ID   MHQE_BACSU              Reviewed;         303 AA.
AC   O34543; Q7BVL4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   19-JAN-2010, entry version 48.
DE   RecName: Full=Putative ring-cleaving dioxygenase mhqE;
DE            EC=1.13.11.-;
GN   Name=mhqE; Synonyms=yodE; OrderedLocusNames=BSU19570;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98403883; PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA   Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A.,
RA   Ehrlich S.D., Park S.-H.;
RT   "Sequence analysis of the Bacillus subtilis 168 chromosome region
RT   between the sspC and odhA loci (184 degrees-180 degrees).";
RL   DNA Res. 5:195-201(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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.,
RA   Zuber P., Antelmann H.;
RT   "The MarR-type repressor MhqR (YkvE) regulates multiple
RT   dioxygenases/glyoxalases and an azoreductase which confer resistance
RT   to 2-methylhydroquinone and catechol in Bacillus subtilis.";
RL   Mol. Microbiol. 66:40-54(2007).
RN   [4]
RP   INDUCTION, DISRUPTION PHENOTYPE, 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-
RT   methylhydroquinone and 6-brom-2-vinyl-chroman-4-on reveal different
RT   degradation systems involved in the catabolism of aromatic compounds
RT   in Bacillus subtilis.";
RL   Proteomics 7:1391-1408(2007).
CC   -!- FUNCTION: Putative ring-cleavage dioxygenase that may contribute
CC       to the degradation of aromatic compounds (Potential).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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
CC       due to hydrogen peroxide or methylglyoxal.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Growth is not
CC       inhibited by 2-methylhydroquinone or catechol.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase
CC       family.
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DR   EMBL; AF015775; AAB72062.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13848.1; -; Genomic_DNA.
DR   PIR; B69903; B69903.
DR   RefSeq; NP_389838.1; -.
DR   HSSP; Q81H03; 1ZSW.
DR   SMR; O34543; 2-303.
DR   GeneID; 940022; -.
DR   GenomeReviews; AL009126_GR; BSU19570.
DR   KEGG; bsu:BSU19570; -.
DR   NMPDR; fig|224308.1.peg.1961; -.
DR   SubtiList; BG13534; mhqE.
DR   HOGENOM; HBG323583; -.
DR   OMA; LPLAIME; -.
DR   BioCyc; SUBTI:BSU19570-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxin; IEA:UniProtKB-KW.
DR   InterPro; IPR000595; cNMP_bd.
DR   InterPro; IPR004360; Glyas_bleo-R_dOase.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; Complete proteome; Cytoplasm;
KW   Detoxification; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    303       Putative ring-cleaving dioxygenase mhqE.
FT                                /FTId=PRO_0000360757.
FT   METAL         8      8       Iron (Potential).
FT   METAL       215    215       Iron (Potential).
FT   METAL       262    262       Iron (Potential).
SQ   SEQUENCE   303 AA;  33851 MW;  8AB061E35B1840C2 CRC64;
     MKTEGLHHVT AFARDPQENL RFYTEVLGLR LVKKTVNFDD PGTYHFYFGN QNGDPGTIMT
     FFPFQGSGQG TVGKGQAGRV YFSVPSGSLS FWKERLEKSG LSLEEKTLFG EKGLIFDDTE
     DLPLAIMEDA KSGKSEWTPD GITTNEAITG MKGVLLYSYD PQATIQLLTE SFGYTKVAEE
     DQIVRLASSA AVGGVIDVHL HPEKRGVGGY GTVHHVAFRT KKKEQAKWLP IIAENHLPSS
     EILDREYFTS VYFREKGGIL FEIATDEPGF MTDETFAELG TSLKLPEWLE KHRQQITDIL
     PEL
//