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P0A396 (TFDC_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chlorocatechol 1,2-dioxygenase

EC=1.13.11.-
Gene names
Name:tfdC
Synonyms:tfdCI
Ordered Locus Names:Reut_D6466
Encoded onPlasmid pJP4 Ref.1 Ref.2 Ref.3 Ref.4
Plasmid pReut1 Ref.5
OrganismCupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Preferentially converts 3,5-dichlorocatechol as opposed to other chlorinated catechols. Retains diminished activity toward non-chlorinated substrates.

Catalytic activity

3,5-dichlorocatechol + O2 = 2,4-dichloro -muconate.

Cofactor

Binds 1 Fe3+ ion per subunit.

Pathway

Aromatic compound metabolism; 3-chlorocatechol degradation.

Sequence similarities

Belongs to the intradiol ring-cleavage dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 255255Chlorocatechol 1,2-dioxygenase
PRO_0000085090

Sites

Metal binding1301Iron By similarity
Metal binding1641Iron By similarity
Metal binding1881Iron By similarity
Metal binding1901Iron By similarity

Experimental info

Sequence conflict115 – 1162ED → DH Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0A396 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 5BCC1BC6A94B19B4

FASTA25528,283
        10         20         30         40         50         60 
MNKRVKDVVD AIVAAVQRVL DQKEVTEAEY RTAVHYLMQV AEQRETALLC DVFFNSTVAA 

        70         80         90        100        110        120 
TKARISEGST PAIEGPYYRD DAPLVDDRLK TYDTDDHKPL LIQGTVKAVD GSVVEDVTID 

       130        140        150        160        170        180 
VWHSTPDGKY SGFHDDIPTD FYRGKLRVGT DGSFRVRTTM PVPYQIPDQG PTGALLETMG 

       190        200        210        220        230        240 
GHSWRPAHVH FKVKAPGYET LTTQYYFEGG DWITDDCCNG VQSSLITPDI VEEGVRLMNI 

       250 
NFVIEPARAQ AGANP 

« Hide

References

« Hide 'large scale' references
[1]"Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4."
Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.
J. Bacteriol. 172:2351-2359(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Partial nucleotide sequence of the chlorocatechol degradative operon tfdCDEF of pJP4 and similarity to promoters of the chlorinated aromatic degradative operons tfdA and clcABD."
Perkins E.J., Bolton G., Gordon M.P., Lurquin P.F.
Nucleic Acids Res. 16:7200-7200(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide homology and organization of chlorocatechol oxidation genes of plasmids pJP4 and pAC27."
Ghosal D., You I.-S.
Mol. Gen. Genet. 211:113-120(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways."
Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T., Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.
Environ. Microbiol. 6:655-668(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequence of plasmid 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35097 Genomic DNA. Translation: AAA98262.1.
M36280 Genomic DNA. Translation: AAA98261.1.
AY365053 Genomic DNA. Translation: AAR31039.1.
CP000093 Genomic DNA. Translation: AAZ65764.1.
PIRA35255.
RefSeqYP_025387.1. NC_005912.1.
YP_293621.1. NC_007337.1.

3D structure databases

ProteinModelPortalP0A396.
ModBaseSearch...

Protein-protein interaction databases

STRING264198.Reut_D6466.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ65764; AAZ65764; Reut_D6466.
GeneID2847422.
3607312.
KEGGreu:Reut_D6466.
PATRIC20225308. VBIRalEut24049_0533.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3485.
HOGENOMHOG000150200.
KOK15247.
OMARVRTTMP.
ProtClustDBCLSK926386.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-6552-MONOMER.
MetaCyc:MONOMER-14417.
UniPathwayUPA00083.

Family and domain databases

Gene3D2.60.130.10. 1 hit.
InterProIPR007535. Catechol_dOase_N.
IPR012817. Chlorcchol_dOase.
IPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
[Graphical view]
PfamPF00775. Dioxygenase_C. 1 hit.
PF04444. Dioxygenase_N. 1 hit.
[Graphical view]
SUPFAMSSF49482. Dioxygenase. 1 hit.
TIGRFAMsTIGR02465. chlorocat_1_2. 1 hit.
PROSITEPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTFDC_CUPPJ
AccessionPrimary (citable) accession number: P0A396
Secondary accession number(s): P05403, P71131, Q46M66
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 56 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

SIMILARITY comments

Index of protein domains and families