[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. STRAIN=cv. Nipponbare; PubMed=10050312 [NCBI, ExPASy, EBI, Israel, Japan] Kaminaka H., Morita S., Nakajima M., Masumura T., Tanaka K.; "Gene cloning and expression of cytosolic glutathione reductase in rice (Oryza sativa L.)."; Plant Cell Physiol. 39:1269-1280(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; The international rice genome sequencing project (IRGSP) consortium; "Oryza sativa nipponbare chromosome 2 genomic DNA sequence."; Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 355-413. PubMed=12399401 [NCBI, ExPASy, EBI, Israel, Japan] Olsen K.M., Purugganan M.D.; "Molecular evidence on the origin and evolution of glutinous rice."; Genetics 162:941-950(2002).

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.
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

D78136; BAA11214.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D85751; BAA36283.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009592; BAA37092.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP004120; BAD21653.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP005691; BAD22392.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136760; AAN15933.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136761; AAN15934.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136762; AAN15935.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136763; AAN15936.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136764; AAN15937.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136765; AAN15938.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136766; AAN15939.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T03766; T03766.

NP_001048485.1; -.

3D structure databases

HSSP

P39040; 1FEC. [HSSP ENTRY / PDB]

ModBase

P48642.

Organism-specific databases

Gramene

P48642; -.

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.

BLOCKS

P48642.

Genome annotation databases

GeneID

4331112; -.

KEGG

osa:4331112; -.

Other

ProtoNet

P48642.

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`	`1 496`	`496`	`Glutathione reductase, cytosolic.`	`PRO_0000067963`
`NP_BIND`	`61 70`	`10`	`FAD (By similarity).`
`ACT_SITE`	`469 469`		`Proton acceptor (By similarity).`
`BINDING`	`231 231`		`NADP (By similarity).`
`BINDING`	`237 237`		`NADP (By similarity).`
`DISULFID`	`70 75`		`Redox-active (By similarity).`
`CONFLICT`	`31 31`		`G -> V (in Ref. 1; BAA11214).`
`CONFLICT`	`48 48`		`V -> F (in Ref. 1; BAA11214).`
`CONFLICT`	`97 97`		`F -> L (in Ref. 1; BAA11214).`

Sequence information

Length: 496 AA [This is the length of the unprocessed precursor]

Molecular weight: 53507 Da [This is the MW of the unprocessed precursor]

CRC64: A27FEE5D847F97F6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARKMLKDEE VEVAVTDGGS YDYDLFVIGA GSGGVRGSRT SASFGAKVAI CELPFHPISS 

        70         80         90        100        110        120 
DWQGGHGGTC VIRGCVPKKI LVYGSSFRGE FEDAKNFGWE INGDINFNWK RLLENKTQEI 

       130        140        150        160        170        180 
VRLNGVYQRI LGNSGVTMIE GAGSLVDAHT VEVTKPDGSK QRYTAKHILI ATGSRAQRVN 

       190        200        210        220        230        240 
IPGKELAITS DEALSLEELP KRAVILGGGY IAVEFASIWK GMGAHVDLFY RKELPLRGFD 

       250        260        270        280        290        300 
DEMRTVVASN LEGRGIRLHP GTNLSELSKT ADGIKVVTDK GEEIIADVVL FATGRTPNSQ 

       310        320        330        340        350        360 
RLNLEAAGVE VDNIGAIKVD DYSRTSVPNI WAVGDVTNRI NLTPVALMEA TCFSKTVFGG 

       370        380        390        400        410        420 
QPTKPDYRDV PCAVFSIPPL SVVGLSEQQA LEEAKSDVLV YTSSFNPMKN SISKRQEKTV 

       430        440        450        460        470        480 
MKLVVDSETD KVLGASMCGP DAPEIIQGMA VALKCGATKA TFDSTVGIHP SAAEEFVTMR 

       490 
TLTRRVSPSS KPKTNL

P48642 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