CATA2_ACILW
ID CATA2_ACILW Reviewed; 275 AA.
AC O33950;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Catechol 1,2-dioxygenase 2;
DE EC=1.13.11.1;
DE AltName: Full=1,2-CTD 2;
DE AltName: Full=CDI2;
GN Name=catA2;
OS Acinetobacter lwoffii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=28090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30; 27-65 AND
RP 229-247.
RC STRAIN=K24;
RX PubMed=9260969; DOI=10.1128/jb.179.16.5226-5231.1997;
RA Kim S.I., Leem S.-H., Choi J.-S., Chung Y.H., Kim S., Park Y.-M.,
RA Park Y.K., Lee Y.N., Ha K.-S.;
RT "Cloning and characterization of two catA genes in Acinetobacter lwoffii
RT K24.";
RL J. Bacteriol. 179:5226-5231(1997).
CC -!- FUNCTION: Can cleave 4-methyl-, 4-chloro-, and 3-methoxycatechol at
CC lower rates than catechol, but has no activity with 4-nitrocatechol or
CC protocatechuic acid.
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; 5-oxo-
CC 4,5-dihydro-2-furylacetate from catechol: step 1/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INDUCTION: By aniline.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77659; AAC31767.1; -; Genomic_DNA.
DR PIR; T46825; T46825.
DR AlphaFoldDB; O33950; -.
DR SMR; O33950; -.
DR UniPathway; UPA00157; UER00258.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0019614; P:catechol-containing compound catabolic process; IEA:InterPro.
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 Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..275
FT /note="Catechol 1,2-dioxygenase 2"
FT /id="PRO_0000085082"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 30399 MW; 3F8B0C127F45A807 CRC64;
MNKQAIDALL QKINDSAINE GNPRTKQIVN RIVRDLFYTI EDLDVQPDEF WTALNYLGDA
GRSGELGLLA AGLGFEHFLD LRMDEAEAKA GVEGGTPRTI EGPLYVAGAP VSDGHARLDD
GTDPGQTLVM RGRVFGEDGK PLANALVEVW HANHLGNYSY FDKSQPAFNL RRSIRTDAEG
KYSFRSVVPV GYSVPPQGQT QLLLDQLGRH GHRPAHIHFF VSAPGFRKLT TQINIDGDPY
LWDDFAFATR DGLVPAVRQA EVRKANRTAW TVSSR
