CLCA_PSEPU
ID CLCA_PSEPU Reviewed; 260 AA.
AC P11451;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Chlorocatechol 1,2-dioxygenase;
DE EC=1.13.11.-;
GN Name=clcA;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pAC27.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3299368; DOI=10.1073/pnas.84.13.4460;
RA Frantz B., Chakrabarty A.M.;
RT "Organization and nucleotide sequence determination of a gene cluster
RT involved in 3-chlorocatechol degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4460-4464(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2830460; DOI=10.1007/bf00338401;
RA Ghosal D., You I.-S.;
RT "Nucleotide homology and organization of chlorocatechol oxidation genes of
RT plasmids pJP4 and pAC27.";
RL Mol. Gen. Genet. 211:113-120(1988).
CC -!- FUNCTION: Preferentially converts 3-chlorocatechol and 3,5-
CC dichlorocatechol as opposed to other chlorinated catechols. Retains
CC diminished activity toward non-chlorinated substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-chlorocatechol + O2 = (2E,4Z)-2-chloromuconate + 2 H(+);
CC Xref=Rhea:RHEA:48568, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:19504, ChEBI:CHEBI:27715;
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 -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; M16964; AAA98281.1; -; Genomic_DNA.
DR EMBL; M36279; AAA98294.1; -; Genomic_DNA.
DR PIR; A27058; A27058.
DR PDB; 3TH1; X-ray; 3.40 A; A/B/C=1-260.
DR PDBsum; 3TH1; -.
DR AlphaFoldDB; P11451; -.
DR SMR; P11451; -.
DR BioCyc; MetaCyc:MON-14416; -.
DR UniPathway; UPA00083; -.
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; Plasmid.
FT CHAIN 1..260
FT /note="Chlorocatechol 1,2-dioxygenase"
FT /id="PRO_0000085087"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 187
FT /note="A -> P (in Ref. 2; AAA98294)"
FT /evidence="ECO:0000305"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:3TH1"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:3TH1"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:3TH1"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3TH1"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3TH1"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3TH1"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3TH1"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:3TH1"
SQ SEQUENCE 260 AA; 28988 MW; 8D04AEC00E6B45AD CRC64;
MDKRVAEVAG AIVEAVRKIL LDKRVTEAEY RAGVDYLTEV AQTRETALLL DVFLNSTIIE
GKAQRSRTSA PAIQGPYFLE GAPVVEGVLK TYDTDDHKPL IIRGTVRSDT GELLAGAVID
VWHSTPDGLY SGIHDNIPVD YYRGKLVTDS QGNYRVRTTM PVPYQIPYEG PTGRLLGHLG
SHTWRPAHVH FKVRKDGFEP LTTQYYFEGG KWVDDDCCHG VTPDLITPET IEDGVRVMTL
DFVIEREQAE QRKSATETVA
