NAMA_BACLD
ID NAMA_BACLD Reviewed; 339 AA.
AC Q65HN9; Q62T42;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=BLi02551, BL00797;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; AE017333; AAU41425.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU24067.1; -; Genomic_DNA.
DR AlphaFoldDB; Q65HN9; -.
DR SMR; Q65HN9; -.
DR STRING; 279010.BL00797; -.
DR EnsemblBacteria; AAU24067; AAU24067; BL00797.
DR KEGG; bld:BLi02551; -.
DR KEGG; bli:BL00797; -.
DR PATRIC; fig|279010.13.peg.2585; -.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_2_1_9; -.
DR OMA; NQRRDQY; -.
DR Proteomes; UP000000606; 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;
KW Reference proteome.
FT CHAIN 1..339
FT /note="NADPH dehydrogenase"
FT /id="PRO_0000216118"
FT BINDING 24..27
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 61
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 103
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 165..168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 216
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 308..309
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
SQ SEQUENCE 339 AA; 37405 MW; A6AE937304B34654 CRC64;
MSNRKLFTPW SLKGVTLKNR IVMSPMCMYS SHEKDGKVQP FHMTHYISRA VGQVGLIMVE
ATAVTPQGRI SDQDLGIWDD AHIDGLAALT SQIKTYGSKT AIQLAHAGRK AEVEGTIYGP
SAIPFDENSR TPVEMTKEDI KETVQAFKKG AERAKAAGFD IIEIHGAHGY LINEFLSPLS
NKREDEYGGS PENRYRLLRE VIDAVKEVWA GPLFVRVSAS DYKTKGLDVA DYVGFAKWMK
EQGVDLIDVS SGAVVPADIN VFPGYQVGFA DTIRAQAEIQ TGAVGLITSG LQAEEILQNG
RADLIFVARE LLRDPYWPKT AAKQLNTKIE GPVQYDRAW
