FUNCTION: Catalyzes the reduction of the double bond of an array of alpha, beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes (By similarity).
CATALYTIC ACTIVITY: NADPH + acceptor = NADP⁺ + reduced acceptor.
COFACTOR: FMN (By similarity).
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.

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

CP000001; AAU18412.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_083438.1; -.

3D structure databases

ModBase

Q63CC9.

Enzyme and pathway databases

BioCyc

BCER288681:BCE33L1843-MON; -.

Ontologies

GO:0003959;	Molecular function: NADPH dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01614; -; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR001155; OxRdtase_FMN_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF00724; Oxidored_FMN; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

3025893; -.

GenomeReviews

CP000001_GR; BCE33L1843.

KEGG

bcz:BCZK1843; -.

Phylogenomic databases

HOGENOM

Q63CC9; -.

Genome annotation databases

CMR

Q63CC9; BCE33L1843.

Other

UniRef

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

Keywords

Complete proteome; Flavoprotein; FMN; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 345`	`345`	`NADPH dehydrogenase.`	`PRO_0000216115`
`NP_BIND`	`23 27`	`5`	`FMN (By similarity).`
`BINDING`	`28 28`		`Substrate (By similarity).`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`167 167`		`Substrate (By similarity).`
`BINDING`	`215 215`		`FMN (By similarity).`
`BINDING`	`308 308`		`FMN (By similarity).`

Sequence information

Length: 345 AA [This is the length of the unprocessed precursor]

Molecular weight: 38462 Da [This is the MW of the unprocessed precursor]

CRC64: 5A7191ED92406A02 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNSELFSPYT IKDVTLKNRI VMSPMCMYSS ENEDGQVTNF HLVHYGTRAA GQVGLVMIEA 

        70         80         90        100        110        120 
TAVLPEGRIS NKDLGIWDDS LIEGLHKTTT FIHDNGAKAA IQLAHAGRKA ELETDALAPS 

       130        140        150        160        170        180 
AIPFNETMKT PVEMSKHQIK DTILAFQQAA IRSKQAGFDV IEIHGAHGYL INEFLSPLSN 

       190        200        210        220        230        240 
KRTDEYGGSP ENRYRFLREI IDSINEVWNG PLFVRISAND YHPDGLTVQD YVQYTKWMKE 

       250        260        270        280        290        300 
QGVDLIDCSS GAVVPARIDV YPGYQVQYAK HIKEHANIAT GAVGLITTGA QAEQILNNNE 

       310        320        330        340 
ADLIFIGREL LRNPYFPRIA ANELGFELEE PHQYERAPGK ISTNK

Q63CC9 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