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P06715 (GSHR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione reductase

Short name=GR
Short name=GRase
EC=1.8.1.7
Gene names
Name:gor
Ordered Locus Names:b3500, JW3467
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activity

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Glutathione reductase
PRO_0000067975

Regions

Nucleotide binding34 – 418FAD

Sites

Active site4391Proton acceptor

Amino acid modifications

Disulfide bond42 ↔ 47Redox-active Ref.7

Secondary structure

..................................................................................... 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06715 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 3C8652AFE4E4ABF6

FASTA45048,773
        10         20         30         40         50         60 
MTKHYDYIAI GGGSGGIASI NRAAMYGQKC ALIEAKELGG TCVNVGCVPK KVMWHAAQIR 

        70         80         90        100        110        120 
EAIHMYGPDY GFDTTINKFN WETLIASRTA YIDRIHTSYE NVLGKNNVDV IKGFARFVDA 

       130        140        150        160        170        180 
KTLEVNGETI TADHILIATG GRPSHPDIPG VEYGIDSDGF FALPALPERV AVVGAGYIAV 

       190        200        210        220        230        240 
ELAGVINGLG AKTHLFVRKH APLRSFDPMI SETLVEVMNA EGPQLHTNAI PKAVVKNTDG 

       250        260        270        280        290        300 
SLTLELEDGR SETVDCLIWA IGREPANDNI NLEAAGVKTN EKGYIVVDKY QNTNIEGIYA 

       310        320        330        340        350        360 
VGDNTGAVEL TPVAVAAGRR LSERLFNNKP DEHLDYSNIP TVVFSHPPIG TVGLTEPQAR 

       370        380        390        400        410        420 
EQYGDDQVKV YKSSFTAMYT AVTTHRQPCR MKLVCVGSEE KIVGIHGIGF GMDEMLQGFA 

       430        440        450 
VALKMGATKK DFDNTVAIHP TAAEEFVTMR 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13141 Genomic DNA. Translation: AAA23926.1.
U00039 Genomic DNA. Translation: AAB18476.1.
U00096 Genomic DNA. Translation: AAC76525.1.
AP009048 Genomic DNA. Translation: BAE77794.1.
PIRRDECU. A24409.
RefSeqNP_417957.1. NC_000913.3.
YP_491935.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GERX-ray1.86A/B1-450[»]
1GESX-ray1.74A/B1-450[»]
1GETX-ray2.00A/B1-450[»]
1GEUX-ray2.20A/B1-450[»]
ProteinModelPortalP06715.
SMRP06715. Positions 2-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP06715. 3 interactions.
STRING511145.b3500.

Chemistry

DrugBankDB00336. Nitrofurazone.

2D gel databases

SWISS-2DPAGEP06715.

Proteomic databases

PaxDbP06715.
PRIDEP06715.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76525; AAC76525; b3500.
BAE77794; BAE77794; BAE77794.
GeneID12932330.
948014.
KEGGecj:Y75_p3677.
eco:b3500.
PATRIC32122450. VBIEscCol129921_3602.

Organism-specific databases

EchoBASEEB0407.
EcoGeneEG10412. gor.

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276712.
KOK00383.
OMAHRQPCKM.
OrthoDBEOG6QCD6D.
PhylomeDBP06715.
ProtClustDBPRK06116.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP06715.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. 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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01421. gluta_reduc_1. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06715.
PROP06715.

Entry information

Entry nameGSHR_ECOLI
AccessionPrimary (citable) accession number: P06715
Secondary accession number(s): Q2M7G2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene