CADE_BACSU
ID CADE_BACSU Reviewed; 285 AA.
AC P54721;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Catechol-2,3-dioxygenase;
DE EC=1.13.11.2;
DE AltName: Full=Catechol-induced ring cleavage extradiol dioxygenase;
GN Name=catE; Synonyms=yfiE; OrderedLocusNames=BSU08240;
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=8704981; DOI=10.1099/13500872-142-6-1417;
RA Yamamoto H., Uchiyama S., Fajar A.N., Ogasawara N., Sekiguchi J.;
RT "Determination of a 12 kb nucleotide sequence around the 76 degrees region
RT of the Bacillus subtilis chromosome.";
RL Microbiology 142:1417-1421(1996).
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 SEQUENCE REVISION TO 68.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=168;
RX PubMed=16872404; DOI=10.1111/j.1462-2920.2006.01034.x;
RA Tam le T., Eymann C., Albrecht D., Sietmann R., Schauer F., Hecker M.,
RA Antelmann H.;
RT "Differential gene expression in response to phenol and catechol reveals
RT different metabolic activities for the degradation of aromatic compounds in
RT Bacillus subtilis.";
RL Environ. Microbiol. 8:1408-1427(2006).
RN [5]
RP INDUCTION, 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: Involved in the meta cleavage of catechol to 2-hydroxymuconic
CC semialdehyde. Essential for growth and viability in the presence of
CC catechol and probably involved in the detoxification of catechol.
CC {ECO:0000269|PubMed:16872404}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate +
CC H(+); Xref=Rhea:RHEA:17337, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:71198; EC=1.13.11.2;
CC Evidence={ECO:0000269|PubMed:16872404};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=1.04 umol/min/mg enzyme (at pH 7 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:16872404};
CC -!- INDUCTION: Strongly induced by catechol, less strongly by 2-
CC methylhydroquinone (2-MHQ) but only weakly by chromanon (6-brom-2-
CC vinyl-chroman-4-on). {ECO:0000269|PubMed:16872404,
CC ECO:0000269|PubMed:17407181}.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; D50543; BAA09109.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12653.2; -; Genomic_DNA.
DR PIR; H69802; H69802.
DR RefSeq; NP_388705.2; NC_000964.3.
DR RefSeq; WP_003233597.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P54721; -.
DR SMR; P54721; -.
DR STRING; 224308.BSU08240; -.
DR PaxDb; P54721; -.
DR EnsemblBacteria; CAB12653; CAB12653; BSU_08240.
DR GeneID; 936164; -.
DR KEGG; bsu:BSU08240; -.
DR PATRIC; fig|224308.179.peg.890; -.
DR eggNOG; COG2514; Bacteria.
DR InParanoid; P54721; -.
DR OMA; GGYHHHM; -.
DR PhylomeDB; P54721; -.
DR BioCyc; BSUB:BSU08240-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0018577; F:catechol 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
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 InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; SSF54593; 2.
DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Detoxification; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..285
FT /note="Catechol-2,3-dioxygenase"
FT /id="PRO_0000049525"
FT DOMAIN 9..126
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 169..285
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 68
FT /note="R -> L (in Ref. 1; BAA09109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31565 MW; CCDA3E510D89C9FC CRC64;
MTSIHEDTHI GYAKLTIRSL ERSLQFYCNV IGFQVLKKTD RQAELTADGK RVLLILEENP
SAVVLPERSV TGLYHFAILL PDRKELGIAL ARLIEHGIAI GHGDHAVSEA LYLSDPDGNG
IEMYADRPRS TWQRDREGNY VMTTTAVDIE GLLEEAGDER KTSLPNDTII GHIHLHVSDL
KEAKAFYTDV LGFDIVGNYA GMSALFVSAG GYHHHIGLNI WAGRNAPPKP TNASGLDYYT
VVLPHQEELD LVANRVKHAG YSIEETENSF RVKDPVSGAY ITFVI
