TFDC_CUPPJ
ID TFDC_CUPPJ Reviewed; 255 AA.
AC P0A396; P05403; P71131; Q46M66;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chlorocatechol 1,2-dioxygenase;
DE EC=1.13.11.-;
GN Name=tfdC; Synonyms=tfdCI; OrderedLocusNames=Reut_D6466;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OG Plasmid pJP4, and Plasmid pPJ4.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pJP4;
RX PubMed=2185214; DOI=10.1128/jb.172.5.2351-2359.1990;
RA Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.;
RT "Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase
RT and dichlorocatechol oxidative operons of plasmid pJP4.";
RL J. Bacteriol. 172:2351-2359(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pJP4;
RX PubMed=3405772; DOI=10.1093/nar/16.14.7200;
RA Perkins E.J., Bolton G., Gordon M.P., Lurquin P.F.;
RT "Partial nucleotide sequence of the chlorocatechol degradative operon
RT tfdCDEF of pJP4 and similarity to promoters of the chlorinated aromatic
RT degradative operons tfdA and clcABD.";
RL Nucleic Acids Res. 16:7200-7200(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pJP4;
RX PubMed=2830460; DOI=10.1007/bf00338401;
RA Ghosal D., You I.-S.;
RT "Nucleotide homology and organization of chlorocatechol oxidation genes of
RT plasmids pJP4 and pAC27.";
RL Mol. Gen. Genet. 211:113-120(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pJP4;
RX PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT and evolution of specialized chloroaromatic degradation pathways.";
RL Environ. Microbiol. 6:655-668(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
CC -!- FUNCTION: Preferentially converts 3,5-dichlorocatechol as opposed to
CC other chlorinated catechols. Retains diminished activity toward non-
CC chlorinated substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,5-dichlorocatechol + O2 = (2E,4E)-2,4-dichloromuconate + 2
CC H(+); Xref=Rhea:RHEA:48572, ChEBI:CHEBI:11438, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15788;
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Note=Binds 1 Fe(3+) ion per subunit.;
CC -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; M35097; AAA98262.1; -; Genomic_DNA.
DR EMBL; M36280; AAA98261.1; -; Genomic_DNA.
DR EMBL; AY365053; AAR31039.1; -; Genomic_DNA.
DR EMBL; CP000093; AAZ65764.1; -; Genomic_DNA.
DR PIR; A35255; A35255.
DR RefSeq; WP_011178386.1; NZ_AY365053.1.
DR AlphaFoldDB; P0A396; -.
DR SMR; P0A396; -.
DR EnsemblBacteria; AAZ65764; AAZ65764; Reut_D6466.
DR GeneID; 55536834; -.
DR KEGG; reu:Reut_D6466; -.
DR HOGENOM; CLU_046727_1_0_4; -.
DR OMA; QRAPHIH; -.
DR OrthoDB; 1456634at2; -.
DR BioCyc; MetaCyc:MON-14417; -.
DR UniPathway; UPA00083; -.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:InterPro.
DR GO; GO:0018575; F:chlorocatechol 1,2-dioxygenase activity; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009712; P:catechol-containing compound metabolic process; IEA:InterPro.
DR CDD; cd03462; 1_2-CCD; 1.
DR Gene3D; 2.60.130.10; -; 1.
DR InterPro; IPR007535; Catechol_dOase_N.
DR InterPro; IPR012817; Chlorcchol_dOase.
DR InterPro; IPR000627; Intradiol_dOase_C.
DR InterPro; IPR015889; Intradiol_dOase_core.
DR Pfam; PF00775; Dioxygenase_C; 1.
DR Pfam; PF04444; Dioxygenase_N; 1.
DR SUPFAM; SSF49482; SSF49482; 1.
DR TIGRFAMs; TIGR02465; chlorocat_1_2; 1.
DR PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..255
FT /note="Chlorocatechol 1,2-dioxygenase"
FT /id="PRO_0000085090"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 115..116
FT /note="ED -> DH (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28283 MW; 5BCC1BC6A94B19B4 CRC64;
MNKRVKDVVD AIVAAVQRVL DQKEVTEAEY RTAVHYLMQV AEQRETALLC DVFFNSTVAA
TKARISEGST PAIEGPYYRD DAPLVDDRLK TYDTDDHKPL LIQGTVKAVD GSVVEDVTID
VWHSTPDGKY SGFHDDIPTD FYRGKLRVGT DGSFRVRTTM PVPYQIPDQG PTGALLETMG
GHSWRPAHVH FKVKAPGYET LTTQYYFEGG DWITDDCCNG VQSSLITPDI VEEGVRLMNI
NFVIEPARAQ AGANP
