[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf; PubMed=1303792 [NCBI, ExPASy, EBI, Israel, Japan] Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P.M.; "Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.)."; Plant J. 2:129-131(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Birte; DOI=10.1007/BF00208308; PubMed=8904805 [NCBI, ExPASy, EBI, Israel, Japan] Mullineaux P.M., Enard C., Hellens R., Creissen G.; "Characterisation of a glutathione reductase gene and its genetic locus from pea (Pisum sativum L.)."; Planta 200:186-194(1996).
[3]	SUBCELLULAR LOCATION. PubMed=7670502 [NCBI, ExPASy, EBI, Israel, Japan] Creissen G.P., Reynolds H., Xue Y., Mullineaux P.M.; "Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco."; Plant J. 8:167-175(1995).

Comments

FUNCTION: Maintains high levels of reduced glutathione in the chloroplast.
CATALYTIC ACTIVITY: 2 glutathione + NADP⁺ = glutathione disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion. Note=The majority of the protein is found in chloroplast, with only 3% in mitochondria.
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

X60373; CAA42921.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X90996; CAA62482.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S18973; S18973.

3D structure databases

HSSP

Q94655; 1ONF. [HSSP ENTRY / PDB]

ModBase

P27456.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
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: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.
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

TIGR01424; gluta_reduc_2; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

Other

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

Keywords

Chloroplast; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Plastid; Redox-active center; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 60`	`60`	`Chloroplast and mitochondrion (Potential).`
`CHAIN`	`61 552`	`492`	`Glutathione reductase, chloroplastic/mitochondrial.`	`PRO_0000030281`
`NP_BIND`	`112 121`	`10`	`FAD (By similarity).`
`ACT_SITE`	`515 515`		`Proton acceptor (By similarity).`
`BINDING`	`277 277`		`NADP (By similarity).`
`BINDING`	`283 283`		`NADP (By similarity).`
`DISULFID`	`121 126`		`Redox-active (By similarity).`

Sequence information

Length: 552 AA [This is the length of the unprocessed precursor]

Molecular weight: 59108 Da [This is the MW of the unprocessed precursor]

CRC64: 690D1058AE4168BC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNQAMATPLS LSCCSPTLTR STLFFTKTFP FSRSFSTPLP LSTKTLISLS PPHRTFAVRA 

        70         80         90        100        110        120 
ESQNGADPAR QYDFDLFTIG AGSGGVRASR FASNFGASSA VCELPFSTIS SDTTGGVGGT 

       130        140        150        160        170        180 
CVIRGCVPKK LLVYASKFSH EFEESNGFGW RYDSEPKHDW SSLIANKNAE LQRLTGIYKN 

       190        200        210        220        230        240 
TLKNAGVKLI EGRGKIVDAH TVDVDGKLYS AKHILVSVGG RPFIPDIPGK EYAIDSDAAL 

       250        260        270        280        290        300 
DLPSKPQKIA IVGGGYIALE FAGIFNGLKS EVHVFIRQKK VLRGFDEEIR DFVAENMALR 

       310        320        330        340        350        360 
GIEFHTEESP VAITKAADGS LSLKTNKGTE EGFSHIMFAT GRSPNTKDLG LESVGVKVAK 

       370        380        390        400        410        420 
DGSIEVDEYS QTSVPSIWAI GDATNRVNLT PVALMEGVAL AKTLFQNEPT KPDYRAIPSA 

       430        440        450        460        470        480 
VFSQPPIGGV GLTEEQAAEQ YGDIDVFTAN FRPMKATLSG LPDRVFMKLI VSAETNVVLG 

       490        500        510        520        530        540 
LHMCGEDAAE IAQGFAVGIK AGLTKADFDA TVGIHPTAAE EFVTMRTPTR KVRKNQASQG 

       550 
KSDSKAKAVA GS

P27456 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