[1]	NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION. STRAIN=cv. Seoul; TISSUE=Leaf; DOI=10.1016/S0167-4781(97)00198-X; PubMed=9512665 [NCBI, ExPASy, EBI, Israel, Japan] Lee H.S., Jo J.K., Son D.Y.; "Molecular cloning and characterization of the gene encoding glutathione reductase in Brassica campestris."; Biochim. Biophys. Acta 1395:309-314(1998).
[2]	SEQUENCE REVISION. Lee H.S., Chung M.S., Jo J.K., Son D.Y.; Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE. STRAIN=cv. Seoul; Lee H.S., Lee B., Won S., Jo J.K.; "Genomic cloning and its expression analysis of glutathione reductase from Brassica campestris var. Pekinensis."; Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Maintains high levels of reduced glutathione in the cytosol (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + NADP⁺ = glutathione disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
INDUCTION: By paraquat and ozone.
MISCELLANEOUS: The active site is a redox-active disulfide bond (By similarity).
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

AF008441; AAC49980.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF255651; AAF67753.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T14394; T14394.

3D structure databases

HSSP

Q94655; 1ONF. [HSSP ENTRY / PDB]

ModBase

O04955.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
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: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.
IPR006324; Glut_reduct_pln.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR001864; Trypnth_redctse.
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.
PR00470; TRYPANRDTASE.

ProDom

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

TIGRFAMs

TIGR01424; gluta_reduc_2; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

Other

ProtoNet

O04955.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 502`	`502`	`Glutathione reductase, cytosolic.`	`PRO_0000067962`
`NP_BIND`	`67 76`	`10`	`FAD (By similarity).`
`ACT_SITE`	`475 475`		`Proton acceptor (By similarity).`
`BINDING`	`237 237`		`NADP (By similarity).`
`BINDING`	`243 243`		`NADP (By similarity).`
`DISULFID`	`76 81`		`Redox-active (By similarity).`

Sequence information

Length: 502 AA [This is the length of the unprocessed precursor]

Molecular weight: 54059 Da [This is the MW of the unprocessed precursor]

CRC64: 397D978EE114B6BE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARKMLSDGE LNKAAAAGEE ATTETHYDFD LFVIGAGSGG VRAARFSANN GAKVGICELP 

        70         80         90        100        110        120 
FHPISSEEIG GVGGTCVIRG CVPKKILVYG ATYGGELEDA RNYGWEINGN VDFNWKKLLQ 

       130        140        150        160        170        180 
KKTDEILRLN NIYKRLLANA AVKLYEGEGR IVGPNEVEVR QIDGTKISYT AKHILIATGS 

       190        200        210        220        230        240 
RAQKPNIPGH ELAITSDEAL SLEEFPKRAI VLGGGYIAVE FASIWRGMGA TVDLFFRKEL 

       250        260        270        280        290        300 
PLRGFDDEMR ALVARNLEGR GINLHPQTSL AELIKTDDGI KVISSHGEEF VADVVLFATG 

       310        320        330        340        350        360 
RIPNTKRLNL EAVGVELDQA GAVKVDEYSR TNIPSIWAVG DATNRINLTP VALMEATCFA 

       370        380        390        400        410        420 
NTVFGGKPAK ADYTNVACAV FCIPPLAVVG LSEEEAVEKA TGDILVFTSG FNPMKNTISG 

       430        440        450        460        470        480 
RQEKSLMKLI VDEKTDKVIG ASMCGPDAAE IMQGIAIALK CGATKAQFDS TVGIHPSSAE 

       490        500 
EFVTMRTVTR RIAYKAKPQT SL

O04955 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