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 03-AUG-2022, entry version 116.
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}.
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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 AlphaFoldDB; P96693; -.
DR SMR; P96693; -.
DR STRING; 224308.BSU05490; -.
DR PaxDb; P96693; -.
DR PRIDE; P96693; -.
DR EnsemblBacteria; CAB12356; CAB12356; BSU_05490.
DR GeneID; 939894; -.
DR KEGG; bsu:BSU05490; -.
DR PATRIC; fig|224308.179.peg.589; -.
DR eggNOG; COG0346; Bacteria.
DR InParanoid; P96693; -.
DR OMA; DHAIRGF; -.
DR PhylomeDB; P96693; -.
DR BioCyc; BSUB:BSU05490-MON; -.
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;
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 BINDING 10
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:3OAJ"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:3OAJ"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:3OAJ"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3OAJ"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3OAJ"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:3OAJ"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3OAJ"
FT TURN 279..283
FT /evidence="ECO:0007829|PDB:3OAJ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3OAJ"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:3OAJ"
FT HELIX 296..302
FT /evidence="ECO:0007829|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
