NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(91)90098-V; PubMed=2013408 [NCBI, ExPASy, EBI, Israel, Japan]
Kivisaar M., Kasak L., Nurk A.;
"Sequence of the plasmid-encoded catechol 1,2-dioxygenase-expressing gene, pheB, of phenol-degrading Pseudomonas sp. strain EST1001.";
Gene 98:15-20(1991).

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 .
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

M57500; AAC64900.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JN0143; JN0143.

3D structure databases

HSSP

P07773; 1DMH. [HSSP ENTRY / PDB]

ModBase

P31019.

Ontologies

GO:0018576;	Molecular function: catechol 1,2-dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0008199;	Molecular function: ferric iron binding (inferred from electronic annotation from InterPro).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0019614;	Biological process: catechol catabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

P31019.

Other

UniRef

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

Keywords

Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 302`	`302`	`Catechol 1,2-dioxygenase.`	`PRO_0000085085`
`METAL`	`164 164`		`Iron (By similarity).`
`METAL`	`198 198`		`Iron (By similarity).`
`METAL`	`222 222`		`Iron (By similarity).`
`METAL`	`224 224`		`Iron (By similarity).`

Sequence information

Length: 302 AA [This is the length of the unprocessed precursor]

Molecular weight: 33362 Da [This is the MW of the unprocessed precursor]

CRC64: A86F17E68D1EAC3A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVKIYDTPE VQDFLKIVAG LDQEGGNDRG KQIIHRILSD LYRTIDDFDI TAEQYWSAVS 

        70         80         90        100        110        120 
LLNALGQASQ FGLLSPGLGF DHYMDMRMDA ADAEAKRTGG TPRTIEGPLY VAGAPEAEGF 

       130        140        150        160        170        180 
ARMDDDPDTD GETMWLHGQV RDTAGKPIPG AKVEIWHCNS KGGYSFFDKS QTPYNLRRTI 

       190        200        210        220        230        240 
IADNEGYYRA RSVIPSGYGV PEGAPTDQVL KLLGRHGERP AHIHYFISAP GHQHLTTQIN 

       250        260        270        280        290        300 
LAGDPYTYDD FAFATRQDLA AEGKRVENHP AAQQYGVEGT VTEVIFNIEL SPTAEEELQA 


RP

P31019 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