CLCA_RHOOP
ID CLCA_RHOOP Reviewed; 257 AA.
AC O67987;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Chlorocatechol 1,2-dioxygenase;
DE EC=1.13.11.-;
GN Name=clcA;
OS Rhodococcus opacus (Nocardia opaca).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=37919;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1CP;
RX PubMed=9495745; DOI=10.1128/jb.180.5.1082-1094.1998;
RA Eulberg D., Kourbatova E.M., Golovleva L.A., Schloemann M.;
RT "Evolutionary relationship between chlorocatechol catabolic enzymes from
RT Rhodococcus opacus 1CP and their counterparts in proteobacteria: sequence
RT divergence and functional convergence.";
RL J. Bacteriol. 180:1082-1094(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-chlorocatechol + O2 = 3-chloro-cis,cis-muconate + 2 H(+);
CC Xref=Rhea:RHEA:48576, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17589, ChEBI:CHEBI:27772;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,5-dichlorocatechol + O2 = (2E,4E)-2,4-dichloromuconate + 2
CC H(+); Xref=Rhea:RHEA:48572, ChEBI:CHEBI:11438, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15788;
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Note=Binds 1 Fe(3+) ion per subunit.;
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; AF003948; AAC38251.1; -; Genomic_DNA.
DR RefSeq; WP_065493674.1; NZ_CP009112.1.
DR PDB; 1S9A; X-ray; 2.47 A; A/B=1-257.
DR PDB; 3O32; X-ray; 2.85 A; A/B=1-257.
DR PDB; 3O5U; X-ray; 2.35 A; A/B=1-257.
DR PDB; 3O6J; X-ray; 2.90 A; A/B=1-257.
DR PDB; 3O6R; X-ray; 2.60 A; A/B=1-257.
DR PDBsum; 1S9A; -.
DR PDBsum; 3O32; -.
DR PDBsum; 3O5U; -.
DR PDBsum; 3O6J; -.
DR PDBsum; 3O6R; -.
DR AlphaFoldDB; O67987; -.
DR SMR; O67987; -.
DR DrugBank; DB03793; Benzoic acid.
DR DrugBank; DB04237; Tris(Hydroxyethyl)Aminomethane.
DR GeneID; 66790434; -.
DR BRENDA; 1.13.11.1; 4353.
DR EvolutionaryTrace; O67987; -.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:InterPro.
DR GO; GO:0018575; F:chlorocatechol 1,2-dioxygenase activity; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009712; P:catechol-containing compound metabolic process; IEA:InterPro.
DR CDD; cd03462; 1_2-CCD; 1.
DR Gene3D; 2.60.130.10; -; 1.
DR InterPro; IPR007535; Catechol_dOase_N.
DR InterPro; IPR012817; Chlorcchol_dOase.
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; TIGR02465; chlorocat_1_2; 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.
FT CHAIN 1..257
FT /note="Chlorocatechol 1,2-dioxygenase"
FT /id="PRO_0000085088"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT HELIX 4..24
FT /evidence="ECO:0007829|PDB:3O5U"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:3O5U"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3O5U"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3O6R"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3O6R"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3O5U"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:3O5U"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:3O5U"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:3O5U"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:3O5U"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:3O5U"
SQ SEQUENCE 257 AA; 28953 MW; D834A96E85A15777 CRC64;
MANTRVIELF DEFTDLIRDF IVRHEITTPE YETIMQYMIS VGEAGEWPLW LDAFFETTVD
SVSYGKGNWT SSAIQGPFFK EGAPLLTGKP ATLPMRADEP GDRMRFTGSV RDTSGTPITG
AVIDVWHSTN DGNYSFFSPA LPDQYLLRGR VVPAEDGSIE FHSIRPVPYE IPKAGPTGQL
MNSYLGRHSW RPAHIHIRIT ADGYRPLITQ LYFEGDPYLD SDSCSAVKSE LVLPVNKIDI
DGETWQLVDF NFILQHN
