NAMA_LISMF
ID NAMA_LISMF Reviewed; 338 AA.
AC Q71WV6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=LMOf2365_2444;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(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; AE017262; AAT05209.1; -; Genomic_DNA.
DR RefSeq; WP_003725406.1; NC_002973.6.
DR AlphaFoldDB; Q71WV6; -.
DR SMR; Q71WV6; -.
DR KEGG; lmf:LMOf2365_2444; -.
DR HOGENOM; CLU_012153_2_1_9; -.
DR OMA; ASMQRPW; -.
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..338
FT /note="NADPH dehydrogenase"
FT /id="PRO_0000216123"
FT BINDING 22..25
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 59
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01614"
FT BINDING 101
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; 37049 MW; FEBCAE68FEB2D5A0 CRC64;
MSKLFSEYKL KDVTLKNRIV MSPMCMYSVE NKDGIATDFH FAHYVSRAAG GTGLVILEAT
AVQEVGRISE FDLGLWNDEQ VPALKKLVDG LHYHGAKAGI QLAHAGRKAV LPGEIVAPSA
IAFDEKSDKP VELTKEAIKE VVADFKRAAY RAKEAGFDVI EIHAAHGYLI HQFLSPITNR
REDNYGGPAG NRYKILSDII KAVKEVWDGP IIVRVSATDY AHGGLQLEDH IPFAKWMKAD
GVELIDVSTG GLVNVAPPVF PGYQVPFADE IRRGAGIATG ALGLITRGEQ AEEILCNERA
DLIIVGRELL RNPYFAKDAA KQLGETIEGP KQYSRAWK
