[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY PHENOL. STRAIN=ATCC 11171 / NCIB 8250 / CIP 63.46 / B94; PubMed=8596453 [NCBI, ExPASy, EBI, Israel, Japan] Ehrt S., Schirmer F., Hillen W.; "Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoacetious."; Mol. Microbiol. 18:13-20(1995).
[2]	INDUCTION BY PHENOL AND BENZOATE. PubMed=8206826 [NCBI, ExPASy, EBI, Israel, Japan] Ehrt S., Ornston L.N., Hillen W.; "RpoN (sigma 54) is required for conversion of phenol to catechol in Acinetobacter calcoaceticus."; J. Bacteriol. 176:3493-3499(1994).

Comments

CATALYTIC ACTIVITY: Catechol + O₂ = cis,cis-muconate.
COFACTOR: Binds 1 Fe(3+) ion per subunit (By similarity).
PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydrofuran-2-acetate from catechol: step 1/3 .
SUBUNIT: Homodimer (By similarity).
INDUCTION: By phenol and benzoate.
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

Z36909; CAA85386.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S47293; S47293.

3D structure databases

HSSP

P07773; 1DMH. [HSSP ENTRY / PDB]

ModBase

Q43984.

Ontologies

GO:0018576;	Molecular function: catechol 1,2-dioxygenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008199;	Molecular function: ferric iron binding (inferred from sequence or structural similarity from UniProtKB).
GO:0019614;	Biological process: catechol catabolic process (inferred from sequence or structural similarity 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.

Other

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`	`1 305`	`305`	`Catechol 1,2-dioxygenase.`	`PRO_0000085080`
`METAL`	`163 163`		`Iron.`
`METAL`	`197 197`		`Iron.`
`METAL`	`221 221`		`Iron.`
`METAL`	`223 223`		`Iron.`

Sequence information

Length: 305 AA [This is the length of the unprocessed precursor]

Molecular weight: 33609 Da [This is the MW of the unprocessed precursor]

CRC64: E65143DFA0572937 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMMNRQQIDS LVQQMNVATA TGEVNLRVQQ IVVRLLGDLF QAIEDLNMSQ TELWKGLEYL 

        70         80         90        100        110        120 
TDAGQANELG LLAAGLGLEH YLDLRADEAD AKAGITGGTP RTIEGPLYVA GAPESVGFAR 

       130        140        150        160        170        180 
MDDGSESAHV DALIIEGNVT DTAGQIIPNA KVEIWHANSL GNYSFFDKSQ SAFNLRRSIF 

       190        200        210        220        230        240 
TDTQGQYIAQ TTMPVGYGCP PEGTTQALLN LLGRHGNRPS HVHYFVSAPG YRKLTTQFNI 

       250        260        270        280        290        300 
EGDKYLWDDF AFATRDGLIA TALDVTDLAK IKQYNLNKAF KHIKFNFQLV QDADQVPLQR 


LIVVE

Q43984 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