CATA_RHOOP
ID CATA_RHOOP Reviewed; 270 AA.
AC P95607;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Catechol 1,2-dioxygenase;
DE EC=1.13.11.1;
DE AltName: Full=1,2-CTD;
DE Flags: Fragment;
GN Name=catA;
OS Rhodococcus opacus (Nocardia opaca).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=37919;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 113-132 AND
RP 195-203.
RC STRAIN=1CP;
RX PubMed=8990288; DOI=10.1128/jb.179.2.370-381.1997;
RA Eulberg D., Golovleva L.A., Schloemann M.;
RT "Characterization of catechol catabolic genes from Rhodococcus erythropolis
RT 1CP.";
RL J. Bacteriol. 179:370-381(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 -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; X99622; CAA67941.1; -; Genomic_DNA.
DR PDB; 3HGI; X-ray; 1.94 A; A=1-270.
DR PDB; 3HHX; X-ray; 2.00 A; A=1-270.
DR PDB; 3HHY; X-ray; 1.55 A; A=1-270.
DR PDB; 3HJ8; X-ray; 2.40 A; A=1-270.
DR PDB; 3HJQ; X-ray; 2.00 A; A=1-270.
DR PDB; 3HJS; X-ray; 1.80 A; A=1-270.
DR PDB; 3HKP; X-ray; 1.85 A; A=1-270.
DR PDB; 3I4V; X-ray; 2.00 A; A=1-270.
DR PDB; 3I4Y; X-ray; 1.85 A; A=1-270.
DR PDB; 3I51; X-ray; 1.80 A; A=1-270.
DR PDBsum; 3HGI; -.
DR PDBsum; 3HHX; -.
DR PDBsum; 3HHY; -.
DR PDBsum; 3HJ8; -.
DR PDBsum; 3HJQ; -.
DR PDBsum; 3HJS; -.
DR PDBsum; 3HKP; -.
DR PDBsum; 3I4V; -.
DR PDBsum; 3I4Y; -.
DR PDBsum; 3I51; -.
DR AlphaFoldDB; P95607; -.
DR SMR; P95607; -.
DR STRING; 37919.EP51_30985; -.
DR eggNOG; COG3485; Bacteria.
DR BRENDA; 1.13.11.1; 4353.
DR EvolutionaryTrace; P95607; -.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
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 Gene3D; 6.10.10.40; -; 1.
DR InterPro; IPR043029; 1_2-CTD_multi_dom.
DR InterPro; IPR007535; Catechol_dOase_N.
DR InterPro; IPR012800; Cchol_dOase_actb.
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; TIGR02438; catachol_actin; 1.
DR PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT CHAIN <1..270
FT /note="Catechol 1,2-dioxygenase"
FT /id="PRO_0000085084"
FT BINDING 152
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT HELIX 21..42
FT /evidence="ECO:0007829|PDB:3HHY"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:3HHY"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:3HHY"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3HHY"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3I4Y"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3HHY"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3HHY"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:3HHY"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:3HHY"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3HHY"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3HJS"
SQ SEQUENCE 270 AA; 29704 MW; BCD5BE5B8365115A CRC64;
GSGSAATDKF KAERATADTS PERLAAIAKD ALGALNDVIL KHGVTYPEYR VFKQWLIDVG
EGGEWPLFLD VFIEHSVEEV LARSRKGTMG SIEGPYYIEN SPELPSKCTL PMREEDEKIT
PLVFSGQVTD LDGNGLAGAK VELWHADNDG YYSQFAPHLP EWNLRGTIIA DEEGRYEITT
IQPAPYQIPT DGPTGQFIEA QNGHPWRPAH LHLIVSAPGK ESVTTQLYFK GGEWIDSDVA
SATKPELILD PKTGDDGKNY VTYNFVLDPA
