ID   TFDC2_DELAC             Reviewed;          25 AA.
AC   P83116;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Chlorocatechol 1,2-dioxygenase 2;
DE            EC=1.13.11.-;
DE   AltName: Full=TfdCII;
DE   Flags: Fragment;
OS   Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=80866 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=MC1 {ECO:0000269|PubMed:12213933};
RX   PubMed=12213933; DOI=10.1099/00221287-148-9-2883;
RA   Benndorf D., Babel W.;
RT   "Assimilatory detoxification of herbicides by Delftia acidovorans MC1:
RT   induction of two chlorocatechol 1,2-dioxygenases as a response to
RT   chemostress.";
RL   Microbiology 148:2883-2888(2002).
RN   [2]
RP   INDUCTION BY 2,4-DCPP.
RC   STRAIN=MC1;
RX   PubMed=15073309; DOI=10.1099/mic.0.26774-0;
RA   Benndorf D., Davidson I., Babel W.;
RT   "Regulation of catabolic enzymes during long-term exposure of Delftia
RT   acidovorans MC1 to chlorophenoxy herbicides.";
RL   Microbiology 150:1005-1014(2004).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Xenobiotic degradation; 2-(2,4-dichlorophenoxy)propanoate
CC       degradation.
CC   -!- INDUCTION: By chemostress caused by the herbicide 2,4-
CC       dichlorophenoxypropionic acid (2,4-DCPP) and its metabolites.
CC       {ECO:0000269|PubMed:12213933, ECO:0000269|PubMed:15073309}.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83116; -.
DR   SMR; P83116; -.
DR   UniPathway; UPA00348; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW   Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..>25
FT                   /note="Chlorocatechol 1,2-dioxygenase 2"
FT                   /id="PRO_0000085093"
FT   NON_TER         25
FT                   /evidence="ECO:0000303|PubMed:12213933"
SQ   SEQUENCE   25 AA;  2872 MW;  E3FCC464EDCD71D6 CRC64;
     MKNPRVHEIA TAMIDAVRKV LVDHQ