NAMA_BACCR
ID NAMA_BACCR Reviewed; 345 AA.
AC Q81EF6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=BC_2023;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAP08992.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016877; AAP08992.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_831791.1; NC_004722.1.
DR RefSeq; WP_001086174.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81EF6; -.
DR SMR; Q81EF6; -.
DR STRING; 226900.BC_2023; -.
DR EnsemblBacteria; AAP08992; AAP08992; BC_2023.
DR KEGG; bce:BC2023; -.
DR PATRIC; fig|226900.8.peg.2032; -.
DR HOGENOM; CLU_012153_2_1_9; -.
DR OMA; NQRRDQY; -.
DR Proteomes; UP000001417; 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..345
FT /note="NADPH dehydrogenase"
FT /id="PRO_0000216114"
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; 38582 MW; 77A2907FB25678FD CRC64;
MNSKLFSPYT IKNVTLKNRI VMSPMCMYSS GNEDGRVTNF HLIHYGTRAA GQVGLVMVEA
TAVLAEGRIS NNDLGIWDDN LIEGLHKTTT FIHDNGAKAA IQLAHAGRKA ELDTNAFAPS
AIPFNDKMKI PVEMNIQQIK ETILAFQRAA LRSKQAGFDV IELHGAHGYL INEFLSPLTN
KRTDKYGGSP ENRYRFLREI IDSVNEVWDG PIFVRISAND YHPDGLTVQD YVQYTKWMKE
QGIDLIDCSS GAVVPAHIDV YPGYQVQYAK HIKEHTNIAT GAVGLITTGS QAEQILNNNE
ADLIFIGREL LRNPYFPRIA ANELGFELQE PHQYKRAPGK IHTNK