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P54721

- CADE_BACSU

UniProt

P54721 - CADE_BACSU

Protein

Catechol-2,3-dioxygenase

Gene

catE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    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+ ion.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

      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: 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.
      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

      MTSIHEDTHI GYAKLTIRSL ERSLQFYCNV IGFQVLKKTD RQAELTADGK    50
      RVLLILEENP SAVVLPERSV TGLYHFAILL PDRKELGIAL ARLIEHGIAI 100
      GHGDHAVSEA LYLSDPDGNG IEMYADRPRS TWQRDREGNY VMTTTAVDIE 150
      GLLEEAGDER KTSLPNDTII GHIHLHVSDL KEAKAFYTDV LGFDIVGNYA 200
      GMSALFVSAG GYHHHIGLNI WAGRNAPPKP TNASGLDYYT VVLPHQEELD 250
      LVANRVKHAG YSIEETENSF RVKDPVSGAY ITFVI 285
      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:
      EMBL
      GenBank
      DDBJ
      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:
      EMBL
      GenBank
      DDBJ
      Links Updated
      D50543 Genomic DNA. Translation: BAA09109.1 .
      AL009126 Genomic DNA. Translation: CAB12653.2 .
      PIRi H69802.
      RefSeqi NP_388705.2. NC_000964.3.

      3D structure databases

      ProteinModelPortali P54721.
      SMRi P54721. Positions 6-137, 167-283.
      ModBasei Search...
      MobiDBi Search...

      Protein-protein interaction databases

      STRINGi 224308.BSU08240.

      Proteomic databases

      PaxDbi P54721.

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Genome annotation databases

      EnsemblBacteriai CAB12653 ; CAB12653 ; BSU08240 .
      GeneIDi 936164.
      KEGGi bsu:BSU08240.
      PATRICi 18973298. VBIBacSub10457_0863.

      Organism-specific databases

      GenoListi BSU08240. [Micado ]

      Phylogenomic databases

      eggNOGi COG2514.
      HOGENOMi HOG000250737.
      OrthoDBi EOG6VQPR2.
      PhylomeDBi P54721.

      Enzyme and pathway databases

      BioCyci BSUB:BSU08240-MONOMER.
      RETL1328306-WGS:GSTH-1235-MONOMER.

      Family and domain databases

      Gene3Di 3.10.180.10. 2 hits.
      InterProi IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
      IPR004360. Glyas_Fos-R_dOase_dom.
      IPR000486. Xdiol_ring_cleave_dOase_1/2.
      [Graphical view ]
      Pfami PF00903. Glyoxalase. 2 hits.
      [Graphical view ]
      SUPFAMi SSF54593. SSF54593. 2 hits.
      PROSITEi PS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
      [Graphical view ]
      ProtoNeti Search...

      Publicationsi

      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: October 1, 2014
      This is version 84 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