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 03-AUG-2022, entry version 153.
DE RecName: Full=Catechol 1,2-dioxygenase {ECO:0000303|PubMed:3170486};
DE EC=1.13.11.1 {ECO:0000305|PubMed:10801478};
DE AltName: Full=1,2-CTD {ECO:0000303|PubMed:10801478};
GN Name=catA {ECO:0000303|PubMed:3170486}; OrderedLocusNames=ACIAD1442;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC 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-dioxygenase I
RT structural gene catA: evidence for evolutionary divergence of intradiol
RT dioxygenases by acquisition of DNA sequence 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., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3] {ECO:0007744|PDB:1DLM, ECO:0007744|PDB:1DLQ, ECO:0007744|PDB:1DLT, ECO:0007744|PDB:1DMH}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH IRON AND CATECHOL,
RP COFACTOR, SUBUNIT, AND DOMAIN.
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 novel
RT 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 Evidence={ECO:0000305|PubMed:10801478};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:10801478};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:10801478};
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:0000269|PubMed:10801478}.
CC -!- DOMAIN: Contains an helical zipper domain, consisting of five N-
CC terminal helices from each subunit, which forms the molecular dimer
CC axis. {ECO:0000269|PubMed:10801478}.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P07773; -.
DR SMR; P07773; -.
DR STRING; 62977.ACIAD1442; -.
DR DrugBank; DB02232; 1,2-Dihydroxybenzene.
DR DrugBank; DB04120; 4-Methyl-1,2-Benzenediol.
DR EnsemblBacteria; CAG68305; CAG68305; ACIAD1442.
DR GeneID; 45233854; -.
DR KEGG; aci:ACIAD1442; -.
DR eggNOG; COG3485; Bacteria.
DR HOGENOM; CLU_046727_0_0_6; -.
DR OMA; YHPTAYS; -.
DR OrthoDB; 1456634at2; -.
DR BioCyc; ASP62977:ACIAD_RS06660-MON; -.
DR BRENDA; 1.13.11.1; 95.
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;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..311
FT /note="Catechol 1,2-dioxygenase"
FT /id="PRO_0000085078"
FT BINDING 164
FT /ligand="catechol"
FT /ligand_id="ChEBI:CHEBI:18135"
FT /evidence="ECO:0000269|PubMed:10801478,
FT ECO:0007744|PDB:1DLT"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:10801478,
FT ECO:0007744|PDB:1DLM, ECO:0007744|PDB:1DLQ,
FT ECO:0007744|PDB:1DLT, ECO:0007744|PDB:1DMH"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:10801478,
FT ECO:0007744|PDB:1DLM, ECO:0007744|PDB:1DLQ"
FT BINDING 224..226
FT /ligand="catechol"
FT /ligand_id="ChEBI:CHEBI:18135"
FT /evidence="ECO:0000269|PubMed:10801478,
FT ECO:0007744|PDB:1DLT"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:10801478,
FT ECO:0007744|PDB:1DLM, ECO:0007744|PDB:1DLQ,
FT ECO:0007744|PDB:1DLT, ECO:0007744|PDB:1DMH"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:10801478,
FT ECO:0007744|PDB:1DLM, ECO:0007744|PDB:1DLQ,
FT ECO:0007744|PDB:1DLT, ECO:0007744|PDB:1DMH"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:1DMH"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1DMH"
FT HELIX 28..47
FT /evidence="ECO:0007829|PDB:1DMH"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:1DMH"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1DMH"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1DLT"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:1DMH"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:1DMH"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1DMH"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:1DMH"
FT STRAND 283..287
FT /evidence="ECO:0007829|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
