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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.

Miscellaneous

The active site is a redox-active disulfide bond.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei439Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 41FAD8

GO - Molecular functioni

  • FAD binding Source: EcoCyc
  • glutathione-disulfide reductase activity Source: EcoCyc
  • NADP binding Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciEcoCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
MetaCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
SABIO-RKiP06715.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10412. gor.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • membrane Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.
DB00336. Nitrofural.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000679751 – 450Glutathione reductaseAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 47Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP06715.
PaxDbiP06715.
PRIDEiP06715.

2D gel databases

SWISS-2DPAGEiP06715.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4261324. 17 interactors.
IntActiP06715. 3 interactors.
STRINGi511145.b3500.

Structurei

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi14 – 24Combined sources11
Turni25 – 27Combined sources3
Beta strandi30 – 36Combined sources7
Helixi40 – 45Combined sources6
Helixi47 – 64Combined sources18
Helixi67 – 70Combined sources4
Beta strandi72 – 79Combined sources8
Helixi81 – 105Combined sources25
Beta strandi109 – 113Combined sources5
Beta strandi116 – 119Combined sources4
Beta strandi122 – 125Combined sources4
Beta strandi128 – 137Combined sources10
Beta strandi141 – 143Combined sources3
Helixi151 – 153Combined sources3
Helixi157 – 162Combined sources6
Beta strandi168 – 173Combined sources6
Helixi177 – 188Combined sources12
Beta strandi192 – 196Combined sources5
Beta strandi198 – 203Combined sources6
Helixi208 – 221Combined sources14
Beta strandi224 – 226Combined sources3
Beta strandi231 – 236Combined sources6
Beta strandi242 – 246Combined sources5
Beta strandi251 – 259Combined sources9
Beta strandi263 – 266Combined sources4
Helixi268 – 270Combined sources3
Helixi272 – 275Combined sources4
Beta strandi298 – 300Combined sources3
Helixi303 – 305Combined sources3
Helixi311 – 326Combined sources16
Beta strandi341 – 343Combined sources3
Beta strandi349 – 353Combined sources5
Helixi356 – 363Combined sources8
Helixi365 – 367Combined sources3
Beta strandi368 – 376Combined sources9
Helixi378 – 381Combined sources4
Beta strandi383 – 385Combined sources3
Beta strandi388 – 396Combined sources9
Turni397 – 400Combined sources4
Beta strandi401 – 409Combined sources9
Helixi412 – 424Combined sources13
Helixi429 – 433Combined sources5
Helixi443 – 447Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06715.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105DC8. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276712.
InParanoidiP06715.
KOiK00383.
PhylomeDBiP06715.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 1 hit.
InterProiView protein in InterPro
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
PANTHERiPTHR42737. PTHR42737. 1 hit.
PfamiView protein in Pfam
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiView protein in PROSITE
PS00076. PYRIDINE_REDOX_1. 1 hit.

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.
WP_000160816.1. NZ_CP014270.1.

Genome annotation databases

EnsemblBacteriaiAAC76525; AAC76525; b3500.
BAE77794; BAE77794; BAE77794.
GeneIDi948014.
KEGGiecj:JW3467.
eco:b3500.
PATRICifig|1411691.4.peg.3222.

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.
WP_000160816.1. NZ_CP014270.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261324. 17 interactors.
IntActiP06715. 3 interactors.
STRINGi511145.b3500.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.
DB00336. Nitrofural.

2D gel databases

SWISS-2DPAGEiP06715.

Proteomic databases

EPDiP06715.
PaxDbiP06715.
PRIDEiP06715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76525; AAC76525; b3500.
BAE77794; BAE77794; BAE77794.
GeneIDi948014.
KEGGiecj:JW3467.
eco:b3500.
PATRICifig|1411691.4.peg.3222.

Organism-specific databases

EchoBASEiEB0407.
EcoGeneiEG10412. gor.

Phylogenomic databases

eggNOGiENOG4105DC8. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276712.
InParanoidiP06715.
KOiK00383.
PhylomeDBiP06715.

Enzyme and pathway databases

BioCyciEcoCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
MetaCyc:GLUTATHIONE-REDUCT-NADPH-MONOMER.
SABIO-RKiP06715.

Miscellaneous databases

EvolutionaryTraceiP06715.
PROiPR:P06715.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 1 hit.
InterProiView protein in InterPro
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
PANTHERiPTHR42737. PTHR42737. 1 hit.
PfamiView protein in Pfam
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiView protein in PROSITE
PS00076. PYRIDINE_REDOX_1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGSHR_ECOLI
AccessioniPrimary (citable) accession number: P06715
Secondary accession number(s): Q2M7G2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 7, 2017
This is version 179 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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 one 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.