NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PAO8;
PubMed=1849605 [NCBI, ExPASy, EBI, Israel, Japan]
Perry A.C.F., Ni Bhriain N., Brown N.L., Rouch D.A.;
"Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases.";
Mol. Microbiol. 5:163-171(1991).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).

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: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X54201; CAA38122.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG05413.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15236; S15236.

RefSeq

NP_250715.1; -.

3D structure databases

HSSP

Q94655; 1ONF. [HSSP ENTRY / PDB]

ModBase

P23189.

Enzyme and pathway databases

BioCyc

PAER208964:PA2025-MON; -.

Organism-specific databases

PseudoCAP

PA2025; -.

Ontologies

GO:0004362;	Molecular function: glutathione-disulfide reductase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

BLOCKS

P23189.

Genome annotation databases

GeneID

878570; -.

GenomeReviews

AE004091_GR; PA2025.

KEGG

pae:PA2025; -.

Phylogenomic databases

HOGENOM

P23189; -.

Genome annotation databases

CMR

P23189; PA2025.

Other

ProtoNet

P23189.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 451`	`451`	`Glutathione reductase.`	`PRO_0000067977`
`NP_BIND`	`34 42`	`9`	`FAD (By similarity).`
`ACT_SITE`	`436 436`		`Proton acceptor (By similarity).`
`DISULFID`	`42 47`		`Redox-active (By similarity).`

Sequence information

Length: 451 AA [This is the length of the unprocessed precursor]

Molecular weight: 49237 Da [This is the MW of the unprocessed precursor]

CRC64: 2924599996DB98EA [This is a checksum on the sequence]

        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

P23189 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools