ID   PCXB_PSEPU              Reviewed;         239 AA.
AC   P00437;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 132.
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   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A;
RX   PubMed=8407791; DOI=10.1128/jb.175.19.6194-6202.1993;
RA   Frazee R.W., Livingston D.M., Laporte D.C., Lipscomb J.D.;
RT   "Cloning, sequencing, and expression of the Pseudomonas putida
RT   protocatechuate 3,4-dioxygenase genes.";
RL   J. Bacteriol. 175:6194-6202(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-239.
RX   PubMed=115853; DOI=10.1093/oxfordjournals.jbchem.a132612;
RA   Iwaki M., Kagamiyama H., Nozaki M.;
RT   "The complete amino acid sequence of the beta-subunit of protocatechuate
RT   3,4-dioxygenase from Pseudomonas aeruginosa.";
RL   J. Biochem. 86:1159-1162(1979).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=3194022; DOI=10.1038/336403a0;
RA   Ohlendorf D.H., Lipscomb J.D., Weber P.C.;
RT   "Structure and assembly of protocatechuate 3,4-dioxygenase.";
RL   Nature 336:403-405(1988).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RC   STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A;
RX   PubMed=7990141; DOI=10.1006/jmbi.1994.1754;
RA   Ohlendorf D.H., Orville A.M., Lipscomb J.D.;
RT   "Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa
RT   at 2.15-A resolution.";
RL   J. Mol. Biol. 244:586-608(1994).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RC   STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A;
RX   PubMed=9254599; DOI=10.1021/bi970468n;
RA   Orville A.M., Elango N., Lipscomb J.D., Ohlendorf D.H.;
RT   "Structures of competitive inhibitor complexes of protocatechuate 3,4-
RT   dioxygenase: multiple exogenous ligand binding orientations within the
RT   active site.";
RL   Biochemistry 36:10039-10051(1997).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
RC   STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A;
RX   PubMed=9254600; DOI=10.1021/bi970469f;
RA   Orville A.M., Lipscomb J.D., Ohlendorf D.H.;
RT   "Crystal structures of substrate and substrate analog complexes of
RT   protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in
RT   response to substrate binding.";
RL   Biochemistry 36:10052-10066(1997).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC   STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A;
RX   PubMed=9298971; DOI=10.1021/bi970691k;
RA   Elgren T.E., Orville A.M., Kelly K.A., Lipscomb J.D., Ohlendorf D.H.,
RA   Que L. Jr.;
RT   "Crystal structure and resonance Raman studies of protocatechuate 3,4-
RT   dioxygenase complexed with 3,4-dihydroxyphenylacetate.";
RL   Biochemistry 36:11504-11513(1997).
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   -!- CAUTION: Strain ATCC 23975 was originally classified as being from
CC       Pseudomonas aeruginosa. {ECO:0000305}.
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DR   EMBL; L14836; AAB41024.1; -; Genomic_DNA.
DR   PIR; A36930; DAPSBA.
DR   PDB; 1YKK; X-ray; 2.06 A; B/D/F/H/J/L=2-239.
DR   PDB; 1YKL; X-ray; 2.25 A; B/D/F/H/J/L=2-239.
DR   PDB; 1YKM; X-ray; 2.22 A; B/D/F/H/J/L=2-239.
DR   PDB; 1YKN; X-ray; 2.06 A; B/D/F/H/J/L=2-239.
DR   PDB; 1YKO; X-ray; 2.54 A; B/D/F/H/J/L=2-239.
DR   PDB; 1YKP; X-ray; 2.41 A; B/D/F/H/J/L=2-239.
DR   PDB; 2PCD; X-ray; 2.15 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3LKT; X-ray; 1.65 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3LMX; X-ray; 2.20 A; M/N/O=2-239.
DR   PDB; 3LXV; X-ray; 1.90 A; M/N/O=2-239.
DR   PDB; 3MFL; X-ray; 1.78 A; M/N/O=2-239.
DR   PDB; 3MI1; X-ray; 1.74 A; M/N/O=2-239.
DR   PDB; 3MI5; X-ray; 1.78 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3MV4; X-ray; 1.59 A; M/N/O=2-239.
DR   PDB; 3MV6; X-ray; 1.86 A; M/N/O=2-239.
