PCXA_ACIAD
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 03-AUG-2022, entry version 156.
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; 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 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}.
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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; 62977.ACIAD1712; -.
DR EnsemblBacteria; CAG68554; CAG68554; ACIAD1712.
DR GeneID; 45234099; -.
DR KEGG; aci:ACIAD1712; -.
DR eggNOG; COG3485; Bacteria.
DR HOGENOM; CLU_027719_7_1_6; -.
DR OMA; YRFDIHL; -.
DR OrthoDB; 1456634at2; -.
DR BioCyc; ASP62977:ACIAD_RS07890-MON; -.
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; -; 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; 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
