PCXB_ACIAD
ID PCXB_ACIAD Reviewed; 241 AA.
AC P20372; Q43976;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protocatechuate 3,4-dioxygenase beta chain;
DE EC=1.13.11.3;
DE AltName: Full=3,4-PCD;
GN Name=pcaH; OrderedLocusNames=ACIAD1711;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX PubMed=2298704; DOI=10.1128/jb.172.2.956-966.1990;
RA Hartnett C., Neidle E.L., Ngai K.-L., Ornston L.N.;
RT "DNA sequences of genes encoding Acinetobacter calcoaceticus
RT protocatechuate 3,4-dioxygenase: evidence indicating shuffling of genes and
RT of DNA sequences within genes during their evolutionary divergence.";
RL J. Bacteriol. 172:956-966(1990).
RN [2]
RP SEQUENCE REVISION TO 12; 22; 36 AND 232-241.
RX PubMed=8063101; DOI=10.1016/0378-1119(94)90829-x;
RA Kowalchuk G.A., Hartnett G.B., Benson A., Houghton J.E., Ngai K.-L.,
RA Ornston L.N.;
RT "Contrasting patterns of evolutionary divergence within the Acinetobacter
RT calcoaceticus pca operon.";
RL Gene 146:23-30(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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 -!- INTERACTION:
CC P20372; P20371: pcaG; NbExp=5; IntAct=EBI-1029420, EBI-1029428;
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; L05770; AAC37153.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68553.1; -; Genomic_DNA.
DR PIR; C35119; C35119.
DR RefSeq; WP_004926639.1; NC_005966.1.
DR PDB; 1EO2; X-ray; 2.25 A; B=1-241.
DR PDB; 1EO9; X-ray; 2.00 A; B=1-241.
DR PDB; 1EOA; X-ray; 2.15 A; B=1-241.
DR PDB; 1EOB; X-ray; 2.20 A; B=1-241.
DR PDB; 1EOC; X-ray; 2.25 A; B=1-241.
DR PDB; 2BUM; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUQ; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUR; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUT; X-ray; 1.85 A; B=1-241.
DR PDB; 2BUU; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUV; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUW; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUX; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUY; X-ray; 1.80 A; B=1-241.
DR PDB; 2BUZ; X-ray; 1.80 A; B=1-241.
DR PDB; 2BV0; X-ray; 1.80 A; B=1-241.
DR PDBsum; 1EO2; -.
DR PDBsum; 1EO9; -.
DR PDBsum; 1EOA; -.
DR PDBsum; 1EOB; -.
DR PDBsum; 1EOC; -.
DR PDBsum; 2BUM; -.
DR PDBsum; 2BUQ; -.
DR PDBsum; 2BUR; -.
DR PDBsum; 2BUT; -.
DR PDBsum; 2BUU; -.
DR PDBsum; 2BUV; -.
DR PDBsum; 2BUW; -.
DR PDBsum; 2BUX; -.
DR PDBsum; 2BUY; -.
DR PDBsum; 2BUZ; -.
DR PDBsum; 2BV0; -.
DR AlphaFoldDB; P20372; -.
DR SMR; P20372; -.
DR IntAct; P20372; 1.
DR STRING; 62977.ACIAD1711; -.
DR PRIDE; P20372; -.
DR EnsemblBacteria; CAG68553; CAG68553; ACIAD1711.
DR GeneID; 45234098; -.
DR KEGG; aci:ACIAD1711; -.
DR eggNOG; COG3485; Bacteria.
DR HOGENOM; CLU_027719_5_0_6; -.
DR OMA; YRWDIVL; -.
DR OrthoDB; 1456634at2; -.
DR BioCyc; ASP62977:ACIAD_RS07885-MON; -.
DR UniPathway; UPA00157; UER00264.
DR EvolutionaryTrace; P20372; -.
DR PRO; PR:P20372; -.
DR Proteomes; UP000000430; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..241
FT /note="Protocatechuate 3,4-dioxygenase beta chain"
FT /id="PRO_0000085097"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 148
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"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2BUM"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:2BUM"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:2BUM"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2BUM"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2BUM"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:2BUM"
SQ SEQUENCE 241 AA; 27548 MW; 0D2F945C92FE675A CRC64;
MSQIIWGAYA QRNTEDHPPA YAPGYKTSVL RSPKNALISI AETLSEVTAP HFSADKFGPK
DNDLILNYAK DGLPIGERVI VHGYVRDQFG RPVKNALVEV WQANASGRYR HPNDQYIGAM
DPNFGGCGRM LTDDNGYYVF RTIKPGPYPW RNRINEWRPA HIHFSLIADG WAQRLISQFY
FEGDTLIDSC PILKTIPSEQ QRRALIALED KSNFIEADSR CYRFDITLRG RRATYFENDL
T
