[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1007/BF00202667; PubMed=8547821 [NCBI, ExPASy, EBI, Israel, Japan] Creissen G.P., Mullineaux P.M.; "Cloning and characterisation of glutathione reductase cDNAs and identification of two genes encoding the tobacco enzyme."; Planta 197:422-425(1995).
[2]	PROTEIN SEQUENCE OF 67-74. TISSUE=Leaf; Willows R.D., Kannangara G.C., Svendsen I.; Submitted (JUN-1995) to UniProtKB.

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.
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

X76293; CAA53925.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S38908; S38908.

3D structure databases

HSSP

P39040; 1FEB. [HSSP ENTRY / PDB]

ModBase

P80461.

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

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

Keywords

Chloroplast; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase; Plastid; Redox-active center; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 66`	`>66`	`Chloroplast.`
`CHAIN`	`67 557`	`491`	`Glutathione reductase, chloroplastic.`	`PRO_0000030284`
`NP_BIND`	`118 127`	`10`	`FAD (By similarity).`
`ACT_SITE`	`521 521`		`Proton acceptor (By similarity).`
`BINDING`	`283 283`		`NADP (By similarity).`
`BINDING`	`289 289`		`NADP (By similarity).`
`DISULFID`	`127 132`		`Redox-active (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 557 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 60035 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 79813D1C6AA1D784 [This is a checksum on the sequence]

        10         20         30         40         50         60 
ATSLSTPKLS TTLSSPTLHS LLYKHKFSLL SLSNPIKPLH FNFLTHSRST PSSLSCTRRR 

        70         80         90        100        110        120 
FTAPRAESSN GADAPRHYDF DLFTIGAGSG GVRASRFASN FGASVAVCEL PFSTISSDST 

       130        140        150        160        170        180 
GGVGGTCVLR GCVPKKLLVY ASKYSHEFEE SCGFGWNYDV EPRFDWSTLI ANKNAELQRL 

       190        200        210        220        230        240 
TGIYKNILKN AGVTLIEGRG KVVDPHTVDV DGKLYSAKNI LISVGGRPFI PDIPGSEYAI 

       250        260        270        280        290        300 
DSDAALDLPT KPNKIAIVGG GYIALEFAGI FNGLKSEVHV FIRQKKVLRG FDEEIRDFVG 

       310        320        330        340        350        360 
EQMSLRGIEF HTEESPQAIV KSADGSLSLK TSRGTVEGFS HIMFATGRRP NTKNLGLETV 

       370        380        390        400        410        420 
GVKMTKNGAI EVDEYSRTSV PSIWAVGDVT DRINLTPVAL MEGGALAKTI FAHEPTKPDY 

       430        440        450        460        470        480 
RNVPAAVFSQ PPIGQVGLME EQAIKEFGDV DVYTANFRPL KATISGLPDR VFMKLIVCAK 

       490        500        510        520        530        540 
TSKVLGLHMC GDDAPEIVQG FAIAVKAGLT KADFDATVGI HPTSAEEFVT MRTPTRKVRS 

       550 
SPSEGKAEHD IKAAAGV

P80461 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