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 02-SEP-2026, entry version 171. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; 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}. 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; 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 AlphaFoldDB; P20372; -. DR MDposit; P20372; -. DR MDRepo; P20372; -. DR SMR; P20372; -. DR IntAct; P20372; 1. DR STRING; 202950.GCA_001485005_03089; -. DR GeneID; 45234098; -. DR KEGG; aci:ACIAD1711; -. DR eggNOG; COG3485; Bacteria. DR HOGENOM; CLU_027719_5_0_6; -. DR OrthoDB; 9805815at2; -. DR BioCyc; ASP62977:ACIAD_RS07885-MONOMER; -. 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; Aromatic compound dioxygenase; 1. DR InterPro; IPR000627; Intradiol_dOase_C. DR InterPro; IPR015889; Intradiol_dOase_core. DR InterPro; IPR050770; Intradiol_RC_Dioxygenase. 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. 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; -. 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 10..12 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 HELIX 144..147 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 //