ID   CATA_ACIAD              Reviewed;         311 AA.
AC   P07773;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   16-JUN-2009, entry version 75.
DE   RecName: Full=Catechol 1,2-dioxygenase;
DE            EC=1.13.11.1;
DE   AltName: Full=1,2-CTD;
GN   Name=catA; OrderedLocusNames=ACIAD1442;
OS   Acinetobacter sp. (strain ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89008110; PubMed=3170486;
RA   Neidle E.L., Hartnett C., Bonitz S., Ornston L.N.;
RT   "DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-
RT   dioxygenase I structural gene catA: evidence for evolutionary
RT   divergence of intradiol dioxygenases by acquisition of DNA sequence
RT   repetitions.";
RL   J. Bacteriol. 170:4874-4880(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=20264309; PubMed=10801478; DOI=10.1016/S0969-2126(00)00122-2;
RA   Vetting M.W., Ohlendorf D.H.;
RT   "The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a
RT   novel hydrophobic helical zipper as a subunit linker.";
RL   Structure 8:429-440(2000).
CC   -!- CATALYTIC ACTIVITY: Catechol + O(2) = cis,cis-muconate.
CC   -!- COFACTOR: Binds 1 Fe(3+) ion per subunit.
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       5-oxo-4,5-dihydrofuran-2-acetate from catechol: step 1/3.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase
CC       family.
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DR   EMBL; AF009224; AAC46426.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68305.1; -; Genomic_DNA.
DR   RefSeq; YP_046127.1; -.
DR   PDB; 1DLM; X-ray; 2.00 A; A/B=1-311.
DR   PDB; 1DLQ; X-ray; 2.30 A; A/B=1-311.
DR   PDB; 1DLT; X-ray; 1.90 A; A/B=1-311.
DR   PDB; 1DMH; X-ray; 1.70 A; A/B=1-311.
DR   PDBsum; 1DLM; -.
DR   PDBsum; 1DLQ; -.
DR   PDBsum; 1DLT; -.
DR   PDBsum; 1DMH; -.
DR   GeneID; 2880527; -.
DR   GenomeReviews; CR543861_GR; ACIAD1442.
DR   KEGG; aci:ACIAD1442; -.
DR   NMPDR; fig|62977.3.peg.799; -.
DR   HOGENOM; P07773; -.
DR   OMA; P07773; NKLGQDG.
DR   BioCyc; ASP62977:ACIAD1442-MON; -.
DR   GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019614; P:catechol catabolic process; IDA: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   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Complete proteome;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    311       Catechol 1,2-dioxygenase.
FT                                /FTId=PRO_0000085078.
FT   METAL       164    164       Iron.
FT   METAL       200    200       Iron.
FT   METAL       224    224       Iron.
FT   METAL       226    226       Iron.
FT   HELIX         9     18
FT   TURN         19     22
FT   STRAND       24     26
FT   HELIX        28     47
FT   HELIX        52     67
FT   HELIX        71     77
FT   HELIX        80     94
FT   STRAND      116    122
FT   STRAND      133    141
FT   STRAND      152    156
FT   TURN        175    178
FT   STRAND      179    183
FT   STRAND      188    195
FT   HELIX       207    214
FT   STRAND      223    230
FT   STRAND      237    243
FT   TURN        247    250
FT   STRAND      266    268
FT   HELIX       271    276
FT   STRAND      283    287
SQ   SEQUENCE   311 AA;  34347 MW;  8999FDD3F783B4DB CRC64;
     MEVKIFNTQD VQDFLRVASG LEQEGGNPRV KQIIHRVLSD LYKAIEDLNI TSDEYWAGVA
     YLNQLGANQE AGLLSPGLGF DHYLDMRMDA EDAALGIENA TPRTIEGPLY VAGAPESVGY
     ARMDDGSDPN GHTLILHGTI FDADGKPLPN AKVEIWHANT KGFYSHFDPT GEQQAFNMRR
     SIITDENGQY RVRTILPAGY GCPPEGPTQQ LLNQLGRHGN RPAHIHYFVS ADGHRKLTTQ
     INVAGDPYTY DDFAYATREG LVVDAVEHTD PEAIKANDVE GPFAEMVFDL KLTRLVDGVD
     NQVVDRPRLA V
//