MHQE_BACSU
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 03-AUG-2022, entry version 110.
DE RecName: Full=Putative ring-cleaving dioxygenase MhqE;
DE EC=1.13.11.-;
GN Name=mhqE; Synonyms=yodE; OrderedLocusNames=BSU19570;
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;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT 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 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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND 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).
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 -!- DISRUPTION PHENOTYPE: No visible phenotype. Growth is not inhibited by
CC 2-methylhydroquinone or catechol. {ECO:0000269|PubMed:17407181}.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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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; NC_000964.3.
DR RefSeq; WP_003231191.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34543; -.
DR SMR; O34543; -.
DR STRING; 224308.BSU19570; -.
DR PaxDb; O34543; -.
DR EnsemblBacteria; CAB13848; CAB13848; BSU_19570.
DR GeneID; 940022; -.
DR KEGG; bsu:BSU19570; -.
DR PATRIC; fig|224308.179.peg.2139; -.
DR eggNOG; COG0346; Bacteria.
DR InParanoid; O34543; -.
DR OMA; DFAISFQ; -.
DR PhylomeDB; O34543; -.
DR BioCyc; BSUB:BSU19570-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; IPR000595; cNMP-bd_dom.
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 2: Evidence at transcript level;
KW Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification; Dioxygenase;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..303
FT /note="Putative ring-cleaving dioxygenase MhqE"
FT /id="PRO_0000360757"
FT DOMAIN 5..129
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 150..266
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 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
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
