[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-36; 45-72 AND 163-180. STRAIN=K24; PubMed=9260969 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.I., Leem S.-H., Choi J.-S., Chung Y.H., Kim S., Park Y.-M., Park Y.K., Lee Y.N., Ha K.-S.; "Cloning and characterization of two catA genes in Acinetobacter lwoffii K24."; J. Bacteriol. 179:5226-5231(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. STRAIN=K24; DOI=10.1006/bbrc.1997.7912; PubMed=9473520 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.I., Leem S.-H., Choi J.-S., Ha K.-S.; "Organization and transcriptional characterization of the cat1 gene cluster in Acinetobacter lwoffi K24."; Biochem. Biophys. Res. Commun. 243:289-294(1998).

Comments

FUNCTION: Can cleave 4-methyl-, 4-chloro-, and 3-methoxycatechol at lower rates than catechol, but has no activity with 4-nitrocatechol or protocatechuic acid.
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 (Potential).
INDUCTION: By aniline.
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

U77658; AAC46228.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC5943; JC5943.

3D structure databases

HSSP

P07773; 1DMH. [HSSP ENTRY / PDB]

ModBase

O33948.

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.

Other

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

Keywords

Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 311`	`310`	`Catechol 1,2-dioxygenase 1.`	`PRO_0000085081`
`METAL`	`164 164`		`Iron (By similarity).`
`METAL`	`200 200`		`Iron (By similarity).`
`METAL`	`224 224`		`Iron (By similarity).`
`METAL`	`226 226`		`Iron (By similarity).`

Sequence information

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

Molecular weight: 33378 Da [This is the MW of the unprocessed precursor]

CRC64: BFA17B07716D41D3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIKVFGTKE VQDLLKAATN LEGKGGNARS KQIVHRLLSD LFKAIDDLDI TPDEVWAGVN 

        70         80         90        100        110        120 
YLNKLGQDGE ATLLAAGSGL EKYLDIRLDA ADKAEGIEGG TPRTIEGPLY VAGATVHDGV 

       130        140        150        160        170        180 
SKIDINPDED AGPLVIHGTV TGPDGKPVAG AVVECWHANS KGFYSHFDPT GAQSDFNLRG 

       190        200        210        220        230        240 
AVKTGADGKY EFRTLMPVGY GCPPQGATQQ LLNVLGRHGN RPAHVHFFVS SDSARKLTTQ 

       250        260        270        280        290        300 
FNIEGDPLIW DDFAYATREE LIPPVTEKKG GTALGLKADT YKDIEFNLTL TSLVKGKDNQ 

       310 
VVHRLRAEVA A

O33948 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