ID   CATA_ACIGB              Reviewed;         305 AA.
AC   Q43984;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   05-MAY-2009, entry version 44.
DE   RecName: Full=Catechol 1,2-dioxygenase;
DE            EC=1.13.11.1;
GN   Name=catA;
OS   Acinetobacter genomosp. 11.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=106649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY PHENOL.
RC   STRAIN=ATCC 11171 / NCIB 8250 / CIP 63.46 / B94;
RX   MEDLINE=96154937; PubMed=8596453;
RX   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
RT   expression of genes encoding phenol hydroxylase and catechol 1,2-
RT   dioxygenase in Acinetobacter calcoacetious.";
RL   Mol. Microbiol. 18:13-20(1995).
RN   [2]
RP   INDUCTION BY PHENOL AND BENZOATE.
RX   MEDLINE=94266700; PubMed=8206826;
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: Catechol + O(2) = cis,cis-muconate.
CC   -!- COFACTOR: Binds 1 Fe(3+) ion per subunit (By similarity).
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       5-oxo-4,5-dihydrofuran-2-acetate from catechol: step 1/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- INDUCTION: By phenol and benzoate.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase
CC       family.
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DR   EMBL; Z36909; CAA85386.1; -; Genomic_DNA.
DR   PIR; S47293; S47293.
DR   HSSP; P07773; 1DMH.
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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019614; P:catechol catabolic process; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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   Gene3D; G3DSA:2.60.130.10; Intradiol_dOase_core; 1.
DR   Pfam; PF00775; Dioxygenase_C; 1.
DR   Pfam; PF04444; Dioxygenase_N; 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       Catechol 1,2-dioxygenase.
FT                                /FTId=PRO_0000085080.
FT   METAL       163    163       Iron.
FT   METAL       197    197       Iron.
FT   METAL       221    221       Iron.
FT   METAL       223    223       Iron.
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
//