(data stored in ACNUC15324 zone)

HOGENOM: ACIAD_1_PE1567

ID   ACIAD_1_PE1567                       STANDARD;      PRT;   209 AA.
AC   ACIAD_1_PE1567; P20371; Q43977; Q6FBK8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Protocatechuate 3,4-dioxygenase alpha chain; EC=1.13.11
DE   3;AltName: Full=3,4-PCD; (ACIAD_1.PE1567).
GN   Name=pcaG; OrderedLocusNames=ACIAD1712;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE1567.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PCXA_ACIAD
CC   -!- FUNCTION: Plays an essential role in the utilization of numerous
CC       aromatic and hydroaromatic compounds via the beta-ketoadipate
CC       pathway.
CC   -!- CATALYTIC ACTIVITY: 3,4-dihydroxybenzoate + O(2) = 3-carboxy-
CC       cis,cis-muconate.
CC   -!- COFACTOR: Binds Fe(3+) ion per subunit.
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       3-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
CC       beta chains.
CC   -!- INTERACTION:
CC       P20372:pcaH; NbExp=5; IntAct=EBI-1029428, EBI-1029420;
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase
CC       family.
CC   -!- GENE_FAMILY: HOG000174838 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P20371; Q43977; Q6FBK8; -.
DR   EMBL; L05770; AAC37154.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68554.1; -; Genomic_DNA.
DR   RefSeq; YP_046376.1; 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   ProteinModelPortal; P20371; -.
DR   SMR; P20371; 8-209.
DR   IntAct; P20371; 1.
DR   STRING; P20371; -.
DR   GeneID; 2879436; -.
DR   GenomeReviews; CR543861_GR; ACIAD1712.
DR   KEGG; aci:ACIAD1712; -.
DR   NMPDR; fig|62977.3.peg.1638; -.
DR   eggNOG; COG3485; -.
DR   OMA; RGINIHL; -.
DR   ProtClustDB; CLSK2307424; -.
DR   BioCyc; ASP62977:ACIAD1712-MON; -.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0018578; F:protocatechuate 3,4-dioxygenase activity; IEA:EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000627; Intradiol_dOase_C.
DR   InterPro; IPR015889; Intradiol_dOase_core.
DR   InterPro; IPR012786; Protocat_dOase_a.
DR   Gene3D; G3DSA:2.60.130.10; Intradiol_dOase_core; 1.
DR   Pfam; PF00775; Dioxygenase_C; 1.
DR   SUPFAM; SSF49482; Dioxygenase; 1.
DR   TIGRFAMs; TIGR02423; Protocat_alph; 1.
DR   PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
DR   HOGENOMDNA; ACIAD_1.PE1567; -.
KW   3D-structure; Aromatic hydrocarbons catabolism; Complete proteome;
KW   Dioxygenase; Direct protein sequencing; Iron; Oxidoreductase.
SQ   SEQUENCE   209 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNGWNFQELK ETPSQTGGPY VHIGLLPKQA NIEVFEHNLD NNLVQDNTQG QRIRLEGQVF
     DGLGLPLRDV LIEIWQADTN GVYPSQADTQ GKQVDPNFLG WGRTGADFGT GFWSFNTIKP
     GAVPGRKGST QAPHISLIIF ARGINIGLHT RVYFDDEAEA NAKDPVLNSI EWATRRQTLV
     AKREERDGEV VYRFDIRIQG ENETVFFDI
//

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