ID NAMA_BACA2 Reviewed; 338 AA. AC A7Z6E7; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 15. DE RecName: Full=NADPH dehydrogenase; DE EC=1.6.99.1; DE AltName: Full=Xenobiotic reductase; GN Name=namA; Synonyms=yqjM; OrderedLocusNames=RBAM_022120; OS Bacillus amyloliquefaciens (strain FZB42). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). CC -!- FUNCTION: Catalyzes the reduction of the double bond of an array CC of alpha, beta-unsaturated aldehydes and ketones. It also reduces CC the nitro group of nitroester and nitroaromatic compounds. It CC could have a role in detoxification processes (By similarity). CC -!- CATALYTIC ACTIVITY: NADPH + acceptor = NADP(+) + reduced acceptor. CC -!- COFACTOR: FMN (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase CC family. NamA subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000560; ABS74573.1; -; Genomic_DNA. DR RefSeq; YP_001421804.1; -. DR GeneID; 5459994; -. DR GenomeReviews; CP000560_GR; RBAM_022120. DR KEGG; bay:RBAM_022120; -. DR OMA; A7Z6E7; WVEDGWN. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01614; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001155; OxRdtase_FMN_N. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF00724; Oxidored_FMN; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; NADP; Oxidoreductase. FT CHAIN 1 338 NADPH dehydrogenase. FT /FTId=PRO_0000323519. FT BINDING 28 28 Substrate (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 167 167 Substrate (By similarity). FT BINDING 215 215 FMN (By similarity). FT BINDING 308 308 FMN (By similarity). SQ SEQUENCE 338 AA; 37643 MW; 662EF82ED4CAAAC2 CRC64; MARKLFTPWT VKDVTIKNRI VMAPMCMYSS HEKDGKLQPF HMAHYISRAI GQVGLIIVEA TAVNPQGRIS DQDLGIWSDD HIEGFAKLTE QVKAQGSKIG IQLAHAGRKA ELEGDIYAPS AIPFDEQSKT PAEMTTEQIK ETIQEFKQAA ARAKEAGFDI IELHAAHGYL MHEFLSPLSN HRTDEYGGSH ENRYRFLGET IEAVKEVWDG PLFVRISASD YTDKGLDIAD HIGFAKWMKE QGVDLIDCSS GALVQADINV FPGYQVSFAE KIREQAEIAT GAVGLITTGT MAEEILQNNR ADLIFVAREL LRDPHFARSA AKQLNTEIPS PVQYDRAW //