NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1672868 [NCBI, ExPASy, EBI, Israel, Japan]
Benjamin R.C., Voss J.A., Kunz D.A.;
"Nucleotide sequence of xylE from the TOL pDK1 plasmid and structural comparison with isofunctional catechol-2,3-dioxygenase genes from TOL, pWW0 and NAH7.";
J. Bacteriol. 173:2724-2728(1991).

Comments

CATALYTIC ACTIVITY: Catechol + O₂ = 2-hydroxymuconate semialdehyde.
COFACTOR: Fe(2+) ion.
PATHWAY: Xenobiotic degradation; toluene degradation .
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the extradiol 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

M65205; AAA23353.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A42733; A42733.

RefSeq

YP_709347.1; -.

3D structure databases

HSSP

P06622; 1MPY. [HSSP ENTRY / PDB]

SMR

Q04285; 1-307.

ModBase

Q04285.

Ontologies

GO:0018577;	Molecular function: catechol 2,3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0008198;	Molecular function: ferrous iron binding (inferred from electronic annotation from InterPro).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR017624; Catechol_2-3_dOase.
IPR004360; Glyas_bleo-R_dOase.
IPR000486; Xdiol_dOase_1_2.
Graphical view of domain structure.

Pfam

PF00903; Glyoxalase; 2.
Pfam graphical view of domain structure.

ProDom

PD002334; Gly_diox; 2.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00082; EXTRADIOL_DIOXYGENAS; 1.

ProtoNet

Q04285.

Genome annotation databases

GeneID

4226923; -.

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`	`1 307`	`307`	`Metapyrocatechase.`	`PRO_0000085028`
`METAL`	`153 153`		`Iron (By similarity).`
`METAL`	`214 214`		`Iron (By similarity).`
`METAL`	`265 265`		`Iron (By similarity).`

Sequence information

Length: 307 AA [This is the length of the unprocessed precursor]

Molecular weight: 35234 Da [This is the MW of the unprocessed precursor]

CRC64: E91D95B331ECFEB8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKGVMRPGH VQLRVLNLEA ALTHYRDLLG LIEMDRDEQG RVYLKAWSEV DKFSVVLREA 

        70         80         90        100        110        120 
DQPGMDFMGF KVTDDACLTR LAGELLEFGC QVEEIPAGEL KDCGRRVRFL APSGHFFELY 

       130        140        150        160        170        180 
AEKEYTGKWG IEEVNPEAWP RDLKGMRAVR FDHCLMYGDE LQATYELFTE VLGFYLAEQV 

       190        200        210        220        230        240 
IEDNGTRISQ FLSLSTKAHD VAFIQHAEKG KFHHVSFFLE TWEDVLRAAD LISMTDTSID 

       250        260        270        280        290        300 
IGPTRHGLTH GKTIYFFDPS GNRNEVFCGG DYNYPDHKPV TWTADQLGKA IFYHDRILNE 


RFMTVLT

Q04285 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