220 230 240 250
APLRSFDPMI SETLVEVMNA EGPQLHTNAI PKAVVKNTDG SLTLELEDGR
260 270 280 290 300
SETVDCLIWA IGREPANDNI NLEAAGVKTN EKGYIVVDKY QNTNIEGIYA
310 320 330 340 350
VGDNTGAVEL TPVAVAAGRR LSERLFNNKP DEHLDYSNIP TVVFSHPPIG
360 370 380 390 400
TVGLTEPQAR EQYGDDQVKV YKSSFTAMYT AVTTHRQPCR MKLVCVGSEE
410 420 430 440 450
KIVGIHGIGF GMDEMLQGFA VALKMGATKK DFDNTVAIHP TAAEEFVTMR
Length:450
Mass (Da):48,773
Last modified:January 1, 1988 - v1
Checksum:i3C8652AFE4E4ABF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

IntActiP06715. 3 interactions.
STRINGi511145.b3500.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.
DB00336. Nitrofural.

2D gel databases

SWISS-2DPAGEP06715.

Proteomic databases

PaxDbiP06715.
PRIDEiP06715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0407.
EcoGeneiEG10412. gor.

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiP06715.
KOiK00383.
OMAiSFDPMII.
OrthoDBiEOG6QCD6D.
PhylomeDBiP06715.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP06715.
PROiP06715.

Gene expression databases

GenevestigatoriP06715.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.