CATA_ACIRA
ID CATA_ACIRA Reviewed; 20 AA.
AC P81422;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Catechol 1,2-dioxygenase;
DE EC=1.13.11.1;
DE AltName: Full=1,2-CTD;
DE Flags: Fragment;
OS Acinetobacter radioresistens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=40216;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=9369233; DOI=10.1016/s0014-5793(97)01167-8;
RA Briganti F., Pessione E., Giunta C., Scozzafava A.;
RT "Purification, biochemical properties and substrate specificity of a
RT catechol 1,2-dioxygenase from a phenol degrading Acinetobacter
RT radioresistens.";
RL FEBS Lett. 416:61-64(1997).
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 which dissociates into active monomeric subunits at
CC high ionic strengths.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P81422; -.
DR UniPathway; UPA00157; UER00258.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Iron; Oxidoreductase.
FT CHAIN 1..>20
FT /note="Catechol 1,2-dioxygenase"
FT /id="PRO_0000085083"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2279 MW; 70E8A5038F802327 CRC64;
TAANVKIFNT EEVQNFINLL