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 16-JUN-2009, entry version 42. 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, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION. 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: Regulated by yodB, and induced by stress due to CC exposure to 2-methylhydroquinone, diamide or catechol. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF015775; AAB72062.1; -; Genomic_DNA. DR EMBL; AL009126; CAB13848.1; -; Genomic_DNA. DR PIR; B69903; B69903. DR RefSeq; NP_389838.1; -. 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; O34543; -. DR OMA; O34543; LPLAIME. DR BioCyc; BSUB224308:BSU1956-MON; -. 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; IPR004360; Glyas_bleo-R_dOase. DR InterPro; IPR000486; Xdiol_dOase_1_2. DR Pfam; PF00903; Glyoxalase; 1. DR ProDom; PD002334; Gly_diox; 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 //