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P06622 (XYLE1_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Metapyrocatechase
Short name=MPC
EC=1.13.11.2
Alternative name(s):
CatO2ase
Catechol 2,3-dioxygenase
Gene names
Name:xylE
Encoded onPlasmid TOL pWW0
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Catechol + O2 = 2-hydroxymuconate semialdehyde.

Cofactor

Fe2+ ion.

Pathway

Xenobiotic degradation; toluene degradation.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the extradiol ring-cleavage dioxygenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological_processtoluene catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functioncatechol 2,3-dioxygenase activity

Inferred from electronic annotation. Source: EC

ferrous iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307Metapyrocatechase
PRO_0000085027

Sites

Metal binding1531Iron
Metal binding2141Iron
Metal binding2651Iron

Secondary structure

1 ................................................... 307
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06622 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 80F189CF33554FAA

FASTA30735,156
        10         20         30         40         50         60 
MNKGVMRPGH VQLRVLDMSK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV DKFSLVLREA 

        70         80         90        100        110        120 
DEPGMDFMGF KVVDEDALRQ LERDLMAYGC AVEQLPAGEL NSCGRRVRFQ APSGHHFELY 

       130        140        150        160        170        180 
ADKEYTGKWG LNDVNPEAWP RDLKGMAAVR FDHALMYGDE LPATYDLFTK VLGFYLAEQV 

       190        200        210        220        230        240 
LDENGTRVAQ FLSLSTKAHD VAFIHHPEKG RLHHVSFHLE TWEDLLRAAD LISMTDTSID 

       250        260        270        280        290        300 
IGPTRHGLTH GKTIYFFDPS GNRNEVFCGG DYNYPDHKPV TWTTDQLGKA IFYHDRILNE 


RFMTVLT

« Hide

References

[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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		V01161 Genomic DNA. Translation: CAA24490.1.
M64747 Genomic DNA. Translation: AAA26052.1.
PIRA20852.
RefSeqNP_542866.1. NC_003350.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MPYX-ray2.80A/B/C/D1-307[»]
ProteinModelPortalP06622.
SMRP06622. Positions 1-307.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1218746.

Phylogenomic databases

ProtClustDBCLSK2754120.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3421.
UniPathwayUPA00273.

Family and domain databases

InterProIPR017624. Catechol_2-3_dOase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamPF00903. Glyoxalase. 2 hits.
[Graphical view]
TIGRFAMsTIGR03211. catechol_2_3. 1 hit.
PROSITEPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06622.

Entry information

Entry nameXYLE1_PSEPU
AccessionPrimary (citable) accession number: P06622
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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