(data stored in ACNUC7421 zone)

SWISSPROT: MHQN_BACSU

ID   MHQN_BACSU              Reviewed;         206 AA.
AC   P96692;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   11-DEC-2019, entry version 108.
DE   RecName: Full=Putative NAD(P)H nitroreductase MhqN;
DE            EC=1.-.-.-;
GN   Name=mhqN; Synonyms=ydfN; OrderedLocusNames=BSU05480;
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;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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   INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=17725564; DOI=10.1111/j.1365-2958.2007.05891.x;
RA   Toewe S., Leelakriangsak M., Kobayashi K., Van Duy N., Hecker M., Zuber P.,
RA   Antelmann H.;
RT   "The MarR-type repressor MhqR (YkvE) regulates multiple
RT   dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-
RT   methylhydroquinone and catechol in Bacillus subtilis.";
RL   Mol. Microbiol. 66:40-54(2007).
RN   [4]
RP   INDUCTION, IDENTIFICATION OF THE YDFNOP OPERON, SUBCELLULAR LOCATION, AND
RP   NOMENCLATURE.
RX   PubMed=17407181; DOI=10.1002/pmic.200700008;
RA   Nguyen V.D., Wolf C., Maeder U., Lalk M., Langer P., Lindequist U.,
RA   Hecker M., Antelmann H.;
RT   "Transcriptome and proteome analyses in response to 2-methylhydroquinone
RT   and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems
RT   involved in the catabolism of aromatic compounds in Bacillus subtilis.";
RL   Proteomics 7:1391-1408(2007).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT.
RG   Joint center for structural genomics (JCSG);
RT   "Crystal structure of putative nitroreductase ydfN (2632848) from Bacillus
RT   subtilis at 1.65 A resolution.";
RL   Submitted (DEC-2007) to the PDB data bank.
CC   -!- FUNCTION: Putative nitroreductase that may contribute to the
CC       degradation of aromatic compounds. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17407181,
CC       ECO:0000269|PubMed:17725564}.
CC   -!- INDUCTION: Repressed by MhqR. Strongly induced by stress due to
CC       exposure to 2-methylhydroquinone (2-MHQ) and less strongly induced
CC       after diamide or catechol stress. Not induced by oxidative stress due
CC       to hydrogen peroxide or methylglyoxal. {ECO:0000269|PubMed:17407181,
CC       ECO:0000269|PubMed:17725564}.
CC   -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA19382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AB001488; BAA19382.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB12355.1; -; Genomic_DNA.
DR   PIR; D69781; D69781.
DR   RefSeq; NP_388429.1; NC_000964.3.
DR   RefSeq; WP_003244392.1; NZ_JNCM01000031.1.
DR   PDB; 3BEM; X-ray; 1.65 A; A/B=1-206.
DR   PDBsum; 3BEM; -.
DR   SMR; P96692; -.
DR   STRING; 224308.BSU05480; -.
DR   PaxDb; P96692; -.
DR   PRIDE; P96692; -.
DR   EnsemblBacteria; CAB12355; CAB12355; BSU05480.
DR   GeneID; 939899; -.
DR   KEGG; bsu:BSU05480; -.
DR   PATRIC; fig|224308.179.peg.588; -.
DR   eggNOG; ENOG4108TVJ; Bacteria.
DR   eggNOG; COG0778; LUCA.
DR   HOGENOM; HOG000146739; -.
DR   InParanoid; P96692; -.
DR   KO; K15976; -.
DR   OMA; AFNLQHT; -.
DR   PhylomeDB; P96692; -.
DR   BioCyc; BSUB:BSU05480-MONOMER; -.
DR   EvolutionaryTrace; P96692; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.109.10; -; 1.
DR   InterPro; IPR029479; Nitroreductase.
DR   InterPro; IPR000415; Nitroreductase-like.
DR   Pfam; PF00881; Nitroreductase; 1.
DR   SUPFAM; SSF55469; SSF55469; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P96692.
DR   SWISS-2DPAGE; P96692.
KW   3D-structure; Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification;
KW   Flavoprotein; FMN; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..206
FT                   /note="Putative NAD(P)H nitroreductase MhqN"
FT                   /id="PRO_0000072717"
FT   NP_BIND         11..13
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|Ref.5"
FT   NP_BIND         68..70
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|Ref.5"
FT   NP_BIND         157..158
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         193
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         196
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|Ref.5"
FT   HELIX           1..10
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           25..35
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           41..43
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   STRAND          47..52
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           55..63
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   TURN            64..67
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           70..73
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   STRAND          74..83
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           86..89
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           90..99
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           105..122
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           124..148
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   STRAND          152..156
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           161..168
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   STRAND          174..183
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           187..189
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   HELIX           199..201
FT                   /evidence="ECO:0000244|PDB:3BEM"
FT   STRAND          203..206
FT                   /evidence="ECO:0000244|PDB:3BEM"
SQ   SEQUENCE   206 AA;  23559 MW;  99BFE7FDBD9075FC CRC64;
     MAEFTHLVNE RRSASNFLSG HPITKEDLNE MFELVALAPS AFNLQHTKYV TVLDQDVKEK
     LKQAANGQYK VVSSSAVLLV LGDKQAYQQA ADIYEGLKVL GILNKQEYDH MVQDTVSFYE
     NRGEQFKRDE AIRNASLSAM MFMLSAKEKG WDTCPMIGFD AEAVKRILNI DDQFEVVMMI
     TIGKEKTESR RPRGYRKPVN EFVEYM
//

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