PCXB_BURCE
ID PCXB_BURCE Reviewed; 235 AA.
AC P15110;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protocatechuate 3,4-dioxygenase beta chain;
DE EC=1.13.11.3;
DE AltName: Full=3,4-PCD;
GN Name=pcaH;
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2808303; DOI=10.1128/jb.171.11.5915-5921.1989;
RA Zylstra G.J., Olsen R.H., Ballou D.P.;
RT "Genetic organization and sequence of the Pseudomonas cepacia genes for the
RT alpha and beta subunits of protocatechuate 3,4-dioxygenase.";
RL J. Bacteriol. 171:5915-5921(1989).
CC -!- FUNCTION: Plays an essential role in the utilization of numerous
CC aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2
CC H(+); Xref=Rhea:RHEA:10084, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57496; EC=1.13.11.3;
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Note=Binds Fe(3+) ion per subunit.;
CC -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 3-
CC carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1.
CC -!- SUBUNIT: The enzyme is an oligomer of 12 copies of the alpha and beta
CC chains.
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; M30791; AAA25924.1; -; Genomic_DNA.
DR PIR; B33487; B33487.
DR AlphaFoldDB; P15110; -.
DR SMR; P15110; -.
DR STRING; 292.DM42_3792; -.
DR eggNOG; COG3485; Bacteria.
DR UniPathway; UPA00157; UER00264.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0018578; F:protocatechuate 3,4-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR CDD; cd03464; 3_4-PCD_beta; 1.
DR Gene3D; 2.60.130.10; -; 1.
DR InterPro; IPR000627; Intradiol_dOase_C.
DR InterPro; IPR015889; Intradiol_dOase_core.
DR InterPro; IPR024756; PCDO_beta_N.
DR InterPro; IPR012785; Protocat_dOase_b.
DR Pfam; PF00775; Dioxygenase_C; 1.
DR Pfam; PF12391; PCDO_beta_N; 1.
DR SUPFAM; SSF49482; SSF49482; 1.
DR TIGRFAMs; TIGR02422; protocat_beta; 1.
DR PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase.
FT CHAIN 1..235
FT /note="Protocatechuate 3,4-dioxygenase beta chain"
FT /id="PRO_0000085099"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 235 AA; 26550 MW; E8D00C95C8854324 CRC64;
MDSPTILTPR DWPSHPAYVH PDYRSSVKRG PTRPMIPLKE RLRDQYAPVY GAEDLGPLDH
DLTKNAVKNG EPLGERIVVT GRVLDEGGKP VRNTLVEVWQ ANAAGRYVHK VDQHDAPLDP
NFLGAGRCMT DAEGRYRFLT IKPGAYPWGN HPNAWRPNHI HFSLFGDYFG SRLVTQMYFP
GDPLLAYDPI FQGTPEAARD RLISRFSLDT TEEGHALGYE FDIVLRGRDA TPMER