(data stored in ACNUC7421 zone)

SWISSPROT: MHQO_BACSU

ID   MHQO_BACSU              Reviewed;         312 AA.
AC   P96693; Q797F9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=Putative ring-cleaving dioxygenase MhqO;
DE            EC=1.13.11.-;
GN   Name=mhqO; Synonyms=ydfO; OrderedLocusNames=BSU05490;
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.
RC   STRAIN=168;
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).
CC   -!- FUNCTION: Putative ring-cleavage dioxygenase that may contribute to the
CC       degradation of aromatic compounds. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000305};
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 extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
DR   EMBL; AB001488; BAA19383.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12356.1; -; Genomic_DNA.
DR   PIR; E69781; E69781.
DR   RefSeq; NP_388430.1; NC_000964.3.
DR   RefSeq; WP_003234172.1; NZ_JNCM01000031.1.
DR   PDB; 3OAJ; X-ray; 1.40 A; A/B=1-312.
DR   PDBsum; 3OAJ; -.
DR   SMR; P96693; -.
DR   STRING; 224308.BSU05490; -.
DR   PaxDb; P96693; -.
DR   PRIDE; P96693; -.
DR   EnsemblBacteria; CAB12356; CAB12356; BSU05490.
DR   GeneID; 939894; -.
DR   KEGG; bsu:BSU05490; -.
DR   PATRIC; fig|224308.179.peg.589; -.
DR   eggNOG; ENOG4105DA2; Bacteria.
DR   eggNOG; COG0346; LUCA.
DR   HOGENOM; HOG000221568; -.
DR   InParanoid; P96693; -.
DR   KO; K15975; -.
DR   OMA; PDVYHLY; -.
DR   PhylomeDB; P96693; -.
DR   BioCyc; BSUB:BSU05490-MONOMER; -.
DR   EvolutionaryTrace; P96693; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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; 3.10.180.10; -; 2.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   1: Evidence at protein level;
DR   PRODOM; P96693.
DR   SWISS-2DPAGE; P96693.
KW   3D-structure; Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Repeat.
FT   CHAIN           1..312
FT                   /note="Putative ring-cleaving dioxygenase MhqO"
FT                   /id="PRO_0000360690"
FT   DOMAIN          7..131
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          152..269
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   METAL           10
FT                   /note="Iron"
FT                   /evidence="ECO:0000255"
FT   METAL           217
FT                   /note="Iron"
FT                   /evidence="ECO:0000255"
FT   METAL           265
FT                   /note="Iron"
FT                   /evidence="ECO:0000255"
FT   STRAND          7..16
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   HELIX           18..25
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   TURN            26..29
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          32..38
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          45..52
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          59..65
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          76..86
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   HELIX           91..100
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          106..110
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          113..119
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          125..130
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   TURN            146..148
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          152..159
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   HELIX           163..172
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          177..182
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          185..189
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          191..195
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          197..203
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          214..224
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   HELIX           225..237
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          249..257
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          263..269
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          275..277
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   TURN            279..283
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   STRAND          284..286
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   HELIX           290..295
FT                   /evidence="ECO:0000244|PDB:3OAJ"
FT   HELIX           296..302
FT                   /evidence="ECO:0000244|PDB:3OAJ"
SQ   SEQUENCE   312 AA;  35056 MW;  9AAF05EF5996782B CRC64;
     MAKKTMGIHH ITAIVGHPQE NTDFYAGVLG LRLVKQTVNF DDPGTYHLYF GNEGGKPGTI
     ITFFPWAGAR QGVIGDGQVG VTSYVVPKGA MAFWEKRLEK FNVPYTKIER FGEQYVEFDD
     PHGLHLEIVE REEGEANTWT FGEVTPDVAI KGFGGATLLS EQPDKTADLL ENIMGLERVG
     KEGDFVRYRS AGDIGNVIDL KLTPIGRGQM GAGTVHHIAW RANDDEDQLD WQRYIASHGY
     GVTPVRDRNY FNAIYFREHG EILFEIATDP PGFAHDETQE TMGEKLMLPV QYEPHRTQIE
     QGLLPFEVRE LD
//

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