Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06622

- XYLE1_PSEPU

UniProt

P06622 - XYLE1_PSEPU

Protein

Metapyrocatechase

Gene

xylE

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Cofactori

    Fe2+ ion.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi153 – 1531Iron
    Metal bindingi214 – 2141Iron
    Metal bindingi265 – 2651Iron

    GO - Molecular functioni

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

    GO - Biological processi

    1. toluene catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3421.
    UniPathwayiUPA00273.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metapyrocatechase (EC:1.13.11.2)
    Short name:
    MPC
    Alternative name(s):
    CatO2ase
    Catechol 2,3-dioxygenase
    Gene namesi
    Name:xylE
    Encoded oniPlasmid TOL pWW00 Publication
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 307307MetapyrocatechasePRO_0000085027Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    307
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1613
    Helixi18 – 2710
    Beta strandi32 – 365
    Beta strandi42 – 454
    Beta strandi54 – 596
    Beta strandi64 – 7310
    Helixi75 – 8814
    Beta strandi93 – 953
    Beta strandi106 – 1105
    Beta strandi116 – 1216
    Beta strandi133 – 1353
    Beta strandi150 – 15910
    Helixi161 – 17010
    Beta strandi175 – 1817
    Beta strandi187 – 19812
    Beta strandi200 – 2056
    Beta strandi207 – 21812
    Helixi222 – 23514
    Beta strandi239 – 2457
    Beta strandi252 – 2576
    Beta strandi263 – 2686
    Beta strandi280 – 2834
    Helixi284 – 2863
    Helixi287 – 2915
    Turni293 – 2953
    Helixi300 – 3034

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MPYX-ray2.80A/B/C/D1-307[»]
    ProteinModelPortaliP06622.
    SMRiP06622. Positions 1-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06622.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.10.180.10. 2 hits.
    InterProiIPR017624. Catechol_2-3_dOase.
    IPR029068. 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. 1 hit.
    TIGRFAMsiTIGR03211. catechol_2_3. 1 hit.
    PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06622-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKGVMRPGH VQLRVLDMSK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV    50
    DKFSLVLREA DEPGMDFMGF KVVDEDALRQ LERDLMAYGC AVEQLPAGEL 100
    NSCGRRVRFQ APSGHHFELY ADKEYTGKWG LNDVNPEAWP RDLKGMAAVR 150
    FDHALMYGDE LPATYDLFTK VLGFYLAEQV LDENGTRVAQ FLSLSTKAHD 200
    VAFIHHPEKG RLHHVSFHLE TWEDLLRAAD LISMTDTSID IGPTRHGLTH 250
    GKTIYFFDPS GNRNEVFCGG DYNYPDHKPV TWTTDQLGKA IFYHDRILNE 300
    RFMTVLT 307
    Length:307
    Mass (Da):35,156
    Last modified:January 1, 1988 - v1
    Checksum:i80F189CF33554FAA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01161 Genomic DNA. Translation: CAA24490.1.
    M64747 Genomic DNA. Translation: AAA26052.1.
    PIRiA20852.
    RefSeqiNP_542866.1. NC_003350.1.
    WP_011005909.1. NC_003350.1.

    Genome annotation databases

    GeneIDi1218746.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01161 Genomic DNA. Translation: CAA24490.1 .
    M64747 Genomic DNA. Translation: AAA26052.1 .
    PIRi A20852.
    RefSeqi NP_542866.1. NC_003350.1.
    WP_011005909.1. NC_003350.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MPY X-ray 2.80 A/B/C/D 1-307 [» ]
    ProteinModelPortali P06622.
    SMRi P06622. Positions 1-307.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1218746.

    Enzyme and pathway databases

    UniPathwayi UPA00273 .
    BioCyci MetaCyc:MONOMER-3421.

    Miscellaneous databases

    EvolutionaryTracei P06622.

    Family and domain databases

    Gene3Di 3.10.180.10. 2 hits.
    InterProi IPR017624. Catechol_2-3_dOase.
    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. 1 hit.
    TIGRFAMsi TIGR03211. catechol_2_3. 1 hit.
    PROSITEi PS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonas putida mt-2."
      Nakai C., Kagamiyama H., Nozaki M., Nakzawa T., Inouye S., Ebina Y., Nakazawa A.
      J. Biol. Chem. 258:2923-2928(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2.
    2. "Chromogenic identification of genetic regulatory signals in Bacillus subtilis based on expression of a cloned Pseudomonas gene."
      Zukowski M.M., Gaffney D.F., Speck D., Kauffmann M., Findeli A., Wisecup A., Lecocq J.-P.
      Proc. Natl. Acad. Sci. U.S.A. 80:1101-1105(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Zukowski M.M.
      Submitted (MAY-1983) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily."
      Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S.
      Eur. J. Biochem. 204:113-120(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "DNA sequence determination of the TOL plasmid (pWWO) xylGFJ genes of Pseudomonas putida: implications for the evolution of aromatic catabolism."
      Horn J.M., Harayama S., Timmis K.N.
      Mol. Microbiol. 5:2459-2474(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-307.
    6. "An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2."
      Kita A., Kita S., Fujisawa I., Inaka K., Ishida T., Horiike K., Nozaki M., Miki K.
      Structure 7:25-34(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiXYLE1_PSEPU
    AccessioniPrimary (citable) accession number: P06622
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Plasmid

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3