[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=AX4; DOI=10.1038/nature00847; PubMed=12097910 [NCBI, ExPASy, EBI, Israel, Japan] Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A.; "Sequence and analysis of chromosome 2 of Dictyostelium discoideum."; Nature 418:79-85(2002).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=AX4; DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan] Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; "The genome of the social amoeba Dictyostelium discoideum."; Nature 435:43-57(2005).
[3]	FUNCTION. DOI=10.1016/j.ydbio.2006.03.038; PubMed=16678813 [NCBI, ExPASy, EBI, Israel, Japan] Choi C.-H., Kim B.-J., Jeong S.-Y., Lee C.-H., Kim J.-S., Park S.-J., Yim H.-S., Kang S.-O.; "Reduced glutathione levels affect the culmination and cell fate decision in Dictyostelium discoideum."; Dev. Biol. 295:523-533(2006).

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).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

AC117075; AAM09354.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AAFI02000008; EAL71014.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_644939.1; -.

3D structure databases

HSSP

P00390; 1ALG. [HSSP ENTRY / PDB]

ModBase

Q8T137.

Organism-specific databases

dictyBase

DDB_G0272754; gsr.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0043295;	Molecular function: glutathione binding (inferred from direct assay from dictyBase).
GO:0004362;	Molecular function: glutathione-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0031154;	Biological process: culmination during sorocarp development (inferred from mutant phenotype from dictyBase).
GO:0006749;	Biological process: glutathione metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR006322; Glut_reduct_1.
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]

TIGRFAMs

TIGR01421; gluta_reduc_1; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

ProtoNet

Q8T137.

Genome annotation databases

GeneID

3396059; -.

KEGG

ddi:DDB_0231410; -.

Other

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`	`1 465`	`465`	`Glutathione reductase.`	`PRO_0000327610`
`NP_BIND`	`42 50`	`9`	`FAD (By similarity).`
`ACT_SITE`	`454 454`		`Proton acceptor (By similarity).`
`DISULFID`	`50 55`		`Redox-active (By similarity).`

Sequence information

Length: 465 AA [This is the length of the unprocessed precursor]

Molecular weight: 50483 Da [This is the MW of the unprocessed precursor]

CRC64: E89CAF09AEA6A771 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSTNHFTYL VLGAGSGGIA SARRAAKHLN AKGNGDRIGI VEVTRPGGTC VNVGCVPKKV 

        70         80         90        100        110        120 
MWNTSFIKEM INAAPSYGFD FGGQQVKFNW PTIKKARDEY IKRLNGIYDS NLAKDNIVRI 

       130        140        150        160        170        180 
NGYGRFSGPK EIQVNGANGE KYTADHILIA AGGRPTVPDV PGKELGITSD GFFELEDLPK 

       190        200        210        220        230        240 
STLVVGAGYI AVELAGVLHS LGSETTMVIR QKQFLRTFDE MLHTTLLKQM TDDGVKFVTE 

       250        260        270        280        290        300 
ASIKSLERDV DGKRIIATTN AGVKLPPVEC VIWAIGRVPN TDDLGIDKAG IQLTEQSGFI 

       310        320        330        340        350        360 
KVDEFQNTNV PGVHAVGDIC GNFLLTPVAI AAGRRLSERL FNGKSDLKFE YENVATVVFS 

       370        380        390        400        410        420 
HPPIGTVGLT EQEAITKYGT ENIKCYNTSF INMFYSVQVH KVRTSMKLVC LGKEEKVIGL 

       430        440        450        460 
HIIGDGCDEI IQGFAVAVKM GCTKWDLDNT CAIHPTSAEE LVTMV

Q8T137 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