NAMA_ALKHC
ID NAMA_ALKHC Reviewed; 338 AA.
AC Q9KCT8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; OrderedLocusNames=BH1481;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05200.1; -; Genomic_DNA.
DR PIR; A83835; A83835.
DR RefSeq; WP_010897646.1; NC_002570.2.
DR AlphaFoldDB; Q9KCT8; -.
DR SMR; Q9KCT8; -.
DR STRING; 272558.10174098; -.
DR EnsemblBacteria; BAB05200; BAB05200; BAB05200.
DR KEGG; bha:BH1481; -.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_2_1_9; -.
DR OMA; NQRRDQY; -.
DR OrthoDB; 1033671at2; -.
DR Proteomes; UP000001258; 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..338
FT /note="NADPH dehydrogenase"
FT /id="PRO_0000216116"
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 163..166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 214
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 306..307
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
SQ SEQUENCE 338 AA; 37170 MW; AFC02D5B5595BEAF CRC64;
MEHKLFSSYV VKGVTLKNRI VMSPMCMYSS DQKDGKIRPF HISHYESRAA GQVGLIIVEA
TAVTPQGRIS PYDLGIWSDD HISGLTETVE RIHAHGAKAA IQLAHAGRKA ELDGPIIAPS
AISYDKMKTP DAMTEEQISE TIEAFKLGAL RAKKAGFDII EIHGAHGYLI NEFLSPLTNK
RTDAYGGSLE NRYRLLREII SEIQTVWDGP LFVRISAAEY AEGGNELSDF ITLAKWMKKQ
GIDLIDCSSG AVVPAPIPVY PGYQVPLAEA IRHEANIATG AVGLITSGIQ AEEILQNERA
DLIFVARELL RNPYWPREAA LELGTTISGP SQYDRAWL