(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 127.
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}.
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   SMR; P54550; -.
DR   STRING; 224308.BSU23820; -.
DR   PaxDb; P54550; -.
DR   PRIDE; P54550; -.
DR   EnsemblBacteria; CAB14314; CAB14314; BSU23820.
DR   GeneID; 938698; -.
DR   KEGG; bsu:BSU23820; -.
DR   PATRIC; fig|224308.179.peg.2595; -.
DR   eggNOG; ENOG4105CCY; Bacteria.
DR   eggNOG; COG1902; LUCA.
DR   HOGENOM; HOG000116232; -.
DR   InParanoid; P54550; -.
DR   KO; K00354; -.
DR   OMA; YNPRWPW; -.
DR   PhylomeDB; P54550; -.
DR   BioCyc; BSUB:BSU23820-MONOMER; -.
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:0052690; F:trichloro-p-hydroquinone reductive dehalogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01614; NamA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR023663; NADPH_DH.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   Pfam; PF00724; Oxidored_FMN; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54550.
DR   SWISS-2DPAGE; P54550.
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   NP_BIND         23..26
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|PubMed:15890652"
FT   NP_BIND         307..308
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|PubMed:15890652"
FT   REGION          164..167
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000269|PubMed:15890652"
FT   BINDING         28
FT                   /note="Substrate"
FT                   /evidence="ECO:0000269|PubMed:15890652"
FT   BINDING         60
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|PubMed:15890652"
FT   BINDING         102
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|PubMed:15890652"
FT   BINDING         215
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|PubMed:15890652"
FT   HELIX           4..6
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          9..11
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          14..22
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          33..35
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           39..50
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          54..64
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           65..67
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          73..75
FT                   /evidence="ECO:0000244|PDB:1Z44"
FT   HELIX           79..81
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           82..94
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          98..104
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           107..109
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          117..121
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           136..155
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          159..165
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           170..175
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   TURN            177..179
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          187..189
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           190..207
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          212..217
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           228..240
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          245..249
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   TURN            262..265
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           266..276
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          279..282
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           289..297
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   STRAND          302..306
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           308..312
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           316..323
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   HELIX           332..334
FT                   /evidence="ECO:0000244|PDB:1Z41"
FT   TURN            335..337
FT                   /evidence="ECO:0000244|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
//

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