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InterPro: IPR017626 2,3-dihydroxybiphenyl 1,2-dioxygenase

Protein matches Help

UniProtKB

Matches:

76 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR017626 DiOHbiphenyl_dOase

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR03213	23dbph12diox	76
Signatures in BioMart

InterPro Relationships Help

Contains

IPR000486 Extradiol ring-cleavage dioxygenase, class I /II

GO Term annotation Help

Process

GO:0042178 xenobiotic catabolic process

Function

GO:0005506 iron ion binding
GO:0051213 dioxygenase activity

InterPro annotation

Entry Details in BioMart

Abstract

2,3-dihydroxybiphenyl 1,2-dioxygenase is the third enzyme of a pathway for biphenyl degradation. Many of the extradiol ring-cleaving dioxygenases, to which these proteins belong, act on a range of related substrates. Some members of this family may be found operons for toluene or naphthalene degradation, where other activities of the same enzyme may be more significant

Structural links Help

PDB - click here

SCOP: d.32.1.3

CATH: 3.10.180.10

Database links Help

Enzyme: EC:1.13.11

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR017626

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P17297 Biphenyl-2,3-diol 1,2-dioxygenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004360	Glyoxalase/bleomycin resistance protein/dioxygenase
IPR000486	Extradiol ring-cleavage dioxygenase, class I /II
IPR017626	2,3-dihydroxybiphenyl 1,2-dioxygenase
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Senda T, Sugiyama K, Narita H, Yamamoto T, Kimbara K, Fukuda M, Sato M, Yano K, Mitsui Y. Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. J. Mol. Biol. 255 1996 735-52 [PubMed: 8636975] http://dx.doi.org/10.1006/jmbi.1996.0060
	Sato N, Uragami Y, Nishizaki T, Takahashi Y, Sazaki G, Sugimoto K, Nonaka T, Masai E, Fukuda M, Senda T. Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase. J. Mol. Biol. 321 2002 621-36 [PubMed: 12206778] http://dx.doi.org/10.1016/S0022-2836(02)00673-3
	Vaillancourt FH, Han S, Fortin PD, Bolin JT, Eltis LD. Molecular basis for the stabilization and inhibition of 2, 3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol. J. Biol. Chem. 273 1998 34887-95 [PubMed: 9857017] http://dx.doi.org/10.1074/jbc.273.52.34887
	Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y. Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase. J. Inorg. Biochem. 83 2001 269-79 [PubMed: 11293547] http://dx.doi.org/10.1016/S0162-0134(00)00172-0
	Dai S, Vaillancourt FH, Maaroufi H, Drouin NM, Neau DB, Snieckus V, Bolin JT, Eltis LD. Identification and analysis of a bottleneck in PCB biodegradation. Nat. Struct. Biol. 9 2002 934-9 [PubMed: 12415290] http://dx.doi.org/10.1038/nsb866

InterPro 23.1