ID   NAMA_BACVZ              Reviewed;         338 AA.
AC   A7Z6E7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; Synonyms=yqjM;
GN   OrderedLocusNames=RBAM_022120;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
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 growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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 + H(+) + NADPH = 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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000560; ABS74573.1; -; Genomic_DNA.
DR   RefSeq; WP_003153250.1; NC_009725.2.
DR   AlphaFoldDB; A7Z6E7; -.
DR   SMR; A7Z6E7; -.
DR   STRING; 326423.RBAM_022120; -.
DR   EnsemblBacteria; ABS74573; ABS74573; RBAM_022120.
DR   GeneID; 66325823; -.
DR   KEGG; bay:RBAM_022120; -.
DR   HOGENOM; CLU_012153_2_1_9; -.
DR   OMA; NQRRDQY; -.
DR   Proteomes; UP000001120; 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   GO; GO:0018548; F:pentaerythritol trinitrate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   CDD; cd02932; OYE_YqiM_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 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   PANTHER; PTHR43303; PTHR43303; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
PE   3: Inferred from homology;
KW   Detoxification; Flavoprotein; FMN; NADP; Oxidoreductase.
FT   CHAIN           1..338
FT                   /note="NADPH dehydrogenase"
FT                   /id="PRO_0000323519"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         60
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         102
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         164..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         215
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT   BINDING         307..308
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
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