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Protein

Glutathione reductase

Gene

gor

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

  • electron transfer activity Source: InterPro
  • 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-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10412 gor

Subcellular locationi

GO - Cellular componenti

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-2DPAGEP06715

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4261324, 39 interactors
IntActiP06715, 3 interactors
STRINGi316385.ECDH10B_3676

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
OMAiKCAIIEA
PhylomeDBiP06715

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 3 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006322 Glutathione_Rdtase_euk/bac
IPR001100 Pyr_nuc-diS_OxRdtase
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
PIRSFiPIRSF000350 Mercury_reductase_MerA, 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

Similar proteinsi

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: March 28, 2018
This is version 188 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

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