ID NAMA_LISW6 Reviewed; 338 AA. AC A0ALF5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 1. DT 16-JUN-2009, entry version 18. DE RecName: Full=NADPH dehydrogenase; DE EC=1.6.99.1; DE AltName: Full=Xenobiotic reductase; GN Name=namA; OrderedLocusNames=lwe2419; OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / OS SLCC5334). OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=386043; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16936040; DOI=10.1128/JB.00758-06; RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., RA Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., RA Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., RA Liang C., Dandekar T., Lampidis R., Kreft J., Goebel W., RA Chakraborty T.; RT "Whole-genome sequence of Listeria welshimeri reveals common steps in RT genome reduction with Listeria innocua as compared to Listeria RT monocytogenes."; RL J. Bacteriol. 188:7405-7415(2006). 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; AM263198; CAK21837.1; -; Genomic_DNA. DR RefSeq; YP_850616.1; -. DR GeneID; 4464713; -. DR GenomeReviews; AM263198_GR; lwe2419. DR KEGG; lwe:lwe2419; -. DR NMPDR; fig|386043.6.peg.2350; -. DR OMA; A0ALF5; 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_1000069458. FT NP_BIND 22 26 FMN (By similarity). FT BINDING 27 27 Substrate (By similarity). FT BINDING 163 163 Substrate (By similarity). FT BINDING 166 166 Substrate (By similarity). FT BINDING 214 214 FMN (By similarity). FT BINDING 307 307 FMN (By similarity). SQ SEQUENCE 338 AA; 36966 MW; 983EB10CB1DE0572 CRC64; MSKLFSEYKL KDVTLKNRIV MSPMCMYSVE NKDGIATDFH FAHYVSRAAG GTGLVILEAT AVQEVGRISE FDLGLWNDEQ VPALKHLVDG LHSHGAKAGI QLAHAGRKAV LPGEIVAPSA IAYDEKSAKP VELTKEAIKE VVADFKRAAY RAKEAGFDVI EIHAAHGYLI HQFLSPITNR REDNYGGPAG NRYKILSDII KAVKEVWDGP IIVRVSATDY AHGGLQLEDY IPFAKWMKAD GVELIDVSTG GLVNVAPPVF PGYQVPFADE IRRGAGIATG VLGLITRGEQ AEEILCNERA DLIIIGRELL RNPYFAKDAA LSLGETIEGP KQYSRAWK //