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   27-MAR-2024, entry version 95.
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; Pseudomonadota; 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}.
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DR   EMBL; M30791; AAA25924.1; -; Genomic_DNA.
DR   PIR; B33487; B33487.
DR   AlphaFoldDB; P15110; -.
DR   SMR; P15110; -.
DR   STRING; 292.WI67_23120; -.
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; Aromatic compound dioxygenase; 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   NCBIfam; TIGR02422; protocat_beta; 1.
DR   PANTHER; PTHR33711; DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED; 1.
DR   PANTHER; PTHR33711:SF10; INTRADIOL RING-CLEAVAGE DIOXYGENASES DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00775; Dioxygenase_C; 1.
DR   Pfam; PF12391; PCDO_beta_N; 1.
DR   SUPFAM; SSF49482; Aromatic compound dioxygenase; 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
//