[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. New Asia; TISSUE=Leaf; Aono M., Fujiyama K., Sano T., Tanaka K.; Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.

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

D37870; BAA07108.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09151; T09151.

3D structure databases

HSSP

Q94655; 1ONF. [HSSP ENTRY / PDB]

ModBase

Q43154.

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 2`	`>2`	`Chloroplast (Potential).`
`CHAIN`	`3 489`	`487`	`Glutathione reductase, chloroplastic.`	`PRO_0000030283`
`NP_BIND`	`54 63`	`10`	`FAD (By similarity).`
`ACT_SITE`	`462 462`		`Proton acceptor (By similarity).`
`BINDING`	`224 224`		`NADP (By similarity).`
`BINDING`	`230 230`		`NADP (By similarity).`
`DISULFID`	`63 68`		`Redox-active (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 489 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 52611 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 970FC5B079A72CCD [This is a checksum on the sequence]

        10         20         30         40         50         60 
EDNHSTVEDD AANYDFDLFV IGAGSGGVRA ARFSANLGAK VGICELPFHP ISSEVIGGVG 

        70         80         90        100        110        120 
GTCVIRGCVP KKILVYGASF GGELEDAKNY GWELNEKIDF NWKKLLQKKT DEIIRLNNIY 

       130        140        150        160        170        180 
KRLLSNAGVK LYEGEGKIVG PNEVQVTQLD GTKLSYSAKH ILIATGSRAQ RPNIPGQELA 

       190        200        210        220        230        240 
ITSDEALSLE EFPKRVVILG GGYISVEFAS IWRGMGADVN LCFRKELPLR GFDDEMRAAV 

       250        260        270        280        290        300 
ARNLEGRGVN VHPRTTLTEL VKTDGGVVAR TDHGEEIEAD VVLFATGRSP NTKRLNLEAL 

       310        320        330        340        350        360 
GVELDRTGAV KVDEYSRTSV PSIWAIGDVT NRMNLTPVAL MEGTCFAKTV FGGQNSKPDY 

       370        380        390        400        410        420 
SNIACAVFSI PPLAVVGLSE EQAIEQASGD ILVFTSSFNP MKNTISGRQE KTIMKLVVDA 

       430        440        450        460        470        480 
ETDKVLGASM CGPDAAEIMQ GIAIALKFGA TKAQFDSTVG IHPSAAEEFV TMREPSRRVP 


GAGKPKTNL

Q43154 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