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   02-SEP-2026, entry version 100.
DE   RecName: Full=NADPH dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01614};
DE            EC=1.6.99.1 {ECO:0000255|HAMAP-Rule:MF_01614};
GN   Name=namA {ECO:0000255|HAMAP-Rule:MF_01614};
GN   OrderedLocusNames=lwe2419;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CCUG 15529
OS   / CIP 8149 / NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Listeriaceae;
OC   Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CCUG 15529 / CIP 8149 / NCTC 11857 /
RC   SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., 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 of
CC       alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro
CC       group of nitroester and nitroaromatic compounds. It could have a role
CC       in detoxification processes. {ECO:0000255|HAMAP-Rule:MF_01614}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + NADPH + H(+) = AH2 + NADP(+); Xref=Rhea:RHEA:13149,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01614};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01614};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01614}.
CC   -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC       family. NamA subfamily. {ECO:0000255|HAMAP-Rule:MF_01614}.
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DR   EMBL; AM263198; CAK21837.1; -; Genomic_DNA.
DR   RefSeq; WP_011703155.1; NC_008555.1.
DR   AlphaFoldDB; A0ALF5; -.
DR   SMR; A0ALF5; -.
DR   STRING; 386043.lwe2419; -.
DR   PaxDb; 386043-lwe2419; -.
DR   GeneID; 61190338; -.
DR   KEGG; lwe:lwe2419; -.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_2_1_9; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000000779; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02932; OYE_YqiM_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01614; NamA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR023663; NADPH_DH_bac.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   InterPro; IPR044152; YqjM-like.
DR   NCBIfam; NF010047; PRK13523.1; 1.
DR   PANTHER; PTHR43303; NADPH DEHYDROGENASE C23G7.10C-RELATED; 1.
DR   PANTHER; PTHR43303:SF4; NADPH DEHYDROGENASE C23G7.10C-RELATED; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Detoxification; Flavoprotein; FMN; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..338
FT                   /note="NADPH dehydrogenase"
FT                   /id="PRO_1000069458"
FT   BINDING         22..25
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         59
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         101
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         163..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         214
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         306..307
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
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
//