ID   NAMA_BACC2              Reviewed;         345 AA.
AC   B7ITF9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=BCG9842_B3281;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
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 G9842.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001186; ACK95059.1; -; Genomic_DNA.
DR   RefSeq; WP_001086172.1; NC_011772.1.
DR   AlphaFoldDB; B7ITF9; -.
DR   SMR; B7ITF9; -.
DR   EnsemblBacteria; ACK95059; ACK95059; BCG9842_B3281.
DR   KEGG; bcg:BCG9842_B3281; -.
DR   HOGENOM; CLU_012153_2_1_9; -.
DR   OMA; NQRRDQY; -.
DR   Proteomes; UP000006744; 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_1000185859"
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;  38525 MW;  97E11E6C14FAB026 CRC64;
     MNSKLFSPYT IKNVTLKNRI VMSPMCMYSS GNEDGRVTNF HLIHYGTRAA GQVGLVMVEA
     TAVLAEGRIS NKDLGIWDDN LIEGLHKTTT FIHDNGAKAA IQLAHAGRKA ELGTNAFAPS
     AIPFSDTMKI PVEMNIQQIK ETILAFQRAA LRSKQAGFDV IELHGAHGYL INEFLSPLTN
     KRTDEYGGSP ENRYRFLREI IDSVNKVWDG PIFVRISAND YHPDGLTVQD YVQYTKWMKE
     QGIDLIDCSS GAVVPAHIDV YPGYQVQYAK HIKEYTKIAT GAVGLITTGS QAEQILNDNE
     ADLIFIGREL LRNPYFPRIA ANELGFELQE PHQYKRAPGK IHTNK