SubmitCancel

Skip Header

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

P06715

- GSHR_ECOLI

UniProt

P06715 - GSHR_ECOLI

(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)

Protein
Glutathione reductase
Gene
gor, b3500, JW3467
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

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

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. 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 reductase
PRO_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

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.

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

« 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: July 9, 2014
This is version 155 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