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Reviewed, UniProtKB/Swiss-Prot P23189 (GSHR_PSEAE)

Last modified February 9, 2010. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutathione reductase
      Short name=GRase
      Short name=GR
    EC=1.8.1.7
Gene names
Name: gor
Ordered Locus Names: PA2025
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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 By similarity.

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

glutathione-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Glutathione reductase
PRO_0000067977

Regions

Nucleotide binding34 – 429FAD By similarity

Sites

Active site4361Proton acceptor By similarity

Amino acid modifications

Disulfide bond42 ↔ 47Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P23189-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 2924599996DB98EA

FASTA45149,237
        10         20         30         40         50         60 
MSFDFDLFVI GAGSGGVRAA RFAAGFGARV AVAESRYLGG TCVNVGCVPK KLLVYGAHFS 

        70         80         90        100        110        120 
EDFEQARAYG WSAGEAQFDW ATLIGNKNRE IQRLNGIYRN LLVNSGVTLL EGHARLLDAH 

       130        140        150        160        170        180 
SVEVDGQRFS AKHILVATGG WPQVPDIPGK EHAITSNEAF FLERLPRRVL VVGGGYIAVE 

       190        200        210        220        230        240 
FASIFNGLGA ETTLLYRRDL FLRGFDRSVR EHLRDELGKK GLDLQFNSDI ARIDKQADGS 

       250        260        270        280        290        300 
LAATLKDGRV LEADCVFYAT GRRPMLDDLG LENTAVKLTD KGFIAVDEHY QTSEPSILAL 

       310        320        330        340        350        360 
GDVIGRVQLT PVALAEGMAV ARRLFKPEEY RPVDYKLIPT AVFSLPNIGT VGLTEEEALS 

       370        380        390        400        410        420 
AGHKVKIFES RFRPMKLTLT DDQEKTLMKL VVDAHDDRVL GCHMVGAEAG EILQGIAVAM 

       430        440        450 
KAGATKQAFD ETIGIHPTAA EEFVTLRTPT R 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases."
Perry A.C.F., Ni Bhriain N., Brown N.L., Rouch D.A.
Mol. Microbiol. 5:163-171(1991) [PubMed: 1849605] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PAO8.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54201 Genomic DNA. Translation: CAA38122.1.
AE004091 Genomic DNA. Translation: AAG05413.1.
PIRS15236.
RefSeqNP_250715.1.

3D structure databases

SMRP23189. Positions 3-450.
ModBaseSearch...

Genome annotation databases

GeneID878570.
GenomeReviewsGene locus PA2025 in contig AE004091_GR.
KEGGpae:PA2025.

Organism-specific databases

PseudoCAPPA2025.
CMRSearch...

Phylogenomic databases

HOGENOMHBG515043.
OMASEDFDHA.

Enzyme and pathway databases

BioCycPAER208964:PA2025-MONOMER.
BRENDA1.8.1.7. 354.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHR_PSEAE
AccessionPrimary (citable) accession number: P23189
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 9, 2010
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents