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Protein

Glutathione reductase

Gene

gor

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei436 – 4361Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

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:PA2025
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA2025.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Glutathione reductasePRO_0000067977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 47Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP23189.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi208964.PA2025.

Structurei

3D structure databases

ProteinModelPortaliP23189.
SMRiP23189. Positions 2-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105DC8. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276712.
InParanoidiP23189.
KOiK00383.
OMAiYIERIHA.
PhylomeDBiP23189.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFDFDLFVI GAGSGGVRAA RFAAGFGARV AVAESRYLGG TCVNVGCVPK
60 70 80 90 100
KLLVYGAHFS EDFEQARAYG WSAGEAQFDW ATLIGNKNRE IQRLNGIYRN
110 120 130 140 150
LLVNSGVTLL EGHARLLDAH SVEVDGQRFS AKHILVATGG WPQVPDIPGK
160 170 180 190 200
EHAITSNEAF FLERLPRRVL VVGGGYIAVE FASIFNGLGA ETTLLYRRDL
210 220 230 240 250
FLRGFDRSVR EHLRDELGKK GLDLQFNSDI ARIDKQADGS LAATLKDGRV
260 270 280 290 300
LEADCVFYAT GRRPMLDDLG LENTAVKLTD KGFIAVDEHY QTSEPSILAL
310 320 330 340 350
GDVIGRVQLT PVALAEGMAV ARRLFKPEEY RPVDYKLIPT AVFSLPNIGT
360 370 380 390 400
VGLTEEEALS AGHKVKIFES RFRPMKLTLT DDQEKTLMKL VVDAHDDRVL
410 420 430 440 450
GCHMVGAEAG EILQGIAVAM KAGATKQAFD ETIGIHPTAA EEFVTLRTPT

R
Length:451
Mass (Da):49,237
Last modified:November 1, 1991 - v1
Checksum:i2924599996DB98EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54201 Genomic DNA. Translation: CAA38122.1.
AE004091 Genomic DNA. Translation: AAG05413.1.
PIRiS15236.
RefSeqiNP_250715.1. NC_002516.2.
WP_003100366.1. NZ_ASJY01000287.1.

Genome annotation databases

EnsemblBacteriaiAAG05413; AAG05413; PA2025.
GeneIDi878570.
KEGGipae:PA2025.
PATRICi19838459. VBIPseAer58763_2110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54201 Genomic DNA. Translation: CAA38122.1.
AE004091 Genomic DNA. Translation: AAG05413.1.
PIRiS15236.
RefSeqiNP_250715.1. NC_002516.2.
WP_003100366.1. NZ_ASJY01000287.1.

3D structure databases

ProteinModelPortaliP23189.
SMRiP23189. Positions 2-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA2025.

Proteomic databases

PaxDbiP23189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG05413; AAG05413; PA2025.
GeneIDi878570.
KEGGipae:PA2025.
PATRICi19838459. VBIPseAer58763_2110.

Organism-specific databases

PseudoCAPiPA2025.

Phylogenomic databases

eggNOGiENOG4105DC8. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276712.
InParanoidiP23189.
KOiK00383.
OMAiYIERIHA.
PhylomeDBiP23189.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSHR_PSEAE
AccessioniPrimary (citable) accession number: P23189
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 7, 2016
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. 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.