(data stored in ACNUC15324 zone)

HOGENOM: ACIAD_1_PE1318

ID   ACIAD_1_PE1318                       STANDARD;      PRT;   311 AA.
AC   ACIAD_1_PE1318; P07773;
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=Catechol 1,2-dioxygenase; EC=1.13.11 1;AltName:
DE   Full=1,2-CTD; (ACIAD_1.PE1318).
GN   Name=catA; OrderedLocusNames=ACIAD1442;
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.PE1318.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:CATA_ACIAD
CC   -!- CATALYTIC ACTIVITY: Catechol + O(2) = cis,cis-muconate.
CC   -!- COFACTOR: Binds 1 Fe(3+) ion per subunit.
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       5-oxo-4,5-dihydro-2-furylacetate from catechol: step 1/3.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase
CC       family.
CC   -!- GENE_FAMILY: HOG000150199 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P07773; -.
DR   EMBL; AF009224; AAC46426.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68305.1; -; Genomic_DNA.
DR   RefSeq; YP_046127.1; NC_005966.1.
DR   PDB; 1DLM; X-ray; 2.00 A; A/B=1-311.
DR   PDB; 1DLQ; X-ray; 2.30 A; A/B=1-311.
DR   PDB; 1DLT; X-ray; 1.90 A; A/B=1-311.
DR   PDB; 1DMH; X-ray; 1.70 A; A/B=1-311.
DR   PDBsum; 1DLM; -.
DR   PDBsum; 1DLQ; -.
DR   PDBsum; 1DLT; -.
DR   PDBsum; 1DMH; -.
DR   ProteinModelPortal; P07773; -.
DR   SMR; P07773; 3-311.
DR   STRING; P07773; -.
DR   GeneID; 2880527; -.
DR   GenomeReviews; CR543861_GR; ACIAD1442.
DR   KEGG; aci:ACIAD1442; -.
DR   NMPDR; fig|62977.3.peg.799; -.
DR   eggNOG; COG3485; -.
DR   OMA; ALVECWH; -.
DR   ProtClustDB; CLSK867324; -.
DR   BioCyc; ASP62977:ACIAD1442-MON; -.
DR   GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019614; P:catechol catabolic process; IDA:UniProtKB.
DR   InterPro; IPR007535; Catechol_dOase_N.
DR   InterPro; IPR012801; Cchol_dOase_prob.
DR   InterPro; IPR000627; Intradiol_dOase_C.
DR   InterPro; IPR015889; Intradiol_dOase_core.
DR   Gene3D; G3DSA:2.60.130.10; Intradiol_dOase_core; 1.
DR   Pfam; PF00775; Dioxygenase_C; 1.
DR   Pfam; PF04444; Dioxygenase_N; 1.
DR   SUPFAM; SSF49482; Dioxygenase; 1.
DR   TIGRFAMs; TIGR02439; Catechol_proteo; 1.
DR   PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
DR   HOGENOMDNA; ACIAD_1.PE1318; -.
KW   3D-structure; Aromatic hydrocarbons catabolism; Complete proteome;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
SQ   SEQUENCE   311 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEVKIFNTQD VQDFLRVASG LEQEGGNPRV KQIIHRVLSD LYKAIEDLNI TSDEYWAGVA
     YLNQLGANQE AGLLSPGLGF DHYLDMRMDA EDAALGIENA TPRTIEGPLY VAGAPESVGY
     ARMDDGSDPN GHTLILHGTI FDADGKPLPN AKVEIWHANT KGFYSHFDPT GEQQAFNMRR
     SIITDENGQY RVRTILPAGY GCPPEGPTQQ LLNQLGRHGN RPAHIHYFVS ADGHRKLTTQ
     INVAGDPYTY DDFAYATREG LVVDAVEHTD PEAIKANDVE GPFAEMVFDL KLTRLVDGVD
     NQVVDRPRLA V
//

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