[1]	NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT. DOI=10.1016/S0014-5793(99)01625-7; PubMed=10606758 [NCBI, ExPASy, EBI, Israel, Japan] Sparla F., Tedeschi G., Pupillo P., Trost P.; "Cloning and heterologous expression of NAD(P)H:quinone reductase of Arabidopsis thaliana, a functional homologue of animal DT-diaphorase."; FEBS Lett. 463:382-386(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/7.3.217; PubMed=10907853 [NCBI, ExPASy, EBI, Israel, Japan] Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."; DNA Res. 7:217-221(2000).

Comments

FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways.
CATALYTIC ACTIVITY: NAD(P)H + a quinone = NAD(P)⁺ + a hydroquinone.
COFACTOR: FMN.
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the ssuE 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

AF145234; AAD37373.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000371; BAB02535.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_189427.1; -.

UniGene

At.5735

3D structure databases

ModBase

Q9LK88.

Organism-specific databases

TAIR

At3g27890; -.

Gene expression databases

GermOnline

AT3G27890; Arabidopsis thaliana.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from direct assay from TAIR).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from TAIR).
GO:0010319;	Cellular component: stromule (inferred from direct assay from TAIR).
GO:0003955;	Molecular function: NAD(P)H dehydrogenase (quinone) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005025; FMN_red.
Graphical view of domain structure.

Pfam

PF03358; FMN_red; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

822411; -.

GenomeReviews

BA000014_GR; AT3G27890.

KEGG

ath:AT3G27890; -.

NMPDR

fig|3702.1.peg.15079; -.

Other

UniRef

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

Keywords

Complete proteome; Flavoprotein; FMN; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 196`	`196`	`NADPH:quinone oxidoreductase.`	`PRO_0000160601`
`CONFLICT`	`178 178`		`R -> K (in Ref. 1; AAD37373).`

Sequence information

Length: 196 AA [This is the length of the unprocessed precursor]

Molecular weight: 21556 Da [This is the MW of the unprocessed precursor]

CRC64: FE74952BC1CB2C18 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAVTAIKPL IRVAALSGSL RKTSFHTGLL RAAIDLTKES VPGLQIEYID ISPLPLINTD 

        70         80         90        100        110        120 
LEVNGTYPPV VEAFRQKILE ADSILFASPE YNFSVSAPLK NALDWASRPP NVWADKPAAI 

       130        140        150        160        170        180 
ISTGGGFGGG RSQYHLRQIG VFLDLHFINK PEFTLNAFQP PQKFDAEGNL VDEVTKERLK 

       190 
QVLLSLQAFT LRLQGK

Q9LK88 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