ID   NAMA_LISIN              Reviewed;         338 AA.
AC   Q928C2;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=NADPH dehydrogenase;
DE            EC=1.6.99.1;
DE   AltName: Full=Xenobiotic reductase;
GN   Name=namA; OrderedLocusNames=lin2614;
OS   Listeria innocua.
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1642;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP 11262 / Serovar 6a;
RX   MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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.
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DR   EMBL; AL596173; CAC97841.1; -; Genomic_DNA.
DR   PIR; AI1758; AI1758.
DR   RefSeq; NP_471944.1; -.
DR   HSSP; Q9XG54; 1ICQ.
DR   GeneID; 1131443; -.
DR   GenomeReviews; AL592022_GR; lin2614.
DR   KEGG; lin:lin2614; -.
DR   NMPDR; fig|272626.1.peg.2597; -.
DR   ListiList; LIN2614; -.
DR   HOGENOM; Q928C2; -.
DR   OMA; Q928C2; WVEDGWN.
DR   BioCyc; LINN272626:LIN2614-MON; -.
DR   BRENDA; 1.6.99.1; 270396.
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_0000216122.
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;  37120 MW;  491FECA770CA6C48 CRC64;
     MSKLFSEYKL KDVTLKNRIV MSPMCMYSVE NKDGIATDFH FAHYVSRAAG GTGLVILEAT
     AVQEVGRISE FDLGLWNDEQ VPALKRLVDG LHYHGAKAGI QLAHAGRKAV LPGEIVAPSA
     IPFDEKSAKP VELTKEAIKE VVADFKRAAY RAKEAGFDVI EIHAAHGYLI HQFLSPISNR
     REDNYGGPAG NRYKILSDII KAVKEVWDGP IIVRVSATDY AHGGLQLEDH IPFAKWMKAD
     GVELIDVSTG GLVNVEPPVF PGYQVPFADE IRRGAGIATG ALGLITRGEQ AEEILCNERA
     DLIIIGRELL RNPYFAKEAA ETLGETIEAP KQYSRAWK
//