NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28, AND CHARACTERIZATION.
STRAIN=P6;
PubMed=8126007 [NCBI, ExPASy, EBI, Israel, Japan]
Asturias J.A., Eltis L.D., Prucha M., Timmis K.N.;
"Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases.";
J. Biol. Chem. 269:7807-7815(1994).

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: Homohexamer.
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

X75634; CAA53298.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C53419; C53419.

3D structure databases

ModBase

P47232.

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).
QuickGo view.

Family and domain databases

InterPro

IPR004360; Glyas_bleo-R_dOase.
IPR000486; Xdiol_dOase_1_2.
Graphical view of domain structure.

Pfam

PF00903; Glyoxalase; 1.
Pfam graphical view of domain structure.

ProDom

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

PROSITE

PS00082; EXTRADIOL_DIOXYGENAS; 1.

ProtoNet

P47232.

Other

UniRef

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

Keywords

Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 190`	`189`	`Biphenyl-2,3-diol 1,2-dioxygenase 2.`	`PRO_0000085038`
`METAL`	`9 9`		`Iron (By similarity).`
`METAL`	`72 72`		`Iron (By similarity).`
`METAL`	`120 120`		`Iron (By similarity).`

Sequence information

Length: 190 AA [This is the length of the unprocessed precursor]

Molecular weight: 20844 Da [This is the MW of the unprocessed precursor]

CRC64: F0B362C3BECF3679 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTATPKFAHV VLQTSRFEAM RDWYCTVLDA HVVYEGHGLC FITFDEEHHR VALLGAPTAL 

        70         80         90        100        110        120 
EPRNPGAAGM HHTAYTFDTL GDLLDRYESL KSKGIEPKVP IQHGVTTSLY YQDPDGNFVE 

       130        140        150        160        170        180 
LQIDNFSTPD EATAYMNGPE YGGNPVGVSF DPVLIPQALS AGTPVDRITT HAWALETTPD 

       190 
LPNPMIALTS

P47232 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