PCXA_PSEPU
ID PCXA_PSEPU Reviewed; 201 AA.
AC P00436;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protocatechuate 3,4-dioxygenase alpha chain;
DE EC=1.13.11.3;
DE AltName: Full=3,4-PCD;
GN Name=pcaG;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; 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 2-201.
RC STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A;
RX PubMed=465136; DOI=10.1016/s0021-9258(18)50320-3;
RA Kohlmiller N.A., Howard J.B.;
RT "The primary structure of the alpha subunit of protocatechuate 3,4-
RT dioxygenase. II. Isolation and sequence of overlap peptides and complete
RT sequence.";
RL J. Biol. Chem. 254:7309-7315(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; AAB41025.1; -; Genomic_DNA.
DR PIR; B36930; DAPSAA.
DR RefSeq; WP_003251601.1; NZ_WOWR01000009.1.
DR PDB; 1YKK; X-ray; 2.06 A; A/C/E/G/I/K=2-201.
DR PDB; 1YKL; X-ray; 2.25 A; A/C/E/G/I/K=2-201.
DR PDB; 1YKM; X-ray; 2.22 A; A/C/E/G/I/K=2-201.
DR PDB; 1YKN; X-ray; 2.06 A; A/C/E/G/I/K=2-201.
DR PDB; 1YKO; X-ray; 2.54 A; A/C/E/G/I/K=2-201.
DR PDB; 1YKP; X-ray; 2.41 A; A/C/E/G/I/K=2-201.
DR PDB; 2PCD; X-ray; 2.15 A; A/B/C/D/E/F=2-201.
DR PDB; 3LKT; X-ray; 1.65 A; A/B/C/D/E/F=2-201.
DR PDB; 3LMX; X-ray; 2.20 A; A/B/C=2-201.
DR PDB; 3LXV; X-ray; 1.90 A; A/B/C=2-201.
DR PDB; 3MFL; X-ray; 1.78 A; A/B/C=2-201.
DR PDB; 3MI1; X-ray; 1.74 A; A/B/C=2-201.
DR PDB; 3MI5; X-ray; 1.78 A; A/B/C/D/E/F=2-201.
DR PDB; 3MV4; X-ray; 1.59 A; A/B/C=2-201.
DR PDB; 3MV6; X-ray; 1.86 A; A/B/C=2-201.
DR PDB; 3PCA; X-ray; 2.20 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCB; X-ray; 2.19 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCC; X-ray; 1.98 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCD; X-ray; 2.10 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCE; X-ray; 2.06 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCF; X-ray; 2.15 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCG; X-ray; 1.96 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCH; X-ray; 2.05 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCI; X-ray; 2.21 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCJ; X-ray; 2.13 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCK; X-ray; 2.13 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCL; X-ray; 2.15 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCM; X-ray; 2.25 A; A/B/C/D/E/F=2-201.
DR PDB; 3PCN; X-ray; 2.40 A; A/B/C/D/E/F=2-201.
DR PDB; 3T63; X-ray; 1.54 A; A/B/C=2-201.
DR PDB; 3T67; X-ray; 1.67 A; A/B/C=2-201.
DR PDB; 4WHO; X-ray; 1.83 A; A/C/E=2-201.
DR PDB; 4WHP; X-ray; 1.54 A; A/C/E=2-201.
DR PDB; 4WHQ; X-ray; 1.78 A; A/C/E=2-201.
DR PDB; 4WHR; X-ray; 1.58 A; A/C/E=2-201.
DR PDB; 4WHS; X-ray; 1.35 A; A/C/E=2-201.
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; P00436; -.
DR SMR; P00436; -.
DR IntAct; P00436; 1.
DR STRING; 1240350.AMZE01000011_gene3681; -.
DR DrugBank; DB01702; 2-(3,4-Dihydroxyphenyl)Acetic Acid.
DR GeneID; 45522229; -.
DR eggNOG; COG3485; Bacteria.
DR BioCyc; MetaCyc:MON-3186; -.
DR UniPathway; UPA00157; UER00264.
DR EvolutionaryTrace; P00436; -.
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:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR CDD; cd03463; 3_4-PCD_alpha; 1.
DR Gene3D; 2.60.130.10; -; 1.
DR InterPro; IPR000627; Intradiol_dOase_C.
DR InterPro; IPR015889; Intradiol_dOase_core.
DR InterPro; IPR012786; Protocat_dOase_a.
DR Pfam; PF00775; Dioxygenase_C; 1.
DR SUPFAM; SSF49482; SSF49482; 1.
DR TIGRFAMs; TIGR02423; protocat_alph; 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; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:465136"
FT CHAIN 2..201
FT /note="Protocatechuate 3,4-dioxygenase alpha chain"
FT /id="PRO_0000085095"
FT BINDING 134
FT /ligand="3,4-dihydroxybenzoate"
FT /ligand_id="ChEBI:CHEBI:36241"
FT /evidence="ECO:0000255"
FT CONFLICT 60
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:4WHS"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4WHS"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:4WHS"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4WHS"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:4WHS"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4WHS"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4WHS"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:4WHS"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4WHS"
SQ SEQUENCE 201 AA; 22387 MW; BF95DB892076FBAF CRC64;
MPIELLPETP SQTAGPYVHI GLALEAAGNP TRDQEIWNRL AKPDAPGEHI LLLGQVYDGN
GHLVRDSFLE VWQADANGEY QDAYNLENAF NSFGRTATTF DAGEWTLHTV KPGVVNNAAG
VPMAPHINIS LFARGINIHL HTRLYFDDEA QANAKCPVLN LIEQPQRRET LIAKRCEVDG
KTAYRFDIRI QGEGETVFFD F
