ID   NAMA_BACC0              Reviewed;         345 AA.
AC   B7JKM7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=BCAH820_2070;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001283; ACK91852.1; -; Genomic_DNA.
DR   RefSeq; WP_001107019.1; NC_011773.1.
DR   AlphaFoldDB; B7JKM7; -.
DR   SMR; B7JKM7; -.
DR   EnsemblBacteria; ACK91852; ACK91852; BCAH820_2070.
DR   KEGG; bcu:BCAH820_2070; -.
DR   HOGENOM; CLU_012153_2_1_9; -.
DR   OMA; NQRRDQY; -.
DR   Proteomes; UP000001363; 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..345
FT                   /note="NADPH dehydrogenase"
FT                   /id="PRO_1000185858"
FT   BINDING         23..26
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
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   345 AA;  38451 MW;  80C52E3E21634968 CRC64;
     MNYKLFSPYT IKDVTLKNRI VMSPMCMYSS ENEDGQVTNF HLVHYGTRAA GQVGLVMIEA
     TAVLPGGRIS NKDLGIWDDS LIEGLHKTTT FIHDNGAKAA IQLAHAGRKA ELETDALAPS
     AVPFNETMKT PVEMSKHQIK DTVLAFQQAA IRSKQAGFDV IEIHGAHGYL INEFLSPLSN
     KRTDEYGGSP ENRYRFLREI IDSINEVWNG PLFVRISAND YHPDGLTVQD YVQYTKWMKE
     QGVDLIDCSS GAVVPARIDV YPGYQVQYAK HIKEHANIAT GAVGLITTGA QAEQILTNNE
     ADLIFIGREL LRNPYFPRIA ANELGFELEE PYQYERAPGK ISTNK