NAMA_BACSU
ID NAMA_BACSU Reviewed; 338 AA.
AC P54550;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=NADPH dehydrogenase;
DE EC=1.6.99.1 {ECO:0000269|PubMed:12660247};
DE AltName: Full=Xenobiotic reductase;
GN Name=namA; Synonyms=yqjM; OrderedLocusNames=BSU23820;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=168;
RX PubMed=12660247; DOI=10.1074/jbc.m211778200;
RA Fitzpatrick T.B., Amrhein N., Macheroux P.;
RT "Characterization of yqjM, an old yellow enzyme homolog from Bacillus
RT subtilis involved in the oxidative stress response.";
RL J. Biol. Chem. 278:19891-19897(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATES,
RP AND SUBUNIT.
RX PubMed=15890652; DOI=10.1074/jbc.m502587200;
RA Kitzing K., Fitzpatrick T.B., Wilken C., Sawa J., Bourenkov G.P.,
RA Macheroux P., Clausen T.;
RT "The 1.3 A crystal structure of the flavoprotein YqjM reveals a novel class
RT of old yellow enzymes.";
RL J. Biol. Chem. 280:27904-27913(2005).
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:0000269|PubMed:12660247}.
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:0000269|PubMed:12660247};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:12660247};
CC -!- ACTIVITY REGULATION: Inhibited by p-hydroxybenzaldehyde (pHBA) and p-
CC nitrophenol (pNP).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for duroquinone {ECO:0000269|PubMed:12660247};
CC KM=109 uM for nitroglycerin {ECO:0000269|PubMed:12660247};
CC KM=293 uM for cyclohex-2-enone {ECO:0000269|PubMed:12660247};
CC KM=705 uM for 2,4,6-trinitrotoluene {ECO:0000269|PubMed:12660247};
CC KM=841 uM for menadione {ECO:0000269|PubMed:12660247};
CC KM=2602 uM for trans-hex-2-enal {ECO:0000269|PubMed:12660247};
CC Note=The highest catalytic efficiency was observed with N-
CC ethylmaleimide for which the KM is inferior to 1.0 uM.;
CC -!- SUBUNIT: Homotetramer. Composed of a dimer of active dimers.
CC {ECO:0000269|PubMed:12660247, ECO:0000269|PubMed:15890652}.
CC -!- INDUCTION: By toxic xenobiotic compounds (2,4,6-trinitrotoluene and
CC nitroglycerin), and in response to oxidative stress (hydrogen peroxide
CC and paraquat). {ECO:0000269|PubMed:12660247}.
CC -!- MISCELLANEOUS: Forms a charge transfer complex with a variety of
CC phenolic compounds.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. NamA subfamily. {ECO:0000305}.
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DR EMBL; D84432; BAA12619.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14314.1; -; Genomic_DNA.
DR PIR; E69964; E69964.
DR RefSeq; NP_390263.1; NC_000964.3.
DR RefSeq; WP_003230377.1; NZ_JNCM01000036.1.
DR PDB; 1Z41; X-ray; 1.30 A; A/B=1-338.
DR PDB; 1Z42; X-ray; 1.85 A; A/B=1-338.
DR PDB; 1Z44; X-ray; 1.40 A; A/B=1-338.
DR PDB; 1Z48; X-ray; 1.80 A; A/B=1-338.
DR PDBsum; 1Z41; -.
DR PDBsum; 1Z42; -.
DR PDBsum; 1Z44; -.
DR PDBsum; 1Z48; -.
DR AlphaFoldDB; P54550; -.
DR SMR; P54550; -.
DR STRING; 224308.BSU23820; -.
DR PaxDb; P54550; -.
DR PRIDE; P54550; -.
DR EnsemblBacteria; CAB14314; CAB14314; BSU_23820.
DR GeneID; 938698; -.
DR KEGG; bsu:BSU23820; -.
DR PATRIC; fig|224308.179.peg.2595; -.
DR eggNOG; COG1902; Bacteria.
DR InParanoid; P54550; -.
DR OMA; NQRRDQY; -.
DR PhylomeDB; P54550; -.
DR BioCyc; BSUB:BSU23820-MON; -.
DR SABIO-RK; P54550; -.
DR EvolutionaryTrace; P54550; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Detoxification; Direct protein sequencing; Flavoprotein; FMN;
KW NADP; Oxidoreductase; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12660247"
FT CHAIN 2..338
FT /note="NADPH dehydrogenase"
FT /id="PRO_0000216119"
FT BINDING 23..26
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15890652"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15890652"
FT BINDING 60
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15890652"
FT BINDING 102
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15890652"
FT BINDING 164..167
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15890652"
FT BINDING 215
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15890652"
FT BINDING 307..308
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15890652"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1Z44"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 136..155
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:1Z41"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1Z41"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:1Z41"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:1Z41"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1Z41"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1Z41"
SQ SEQUENCE 338 AA; 37584 MW; BDC52D34236326FE CRC64;
MARKLFTPIT IKDMTLKNRI VMSPMCMYSS HEKDGKLTPF HMAHYISRAI GQVGLIIVEA
SAVNPQGRIT DQDLGIWSDE HIEGFAKLTE QVKEQGSKIG IQLAHAGRKA ELEGDIFAPS
AIAFDEQSAT PVEMSAEKVK ETVQEFKQAA ARAKEAGFDV IEIHAAHGYL IHEFLSPLSN
HRTDEYGGSP ENRYRFLREI IDEVKQVWDG PLFVRVSASD YTDKGLDIAD HIGFAKWMKE
QGVDLIDCSS GALVHADINV FPGYQVSFAE KIREQADMAT GAVGMITDGS MAEEILQNGR
ADLIFIGREL LRDPFFARTA AKQLNTEIPA PVQYERGW
