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Protein

Catechol-2,3-dioxygenase

Gene

catE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.1 Publication

Catalytic activityi

Catechol + O2 = 2-hydroxymuconate-6-semialdehyde.1 Publication

Cofactori

Fe2+By similarity

Kineticsi

    Vmax=1.04 µmol/min/mg enzyme (at pH 7 and at 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi213 – 2131IronBy similarity
    Metal bindingi264 – 2641IronBy similarity

    GO - Molecular functioni

    1. catechol 2,3-dioxygenase activity Source: UniProtKB-EC
    2. ferrous iron binding Source: InterPro

    GO - Biological processi

    1. aromatic compound catabolic process Source: UniProtKB-KW
    2. response to toxic substance Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism, Detoxification

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU08240-MONOMER.
    RETL1328306-WGS:GSTH-1235-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catechol-2,3-dioxygenase (EC:1.13.11.2)
    Alternative name(s):
    Catechol-induced ring cleavage extradiol dioxygenase
    Gene namesi
    Name:catE
    Synonyms:yfiE
    Ordered Locus Names:BSU08240
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570 Componenti: Chromosome

    Organism-specific databases

    GenoListiBSU08240. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 285285Catechol-2,3-dioxygenasePRO_0000049525Add
    BLAST

    Proteomic databases

    PaxDbiP54721.

    Expressioni

    Inductioni

    Strongly induced by catechol, less strongly by 2-methylhydroquinone (2-MHQ) but only weakly by chromanon (6-brom-2-vinyl-chroman-4-on).2 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU08240.

    Structurei

    3D structure databases

    ProteinModelPortaliP54721.
    SMRiP54721. Positions 6-137, 167-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2514.
    HOGENOMiHOG000250737.
    InParanoidiP54721.
    OMAiAMNVWNS.
    OrthoDBiEOG6VQPR2.
    PhylomeDBiP54721.

    Family and domain databases

    Gene3Di3.10.180.10. 2 hits.
    InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    IPR000486. Xdiol_ring_cleave_dOase_1/2.
    [Graphical view]
    PfamiPF00903. Glyoxalase. 2 hits.
    [Graphical view]
    SUPFAMiSSF54593. SSF54593. 2 hits.
    PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54721-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSIHEDTHI GYAKLTIRSL ERSLQFYCNV IGFQVLKKTD RQAELTADGK
    60 70 80 90 100
    RVLLILEENP SAVVLPERSV TGLYHFAILL PDRKELGIAL ARLIEHGIAI
    110 120 130 140 150
    GHGDHAVSEA LYLSDPDGNG IEMYADRPRS TWQRDREGNY VMTTTAVDIE
    160 170 180 190 200
    GLLEEAGDER KTSLPNDTII GHIHLHVSDL KEAKAFYTDV LGFDIVGNYA
    210 220 230 240 250
    GMSALFVSAG GYHHHIGLNI WAGRNAPPKP TNASGLDYYT VVLPHQEELD
    260 270 280
    LVANRVKHAG YSIEETENSF RVKDPVSGAY ITFVI
    Length:285
    Mass (Da):31,565
    Last modified:June 16, 2009 - v2
    Checksum:iCCDA3E510D89C9FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681R → L in BAA09109 (PubMed:8704981).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D50543 Genomic DNA. Translation: BAA09109.1.
    AL009126 Genomic DNA. Translation: CAB12653.2.
    PIRiH69802.
    RefSeqiNP_388705.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12653; CAB12653; BSU08240.
    GeneIDi936164.
    KEGGibsu:BSU08240.
    PATRICi18973298. VBIBacSub10457_0863.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D50543 Genomic DNA. Translation: BAA09109.1.
    AL009126 Genomic DNA. Translation: CAB12653.2.
    PIRiH69802.
    RefSeqiNP_388705.2. NC_000964.3.

    3D structure databases

    ProteinModelPortaliP54721.
    SMRiP54721. Positions 6-137, 167-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.BSU08240.

    Proteomic databases

    PaxDbiP54721.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB12653; CAB12653; BSU08240.
    GeneIDi936164.
    KEGGibsu:BSU08240.
    PATRICi18973298. VBIBacSub10457_0863.

    Organism-specific databases

    GenoListiBSU08240. [Micado]

    Phylogenomic databases

    eggNOGiCOG2514.
    HOGENOMiHOG000250737.
    InParanoidiP54721.
    OMAiAMNVWNS.
    OrthoDBiEOG6VQPR2.
    PhylomeDBiP54721.

    Enzyme and pathway databases

    BioCyciBSUB:BSU08240-MONOMER.
    RETL1328306-WGS:GSTH-1235-MONOMER.

    Family and domain databases

    Gene3Di3.10.180.10. 2 hits.
    InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    IPR000486. Xdiol_ring_cleave_dOase_1/2.
    [Graphical view]
    PfamiPF00903. Glyoxalase. 2 hits.
    [Graphical view]
    SUPFAMiSSF54593. SSF54593. 2 hits.
    PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Determination of a 12 kb nucleotide sequence around the 76 degrees region of the Bacillus subtilis chromosome."
      Yamamoto H., Uchiyama S., Fajar A.N., Ogasawara N., Sekiguchi J.
      Microbiology 142:1417-1421(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 68.
    4. "Differential gene expression in response to phenol and catechol reveals different metabolic activities for the degradation of aromatic compounds in Bacillus subtilis."
      Tam le T., Eymann C., Albrecht D., Sietmann R., Schauer F., Hecker M., Antelmann H.
      Environ. Microbiol. 8:1408-1427(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
      Strain: 168.
    5. "Transcriptome and proteome analyses in response to 2-methylhydroquinone and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems involved in the catabolism of aromatic compounds in Bacillus subtilis."
      Nguyen V.D., Wolf C., Maeder U., Lalk M., Langer P., Lindequist U., Hecker M., Antelmann H.
      Proteomics 7:1391-1408(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, NOMENCLATURE.
      Strain: 168.

    Entry informationi

    Entry nameiCADE_BACSU
    AccessioniPrimary (citable) accession number: P54721
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: June 16, 2009
    Last modified: January 7, 2015
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.