MHQA_BACSU
ID MHQA_BACSU Reviewed; 316 AA.
AC O34689; Q7B3Q9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative ring-cleaving dioxygenase MhqA;
DE EC=1.13.11.-;
GN Name=mhqA; Synonyms=ykcA; OrderedLocusNames=BSU12870;
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 Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-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, SUBCELLULAR LOCATION, AND 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; AJ002571; CAA05567.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13144.1; -; Genomic_DNA.
DR PIR; C69855; C69855.
DR RefSeq; NP_389170.1; NC_000964.3.
DR RefSeq; WP_003245086.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34689; -.
DR SMR; O34689; -.
DR STRING; 224308.BSU12870; -.
DR PaxDb; O34689; -.
DR PRIDE; O34689; -.
DR EnsemblBacteria; CAB13144; CAB13144; BSU_12870.
DR GeneID; 936149; -.
DR KEGG; bsu:BSU12870; -.
DR PATRIC; fig|224308.179.peg.1396; -.
DR eggNOG; COG0346; Bacteria.
DR InParanoid; O34689; -.
DR OMA; PPYLEHR; -.
DR PhylomeDB; O34689; -.
DR BioCyc; BSUB:BSU12870-MON; -.
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; 2.
DR SUPFAM; SSF54593; SSF54593; 1.
DR PROSITE; PS51819; VOC; 2.
PE 2: Evidence at transcript level;
KW Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification; Dioxygenase;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..316
FT /note="Putative ring-cleaving dioxygenase MhqA"
FT /id="PRO_0000360756"
FT DOMAIN 5..131
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 154..278
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 8
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 274
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
SQ SEQUENCE 316 AA; 35387 MW; 8EE039147A3A2A2E CRC64;
MKVNGIHHVS ALTADAQKNL DFYKKVLGLK LVKKSVNQDE PTMYHLFYGD EVANPGTELT
FFEIPRIAPF HAGTNSISSI GLRVPGTEAL HYWKERFEEQ QVTHSGISKR AGRDILAFQD
HEGQRLVLTA DEEGKGYGLP VKQSGIPEEF SFRGLGPVEL TVPYAEPTLH VLTNILGFTE
ISREPVEGQG TAVILESGEG GAATEIHLIE RNDLPRERQG KGSVHHVAFR VRDEEELAGW
HRIISREGFS NSGIVERYYF KALYFREPNG ILFELSTDGP GFMVDENLDE LGQTIALPPY
LEHRRAEIEA KLKPIQ
