[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3170486 [NCBI, ExPASy, EBI, Israel, Japan] Neidle E.L., Hartnett C., Bonitz S., Ornston L.N.; "DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase I structural gene catA: evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions."; J. Bacteriol. 170:4874-4880(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan] Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.; "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."; Nucleic Acids Res. 32:5766-5779(2004).
[3]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). DOI=10.1016/S0969-2126(00)00122-2; PubMed=10801478 [NCBI, ExPASy, EBI, Israel, Japan] Vetting M.W., Ohlendorf D.H.; "The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker."; Structure 8:429-440(2000).

Comments

CATALYTIC ACTIVITY: Catechol + O₂ = cis,cis-muconate.
COFACTOR: Binds 1 Fe(3+) ion per subunit.
PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydrofuran-2-acetate from catechol: step 1/3 .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF009224; AAC46426.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR543861; CAG68305.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_046127.1; -.

3D structure databases

PDB

1DLM; X-ray; 2.00 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1DLQ; X-ray; 2.30 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1DLT; X-ray; 1.90 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1DMH; X-ray; 1.70 A; A/B=1-311.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DLM; -.
1DLQ; -.
1DLT; -.
1DMH; -.

ModBase

P07773.

Enzyme and pathway databases

BioCyc

ASP62977:ACIAD1442-MON; -.

Ontologies

GO:0018576;	Molecular function: catechol 1,2-dioxygenase activity (inferred from direct assay from UniProtKB).
GO:0008199;	Molecular function: ferric iron binding (inferred from direct assay from UniProtKB).
GO:0019614;	Biological process: catechol catabolic process (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR007535; Catechol_dOase_N.
IPR012801; Cchol_dOase_prob.
IPR000627; Intradiol_dOase_C.
IPR015889; Intradiol_dOase_core.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.130.10; Intradiol_dOase_core; 1.

Pfam

PF00775; Dioxygenase_C; 1.
PF04444; Dioxygenase_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02439; catechol_proteo; 1.

PROSITE

PS00083; INTRADIOL_DIOXYGENAS; 1.

Genome annotation databases

GeneID

2880527; -.

GenomeReviews

CR543861_GR; ACIAD1442.

KEGG

aci:ACIAD1442; -.

NMPDR

fig|62977.3.peg.799; -.

Phylogenomic databases

HOGENOM

P07773; -.

Genome annotation databases

CMR

P07773; ACIAD1442.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 311`	`311`	`Catechol 1,2-dioxygenase.`	`PRO_0000085078`
`METAL`	`164 164`		`Iron.`
`METAL`	`200 200`		`Iron.`
`METAL`	`224 224`		`Iron.`
`METAL`	`226 226`		`Iron.`
`HELIX`	`9 18`	`10`
`TURN`	`19 22`	`4`
`STRAND`	`24 26`	`3`
`HELIX`	`28 47`	`20`
`HELIX`	`52 67`	`16`
`HELIX`	`71 77`	`7`
`HELIX`	`80 94`	`15`
`STRAND`	`116 122`	`7`
`STRAND`	`133 141`	`9`
`STRAND`	`152 156`	`5`
`TURN`	`175 178`	`4`
`STRAND`	`179 183`	`5`
`STRAND`	`188 195`	`8`
`HELIX`	`207 214`	`8`
`STRAND`	`223 230`	`8`
`STRAND`	`237 243`	`7`
`TURN`	`247 250`	`4`
`STRAND`	`266 268`	`3`
`HELIX`	`271 276`	`6`
`STRAND`	`283 287`	`5`

Sequence information

Length: 311 AA [This is the length of the unprocessed precursor]

Molecular weight: 34347 Da [This is the MW of the unprocessed precursor]

CRC64: 8999FDD3F783B4DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEVKIFNTQD VQDFLRVASG LEQEGGNPRV KQIIHRVLSD LYKAIEDLNI TSDEYWAGVA 

        70         80         90        100        110        120 
YLNQLGANQE AGLLSPGLGF DHYLDMRMDA EDAALGIENA TPRTIEGPLY VAGAPESVGY 

       130        140        150        160        170        180 
ARMDDGSDPN GHTLILHGTI FDADGKPLPN AKVEIWHANT KGFYSHFDPT GEQQAFNMRR 

       190        200        210        220        230        240 
SIITDENGQY RVRTILPAGY GCPPEGPTQQ LLNQLGRHGN RPAHIHYFVS ADGHRKLTTQ 

       250        260        270        280        290        300 
INVAGDPYTY DDFAYATREG LVVDAVEHTD PEAIKANDVE GPFAEMVFDL KLTRLVDGVD 

       310 
NQVVDRPRLA V

P07773 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools