(data stored in ACNUC15324 zone)

SWISSPROT: CATA_ACIAD

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   08-MAY-2019, entry version 135.
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 baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3170486; DOI=10.1128/jb.170.10.4874-4880.1988;
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].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
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   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:
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;
CC       5-oxo-4,5-dihydro-2-furylacetate from catechol: step 1/3.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase
CC       family. {ECO:0000305}.
DR   EMBL; AF009224; AAC46426.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68305.1; -; Genomic_DNA.
DR   RefSeq; WP_004925474.1; NC_005966.1.
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   SMR; P07773; -.
DR   STRING; 62977.ACIAD1442; -.
DR   EnsemblBacteria; CAG68305; CAG68305; ACIAD1442.
DR   KEGG; aci:ACIAD1442; -.
DR   eggNOG; ENOG410626B; Bacteria.
DR   eggNOG; COG3485; LUCA.
DR   HOGENOM; HOG000150199; -.
DR   KO; K03381; -.
DR   OMA; AHIHLIV; -.
DR   OrthoDB; 1456634at2; -.
DR   BioCyc; ASP62977:ACIAD_RS06660-MONOMER; -.
DR   BRENDA; 1.13.11.1; 107.
DR   UniPathway; UPA00157; UER00258.
DR   EvolutionaryTrace; P07773; -.
DR   Proteomes; UP000000430; Chromosome.
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:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019614; P:catechol-containing compound catabolic process; IDA: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   1: Evidence at protein level;
DR   PRODOM; P07773.
DR   SWISS-2DPAGE; P07773.
KW   3D-structure; Aromatic hydrocarbons catabolism; Complete proteome;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
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       {ECO:0000244|PDB:1DMH}.
FT   TURN         19     22       {ECO:0000244|PDB:1DMH}.
FT   STRAND       24     26       {ECO:0000244|PDB:1DMH}.
FT   HELIX        28     47       {ECO:0000244|PDB:1DMH}.
FT   HELIX        52     67       {ECO:0000244|PDB:1DMH}.
FT   HELIX        71     77       {ECO:0000244|PDB:1DMH}.
FT   HELIX        80     94       {ECO:0000244|PDB:1DMH}.
FT   STRAND      116    122       {ECO:0000244|PDB:1DMH}.
FT   STRAND      133    141       {ECO:0000244|PDB:1DMH}.
FT   STRAND      152    156       {ECO:0000244|PDB:1DMH}.
FT   STRAND      169    171       {ECO:0000244|PDB:1DLT}.
FT   TURN        175    178       {ECO:0000244|PDB:1DMH}.
FT   STRAND      179    183       {ECO:0000244|PDB:1DMH}.
FT   STRAND      188    195       {ECO:0000244|PDB:1DMH}.
FT   HELIX       207    214       {ECO:0000244|PDB:1DMH}.
FT   STRAND      223    230       {ECO:0000244|PDB:1DMH}.
FT   STRAND      237    243       {ECO:0000244|PDB:1DMH}.
FT   TURN        247    250       {ECO:0000244|PDB:1DMH}.
FT   STRAND      266    268       {ECO:0000244|PDB:1DMH}.
FT   HELIX       271    276       {ECO:0000244|PDB:1DMH}.
FT   STRAND      283    287       {ECO:0000244|PDB:1DMH}.
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
//

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