ID   CATA1_ACILW             Reviewed;         311 AA.
AC   O33948;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Catechol 1,2-dioxygenase 1;
DE            EC=1.13.11.1;
DE   AltName: Full=1,2-CTD 1;
DE   AltName: Full=CDI1;
GN   Name=catA1;
OS   Acinetobacter lwoffii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=28090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-36; 45-72 AND
RP   163-180.
RC   STRAIN=K24;
RX   PubMed=9260969; DOI=10.1128/jb.179.16.5226-5231.1997;
RA   Kim S.I., Leem S.-H., Choi J.-S., Chung Y.H., Kim S., Park Y.-M.,
RA   Park Y.K., Lee Y.N., Ha K.-S.;
RT   "Cloning and characterization of two catA genes in Acinetobacter lwoffii
RT   K24.";
RL   J. Bacteriol. 179:5226-5231(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RC   STRAIN=K24;
RX   PubMed=9473520; DOI=10.1006/bbrc.1997.7912;
RA   Kim S.I., Leem S.-H., Choi J.-S., Ha K.-S.;
RT   "Organization and transcriptional characterization of the cat1 gene cluster
RT   in Acinetobacter lwoffi K24.";
RL   Biochem. Biophys. Res. Commun. 243:289-294(1998).
CC   -!- FUNCTION: Can cleave 4-methyl-, 4-chloro-, and 3-methoxycatechol at
CC       lower rates than catechol, but has no activity with 4-nitrocatechol or
CC       protocatechuic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=catechol + O2 = cis,cis-muconate + 2 H(+);
CC         Xref=Rhea:RHEA:23852, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:18135, ChEBI:CHEBI:32379; EC=1.13.11.1;
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC       Note=Binds 1 Fe(3+) ion per subunit.;
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-
CC       4,5-dihydro-2-furylacetate from catechol: step 1/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- INDUCTION: By aniline.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; U77658; AAC46228.1; -; Genomic_DNA.
DR   PIR; JC5943; JC5943.
DR   AlphaFoldDB; O33948; -.
DR   SMR; O33948; -.
DR   UniPathway; UPA00157; UER00258.
DR   GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019614; P:catechol-containing compound catabolic process; IEA:InterPro.
DR   CDD; cd03460; 1_2-CTD; 1.
DR   Gene3D; 2.60.130.10; -; 1.
DR   InterPro; IPR007535; Catechol_dOase_N.
DR   InterPro; IPR012801; Cchol_dOase_prob.
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; TIGR02439; catechol_proteo; 1.
DR   PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW   Iron; Metal-binding; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9260969"
FT   CHAIN           2..311
FT                   /note="Catechol 1,2-dioxygenase 1"
FT                   /id="PRO_0000085081"
FT   BINDING         164
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  33378 MW;  BFA17B07716D41D3 CRC64;
     MSIKVFGTKE VQDLLKAATN LEGKGGNARS KQIVHRLLSD LFKAIDDLDI TPDEVWAGVN
     YLNKLGQDGE ATLLAAGSGL EKYLDIRLDA ADKAEGIEGG TPRTIEGPLY VAGATVHDGV
     SKIDINPDED AGPLVIHGTV TGPDGKPVAG AVVECWHANS KGFYSHFDPT GAQSDFNLRG
     AVKTGADGKY EFRTLMPVGY GCPPQGATQQ LLNVLGRHGN RPAHVHFFVS SDSARKLTTQ
     FNIEGDPLIW DDFAYATREE LIPPVTEKKG GTALGLKADT YKDIEFNLTL TSLVKGKDNQ
     VVHRLRAEVA A