NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JI104;
Kitayama A., Achioku T., Yanagawa T., Kanou K., Kikuchi M., Ueda H., Suzuki E., Nishimura H., Nagamune T., Kawakami Y.;
"Cloning and characterization of extradiol aromatic ring-cleavage dioxygenases of Pseudomonas aeruginosa JI104.";
J. Ferment. Bioeng. 82:217-223(1996).

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

X60740; CAA43145.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15522; JC2503.

3D structure databases

HSSP

P06622; 1MPY. [HSSP ENTRY / PDB]

SMR

P27887; 1-307.

ModBase

P27887.

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

P27887.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 307`	`307`	`Metapyrocatechase.`	`PRO_0000085026`
`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: 35124 Da [This is the MW of the unprocessed precursor]

CRC64: E178E5F287410ACC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKGIMRPGH VQLRVLDMSK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV DKFSVVLRER 

        70         80         90        100        110        120 
DEPGMDFMGF KVVDEDALRQ LERDLTAYGC AVEQLPAGEL NSCGRRVRFQ APSGHHFELY 

       130        140        150        160        170        180 
ADKEYTGKWG VNEVNPEAWP RDLKGMAAVR FDHCLLYGDE LPATYDLFTK VLGFYLAEQV 

       190        200        210        220        230        240 
LDENGTRVAQ FLSLSTKAHD VAFIHHPEKG RLHHVSFHLE TWEDVLRAAD LISMTDTSID 

       250        260        270        280        290        300 
IGPTRHGLTH GKTIYFFDPS GNRSEVFCGG NYSYPDHKPV TWLAKDLGKA IFYHDRVLNE 


RFMTVLT

P27887 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