P11122 (BPHC_PSEPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biphenyl-2,3-diol 1,2-dioxygenase
EC=1.13.11.39

Alternative name(s):
2,3-dihydroxybiphenyl dioxygenase
Short name=DHBD
23OHBP oxygenase

Gene names

Name:

bphC

Organism

Pseudomonas paucimobilis (Sphingomonas paucimobilis)

Taxonomic identifier

13689 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Sphingomonas

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate.
Cofactor	Fe2+ ion.
Pathway	Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 3/4.
Subunit structure	Homooctamer.
Sequence similarities	Belongs to the extradiol ring-cleavage dioxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	biphenyl-2,3-diol 1,2-dioxygenase activity Inferred from electronic annotation. Source: EC ferrous iron binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 299	299	Biphenyl-2,3-diol 1,2-dioxygenase		PRO_0000085036
Sites
	Metal binding	149	1	Iron By similarity
	Metal binding	212	1	Iron By similarity
	Metal binding	263	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11122 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 29746CAB79D6FC7B	FASTA	299	33,095
	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

References

[1]	"Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1." Taira K., Hayase N., Arimura N., Yamashita S., Miyazaki T., Furukawa K. Biochemistry 27:3990-3996(1988) [PubMed: 3137968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Q1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M20640 Genomic DNA. Translation: AAA25678.1.
PIR	A28718.
3D structure databases
ProteinModelPortal	P11122.
SMR	P11122. Positions 2-299.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR017626. DiOHbiphenyl_dOase. IPR004360. Glyas_Fos-R_dOase. IPR000486. Xdiol_ring_cleave_dOase_1/2. [Graphical view]
Pfam	PF00903. Glyoxalase. 1 hit. [Graphical view]
TIGRFAMs	TIGR03213. 23dbph12diox. 1 hit.
PROSITE	PS00082. EXTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BPHC_PSEPA

Accession

Primary (citable) accession number: P11122

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	September 21, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program