TCBC_PSESQ
ID TCBC_PSESQ Reviewed; 251 AA.
AC P27098;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Chlorocatechol 1,2-dioxygenase {ECO:0000303|PubMed:2013566};
DE EC=1.13.11.- {ECO:0000269|PubMed:2013566};
DE AltName: Full=Chlorocatechol 1,2-dioxygenase II {ECO:0000303|PubMed:2013566};
GN Name=tcbC {ECO:0000303|PubMed:2013566};
OS Pseudomonas sp. (strain P51).
OG Plasmid pP51.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=65067;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=P51; PLASMID=pP51;
RX PubMed=2013566; DOI=10.1128/jb.173.8.2425-2434.1991;
RA van der Meer J.R., Eggen R.I., Zehnder A.J., de Vos W.M.;
RT "Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster,
RT which encodes metabolism of chlorinated catechols: evidence for
RT specialization of catechol 1,2-dioxygenases for chlorinated substrates.";
RL J. Bacteriol. 173:2425-2434(1991).
CC -!- FUNCTION: Chlorocatechol 1,2-dioxygenase involved in the degradation of
CC chlorinated benzenes, that occurs via chlorocatechol intermediates.
CC Displays broad substrate specificity. Preferentially cleaves 3-
CC chlorocatechol and 3,4-dichlorocatechol, and shows lower activity on
CC 3,5-dichlorocatechol, 3,6-dichlorocatechol and 3,4,6-trichlorocatechol
CC in vitro. Is not able to convert 3,4,5-trichlorocatechol and 3,4,5,6-
CC tetrachlorocatechol. Thus, probably functions in the degradation
CC pathways of 1,2-dichlorobenzene, 1,4-dichlorobenzene and 1,2,4-
CC trichlorobenzene (via 3,4-dichlorocatechol, 3,6-dichlorocatechol and
CC 3,4,6-trichlorocatechol intermediates, respectively), which allow
CC Pseudomonas sp. strain P51 to grow on these substrates as the sole
CC carbon and energy source. {ECO:0000269|PubMed:2013566}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-chlorocatechol + O2 = (2E,4Z)-2-chloromuconate + 2 H(+);
CC Xref=Rhea:RHEA:48568, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:19504, ChEBI:CHEBI:27715;
CC Evidence={ECO:0000269|PubMed:2013566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dichlorocatechol + O2 = (2Z,4Z)-2,3-dichloromuconate + 2
CC H(+); Xref=Rhea:RHEA:48980, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:90882, ChEBI:CHEBI:91011;
CC Evidence={ECO:0000269|PubMed:2013566};
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 Evidence={ECO:0000269|PubMed:2013566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,6-dichlorocatechol + O2 = (2E,4E)-2,5-dichloromuconate +
CC H(+); Xref=Rhea:RHEA:35055, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:19375, ChEBI:CHEBI:77767;
CC Evidence={ECO:0000269|PubMed:2013566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4,6-trichlorocatechol + O2 = (2Z,4E)-2,3,5-trichloromuconate
CC + H(+); Xref=Rhea:RHEA:51880, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:19298, ChEBI:CHEBI:134391;
CC Evidence={ECO:0000269|PubMed:2013566};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:Q5PXQ6};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250|UniProtKB:Q5PXQ6};
CC -!- PATHWAY: Xenobiotic degradation. {ECO:0000305|PubMed:2013566}.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; M57629; AAD13625.1; -; Genomic_DNA.
DR PIR; A43673; A43673.
DR AlphaFoldDB; P27098; -.
DR SMR; P27098; -.
DR PRIDE; P27098; -.
DR KEGG; ag:AAD13625; -.
DR BioCyc; MetaCyc:MON-14402; -.
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 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..251
FT /note="Chlorocatechol 1,2-dioxygenase"
FT /id="PRO_0000085089"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT BINDING 188
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
SQ SEQUENCE 251 AA; 27554 MW; 8867F76282D7C6D7 CRC64;
MNERVKQVAS ALVDAIQKTL TEQRVTEEEW RAGVGYMMKL AEAKEVAVLL DAFFNHTIVD
LKAQATRGSR PAMQGPYFLE GAPVVAGALK TYEDDSHHPL VIRGAVRTDD GAPAAGAVID
VWHSTPDGKY SGIHDQIPTD MYRGKVVADA QGKYAVRTTM PAPYQIPNKG PTGVLLEMMG
SHTWRPAHVH FKVRKDGFAP LTTQYYFEGG DWVDSDCCKG VAPDLVMPTK TEGGAQVMDI
DFVIERAREH V