DR   PDB; 3PCA; X-ray; 2.20 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCB; X-ray; 2.19 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCC; X-ray; 1.98 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCD; X-ray; 2.10 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCE; X-ray; 2.06 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCF; X-ray; 2.15 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCG; X-ray; 1.96 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCH; X-ray; 2.05 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCI; X-ray; 2.21 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCJ; X-ray; 2.13 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCK; X-ray; 2.13 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCL; X-ray; 2.15 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCM; X-ray; 2.25 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3PCN; X-ray; 2.40 A; M/N/O/P/Q/R=2-239.
DR   PDB; 3T63; X-ray; 1.54 A; M/N/O=2-239.
DR   PDB; 3T67; X-ray; 1.67 A; M/N/O=2-239.
DR   PDB; 4WHO; X-ray; 1.83 A; B/D/F=2-239.
DR   PDB; 4WHP; X-ray; 1.54 A; B/D/F=2-239.
DR   PDB; 4WHQ; X-ray; 1.78 A; B/D/F=2-239.
DR   PDB; 4WHR; X-ray; 1.58 A; B/D/F=2-239.
DR   PDB; 4WHS; X-ray; 1.35 A; B/D/F=2-239.
DR   PDBsum; 1YKK; -.
DR   PDBsum; 1YKL; -.
DR   PDBsum; 1YKM; -.
DR   PDBsum; 1YKN; -.
DR   PDBsum; 1YKO; -.
DR   PDBsum; 1YKP; -.
DR   PDBsum; 2PCD; -.
DR   PDBsum; 3LKT; -.
DR   PDBsum; 3LMX; -.
DR   PDBsum; 3LXV; -.
DR   PDBsum; 3MFL; -.
DR   PDBsum; 3MI1; -.
DR   PDBsum; 3MI5; -.
DR   PDBsum; 3MV4; -.
DR   PDBsum; 3MV6; -.
DR   PDBsum; 3PCA; -.
DR   PDBsum; 3PCB; -.
DR   PDBsum; 3PCC; -.
DR   PDBsum; 3PCD; -.
DR   PDBsum; 3PCE; -.
DR   PDBsum; 3PCF; -.
DR   PDBsum; 3PCG; -.
DR   PDBsum; 3PCH; -.
DR   PDBsum; 3PCI; -.
DR   PDBsum; 3PCJ; -.
DR   PDBsum; 3PCK; -.
DR   PDBsum; 3PCL; -.
DR   PDBsum; 3PCM; -.
DR   PDBsum; 3PCN; -.
DR   PDBsum; 3T63; -.
DR   PDBsum; 3T67; -.
DR   PDBsum; 4WHO; -.
DR   PDBsum; 4WHP; -.
DR   PDBsum; 4WHQ; -.
DR   PDBsum; 4WHR; -.
DR   PDBsum; 4WHS; -.
DR   AlphaFoldDB; P00437; -.
DR   SMR; P00437; -.
DR   IntAct; P00437; 1.
DR   DrugBank; DB01702; 2-(3,4-Dihydroxyphenyl)Acetic Acid.
DR   eggNOG; COG3485; Bacteria.
DR   BioCyc; MetaCyc:MONOMER-3185; -.
DR   UniPathway; UPA00157; UER00264.
DR   EvolutionaryTrace; P00437; -.
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   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW   Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:115853"
FT   CHAIN           2..239
FT                   /note="Protocatechuate 3,4-dioxygenase beta chain"
FT                   /id="PRO_0000085098"
FT   BINDING         109
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:7990141"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:7990141"
FT   BINDING         161
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:7990141"
FT   BINDING         163
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:7990141"
FT   CONFLICT        62
FT                   /note="H -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:4WHR"
FT   HELIX           44..47
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   TURN            64..68
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          78..87
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          136..143
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          175..181
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   HELIX           199..203
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:4WHS"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:4WHS"
SQ   SEQUENCE   239 AA;  26793 MW;  8F8CC293B6E434CE CRC64;
     MPAQDNSRFV IRDRNWHPKA LTPDYKTSIA RSPRQALVSI PQSISETTGP NFSHLGFGAH
     DHDLLLNFNN GGLPIGERII VAGRVVDQYG KPVPNTLVEM WQANAGGRYR HKNDRYLAPL
     DPNFGGVGRC LTDSDGYYSF RTIKPGPYPW RNGPNDWRPA HIHFGISGPS IATKLITQLY
     FEGDPLIPMC PIVKSIANPE AVQQLIAKLD MNNANPMDCL AYRFDIVLRG QRKTHFENC
//