NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1325; PubMed=17704766 [NCBI, ExPASy, EBI, Israel, Japan]
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.;
"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
Nat. Biotechnol. 25:1007-1014(2007).

Comments

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

CP000560; ABS74573.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001421804.1; -.

3D structure databases

ModBase

A7Z6E7.

Ontologies

GO:0003959;	Molecular function: NADPH dehydrogenase activity (inferred from electronic annotation from HAMAP).
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.

BLOCKS

A7Z6E7.

Genome annotation databases

GeneID

5459994; -.

GenomeReviews

CP000560_GR; RBAM_022120.

KEGG

bay:RBAM_022120; -.

CMR

A7Z6E7; RBAM_022120.

Other

ProtoNet

A7Z6E7.

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`	`1 338`	`338`	`NADPH dehydrogenase.`	`PRO_0000323519`
`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: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 37643 Da [This is the MW of the unprocessed precursor]

CRC64: 662EF82ED4CAAAC2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARKLFTPWT VKDVTIKNRI VMAPMCMYSS HEKDGKLQPF HMAHYISRAI GQVGLIIVEA 

        70         80         90        100        110        120 
TAVNPQGRIS DQDLGIWSDD HIEGFAKLTE QVKAQGSKIG IQLAHAGRKA ELEGDIYAPS 

       130        140        150        160        170        180 
AIPFDEQSKT PAEMTTEQIK ETIQEFKQAA ARAKEAGFDI IELHAAHGYL MHEFLSPLSN 

       190        200        210        220        230        240 
HRTDEYGGSH ENRYRFLGET IEAVKEVWDG PLFVRISASD YTDKGLDIAD HIGFAKWMKE 

       250        260        270        280        290        300 
QGVDLIDCSS GALVQADINV FPGYQVSFAE KIREQAEIAT GAVGLITTGT MAEEILQNNR 

       310        320        330 
ADLIFVAREL LRDPHFARSA AKQLNTEIPS PVQYDRAW

A7Z6E7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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