ID   NAMA_BACP2              Reviewed;         338 AA.
AC   A8FEW4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   04-NOV-2026, entry version 93.
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=BPUM_2112;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(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 + 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; CP000813; ABV62781.1; -; Genomic_DNA.
DR   RefSeq; WP_012010480.1; NC_009848.4.
DR   AlphaFoldDB; A8FEW4; -.
DR   SMR; A8FEW4; -.
DR   STRING; 315750.BPUM_2112; -.
DR   PaxDb; 315750-BPUM_2112; -.
DR   GeneID; 5621378; -.
DR   KEGG; bpu:BPUM_2112; -.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_2_1_9; -.
DR   OMA; AAHQIRW; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000001355; 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; namA; 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_1000069456"
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   338 AA;  37484 MW;  55640EE0A00E7407 CRC64;
     METKLFSPWT LKGVTLKNRI VMSPMCMYSS YDRDGKLQPF HFTHYISRAQ GQAGLIMVEA
     SAVSPEGRIS DQDLGIWSDE HIEGFASLNE QIKAYGTKTA IQLAHAGRKA ELDGDILAPS
     SIPFDEQSKT PVQMSVDQIK DTVQAFQDAA VRAKKAGFDI IEIHGAHGYL INEFLSPLAN
     HRTDDYGGSP ENRYRFLREV VNAVNEVWDG PLFVRVSASD YTTKGLDIAD YIGIATWLKE
     QGVDLIDVSS GAVVQARIST FPGYQVTFAE KIKEGAGIQT GAVGLITSGV QAEEILRNQR
     ADLIFIGREF LRDPYFPKTA AEELRTSIEG PRQYDRAW
//