[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=KF707; PubMed=3793719 [NCBI, ExPASy, EBI, Israel, Japan] Furukawa K., Arimura N., Miyazaki T.; "Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of Pseudomonas pseudoalcaligenes."; J. Bacteriol. 169:427-429(1987).

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

M15333; AAA25753.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P47228; 1KND. [HSSP ENTRY / PDB]

SMR

P08695; 2-288.

ModBase

P08695.

Ontologies

GO:0018583;	Molecular function: biphenyl-2,3-diol 1,2-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).
GO:0042178;	Biological process: xenobiotic catabolic process (inferred from electronic annotation from InterPro).
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; 2.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00082; EXTRADIOL_DIOXYGENAS; 1.

ProtoNet

P08695.

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`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 303`	`302`	`Biphenyl-2,3-diol 1,2-dioxygenase.`	`PRO_0000085034`
`METAL`	`146 146`		`Iron (By similarity).`
`METAL`	`210 210`		`Iron (By similarity).`
`METAL`	`260 260`		`Iron (By similarity).`

Sequence information

Length: 303 AA [This is the length of the unprocessed precursor]

Molecular weight: 33206 Da [This is the MW of the unprocessed precursor]

CRC64: 6844D0ABBD81FED5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIRSLGYMG FAVSDVAAWR SFLTQKLGLM EAGTTDNGDL FRIDSRAWRI AVQQGEVDDL 

        70         80         90        100        110        120 
AFAGYEVADA AGLAQMADKL KQAGIAVTTG DASLARRRGV TGLITFADPF GLPLEIYYGA 

       130        140        150        160        170        180 
SEVFEKPFLP GAAVSGFLTG EQGLGHFVRC VPDSDKALAF YTDVLGFQLS DVIDMKMGPD 

       190        200        210        220        230        240 
VTVPVYFLHC NERHHTLAIA AFPLPKRIHH FMLEVASLDD VGFAFDRVDA DGLITSTLGR 

       250        260        270        280        290        300 
HTNDHMVSFY ASTPSGVEVE YGWSARTVDR SWVVVRHDSP SMWGHKSVRD KALRATKHEQ 


QPE

P08695 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