ID PCXA_ACIAD Reviewed; 209 AA. AC P20371; Q43977; Q6FBK8; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 3. DT 27-MAR-2024, entry version 162. DE RecName: Full=Protocatechuate 3,4-dioxygenase alpha chain; DE EC=1.13.11.3; DE AltName: Full=3,4-PCD; GN Name=pcaG; OrderedLocusNames=ACIAD1712; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadota; 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 40. 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 P20371; P20372: pcaH; NbExp=5; IntAct=EBI-1029428, EBI-1029420; 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; AAC37154.1; -; Genomic_DNA. DR EMBL; CR543861; CAG68554.1; -; Genomic_DNA. DR RefSeq; WP_004926643.1; NC_005966.1. DR PDB; 1EO2; X-ray; 2.25 A; A=1-209. DR PDB; 1EO9; X-ray; 2.00 A; A=1-209. DR PDB; 1EOA; X-ray; 2.15 A; A=1-209. DR PDB; 1EOB; X-ray; 2.20 A; A=1-209. DR PDB; 1EOC; X-ray; 2.25 A; A=1-209. DR PDB; 2BUM; X-ray; 1.80 A; A=1-209. DR PDB; 2BUQ; X-ray; 1.80 A; A=1-209. DR PDB; 2BUR; X-ray; 1.80 A; A=1-209. DR PDB; 2BUT; X-ray; 1.85 A; A=1-209. DR PDB; 2BUU; X-ray; 1.80 A; A=1-209. DR PDB; 2BUV; X-ray; 1.80 A; A=1-209. DR PDB; 2BUW; X-ray; 1.80 A; A=1-209. DR PDB; 2BUX; X-ray; 1.80 A; A=1-209. DR PDB; 2BUY; X-ray; 1.80 A; A=1-209. DR PDB; 2BUZ; X-ray; 1.80 A; A=1-209. DR PDB; 2BV0; X-ray; 1.80 A; A=1-209. 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; P20371; -. DR SMR; P20371; -. DR IntAct; P20371; 1. DR STRING; 202950.GCA_001485005_03090; -. DR GeneID; 45234099; -. DR KEGG; aci:ACIAD1712; -. DR eggNOG; COG3485; Bacteria. DR HOGENOM; CLU_027719_7_1_6; -. DR OrthoDB; 9805815at2; -. DR BioCyc; ASP62977:ACIAD_RS07890-MONOMER; -. DR UniPathway; UPA00157; UER00264. DR EvolutionaryTrace; P20371; -. DR PRO; PR:P20371; -. 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:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway. DR CDD; cd03463; 3_4-PCD_alpha; 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; IPR012786; Protocat_dOase_a. DR NCBIfam; TIGR02423; protocat_alph; 1. DR PANTHER; PTHR33711; DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED; 1. DR PANTHER; PTHR33711:SF9; PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN; 1. DR Pfam; PF00775; Dioxygenase_C; 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; Oxidoreductase; Reference proteome. FT CHAIN 1..209 FT /note="Protocatechuate 3,4-dioxygenase alpha chain" FT /id="PRO_0000085094" FT BINDING 142 FT /ligand="3,4-dihydroxybenzoate" FT /ligand_id="ChEBI:CHEBI:36241" FT /evidence="ECO:0000255" FT CONFLICT 64 FT /note="G -> S (in Ref. 1; AAC37154)" FT /evidence="ECO:0000305" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:2BUM" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:2BUM" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:2BUM" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:2BUM" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:2BUM" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:2BUM" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:2BUM" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:2BUX" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:2BUM" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:2BUM" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:2BUM" FT HELIX 158..161 FT /evidence="ECO:0007829|PDB:2BUM" FT HELIX 165..168 FT /evidence="ECO:0007829|PDB:2BUM" FT HELIX 173..176 FT /evidence="ECO:0007829|PDB:2BUM" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:2BUM" FT STRAND 180..186 FT /evidence="ECO:0007829|PDB:2BUM" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:2BUM" SQ SEQUENCE 209 AA; 23484 MW; 68FC09910CDB86EF CRC64; MNGWNFQELK ETPSQTGGPY VHIGLLPKQA NIEVFEHNLD NNLVQDNTQG QRIRLEGQVF DGLGLPLRDV LIEIWQADTN GVYPSQADTQ GKQVDPNFLG WGRTGADFGT GFWSFNTIKP GAVPGRKGST QAPHISLIIF ARGINIGLHT RVYFDDEAEA NAKDPVLNSI EWATRRQTLV AKREERDGEV VYRFDIRIQG ENETVFFDI //