ID   CATA_ACIGI              Reviewed;         305 AA.
AC   Q43984;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Catechol 1,2-dioxygenase;
DE            EC=1.13.11.1;
GN   Name=catA;
OS   Acinetobacter guillouiae (Acinetobacter genomosp. 11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=106649;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY PHENOL.
RC   STRAIN=ATCC 11171 / DSM 590 / CCUG 2491 / LMG 988 / NCIMB 8250 / CIP 63.46
RC   / B94;
RX   PubMed=8596453; DOI=10.1111/j.1365-2958.1995.mmi_18010013.x;
RA   Ehrt S., Schirmer F., Hillen W.;
RT   "Genetic organization, nucleotide sequence and regulation of expression of
RT   genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in
RT   Acinetobacter calcoacetious.";
RL   Mol. Microbiol. 18:13-20(1995).
RN   [2] {ECO:0000305}
RP   INDUCTION BY PHENOL AND BENZOATE.
RX   PubMed=8206826; DOI=10.1128/jb.176.12.3493-3499.1994;
RA   Ehrt S., Ornston L.N., Hillen W.;
RT   "RpoN (sigma 54) is required for conversion of phenol to catechol in
RT   Acinetobacter calcoaceticus.";
RL   J. Bacteriol. 176:3493-3499(1994).
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         Evidence={ECO:0000250|UniProtKB:P07773};
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: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-
CC       4,5-dihydro-2-furylacetate from catechol: step 1/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07773}.
CC   -!- INDUCTION: By phenol and benzoate. {ECO:0000269|PubMed:8206826,
CC       ECO:0000269|PubMed:8596453}.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; Z36909; CAA85386.1; -; Genomic_DNA.
DR   PIR; S47293; S47293.
DR   AlphaFoldDB; Q43984; -.
DR   SMR; Q43984; -.
DR   STRING; 106649.GCA_000829655_03935; -.
DR   UniPathway; UPA00157; UER00258.
DR   GO; GO:0018576; F:catechol 1,2-dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR   GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019614; P:catechol-containing compound catabolic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..305
FT                   /note="Catechol 1,2-dioxygenase"
FT                   /id="PRO_0000085080"
FT   BINDING         163
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         221
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         223
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
SQ   SEQUENCE   305 AA;  33609 MW;  E65143DFA0572937 CRC64;
     MMMNRQQIDS LVQQMNVATA TGEVNLRVQQ IVVRLLGDLF QAIEDLNMSQ TELWKGLEYL
     TDAGQANELG LLAAGLGLEH YLDLRADEAD AKAGITGGTP RTIEGPLYVA GAPESVGFAR
     MDDGSESAHV DALIIEGNVT DTAGQIIPNA KVEIWHANSL GNYSFFDKSQ SAFNLRRSIF
     TDTQGQYIAQ TTMPVGYGCP PEGTTQALLN LLGRHGNRPS HVHYFVSAPG YRKLTTQFNI
     EGDKYLWDDF AFATRDGLIA TALDVTDLAK IKQYNLNKAF KHIKFNFQLV QDADQVPLQR
     LIVVE