NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Q1;
DOI=10.1021/bi00411a015; PubMed=3137968 [NCBI, ExPASy, EBI, Israel, Japan]
Taira K., Hayase N., Arimura N., Yamashita S., Miyazaki T., Furukawa K.;
"Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1.";
Biochemistry 27:3990-3996(1988).

Comments

CATALYTIC ACTIVITY: Biphenyl-2,3-diol + O₂ = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H₂O.
COFACTOR: Fe(2+) ion.
PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoic acid and benzoic acid from biphenyl: step 3/4 .
SUBUNIT: Homooctamer.
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

M20640; AAA25678.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A28718; A28718.

3D structure databases

HSSP

P17297; 1DHY. [HSSP ENTRY / PDB]

ModBase

P11122.

Ontologies

GO:0018583;	Molecular function: biphenyl-2,3-diol 1,2-dioxygenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR017626; DiOHbiphenyl_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; 3.
PD000977; Xdiol_dioxygnse; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00082; EXTRADIOL_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`	`1 299`	`299`	`Biphenyl-2,3-diol 1,2-dioxygenase.`	`PRO_0000085036`
`METAL`	`149 149`		`Iron (By similarity).`
`METAL`	`212 212`		`Iron (By similarity).`
`METAL`	`263 263`		`Iron (By similarity).`

Sequence information

Length: 299 AA [This is the length of the unprocessed precursor]

Molecular weight: 33095 Da [This is the MW of the unprocessed precursor]

CRC64: 29746CAB79D6FC7B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVAVTELGYL GLTVTNLDAW RSYAAEVAGM EIVDEGEGDR LYLRMDQWHH RIVLHASDSD 

        70         80         90        100        110        120 
DLAYLGWRVA DPVEFDAMVA KLTAAGISLT VASEAEARER RVLGLAKLAD PGGNPTEIFY 

       130        140        150        160        170        180 
GPQVDTHKPF HPGRPMYGKF VTGSEGIGHC ILRQDDVPAA AAFYGLLGLR GSVEYHLQLP 

       190        200        210        220        230        240 
NGMVAQPYFM HCNERQHSVA FGLGPMEKRI NHLMFEYTDL DDLGLAHDIV RARKIDVALQ 

       250        260        270        280        290 
LGKHANDQAL TFYCANPSGW LWEFGWGARK APSQQEYYTR DIFGHGNEAA GYGMDIPLG

P11122 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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