Reviewed, UniProtKB/Swiss-Prot P47233 (BPHC3_RHOGO)

Names and origin

Protein names

Recommended name:
    Biphenyl-2,3-diol 1,2-dioxygenase 3
    EC=1.13.11.39
Alternative name(s):
    Biphenyl-2,3-diol 1,2-dioxygenase III
    23OHBP oxygenase III
    2,3-dihydroxybiphenyl dioxygenase III
      Short name=DHBD III

Gene names

Name:

bphC3

Organism

Rhodococcus globerulus

Taxonomic identifier

33008 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Biphenyl-2,3-diol + O(2) = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H(2)O.
Cofactor	Fe(2+) ion.
Pathway	Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoic acid and benzoic acid from biphenyl: step 3/4.
Subunit structure	Homohexamer By similarity.
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 190	189	Biphenyl-2,3-diol 1,2-dioxygenase 3		PRO_0000085039
Sites
	Metal binding	9	1	Iron By similarity
	Metal binding	73	1	Iron By similarity
	Metal binding	121	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47233-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5CA026ED8D13C7E2	FASTA	190	21,191
	10 20 30 40 50 60 MTVTPRLAHF VLQTNQLPAM TQWYIDVLGA HVVYENPAMC FLTTDEEHHR VALFGPPGGG 70 80 90 100 110 120 LPERTPATVG LAHTAFTFPT LGDLIDKYLQ LRDKGIEPRV PVQHGVTTSL YYRDPDGNMV 130 140 150 160 170 180 ELQIDNFATP EESTDYMHGE EYTTDTIGPS FNPLALAEAY KAGVPESELT TRAWALKTEQ 190 INVMERMLTP

References

[1]

"Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases." Asturias J.A., Eltis L.D., Prucha M., Timmis K.N. J. Biol. Chem. 269:7807-7815(1994) [PubMed: 8126007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: P6.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X75635 Genomic DNA. Translation: CAA53299.1.
PIR	D53419.
3D structure databases
HSSP	HSSP built from PDB template 1KMZ based on UniProtKB O05205.
ModBase	Search...
Family and domain databases
InterPro	IPR004360. Glyas_bleo-R_dOase. IPR000486. Xdiol_dOase_1_2. [Graphical view]
Pfam	PF00903. Glyoxalase. 1 hit. [Graphical view]
ProDom	PD002334. Gly_diox. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00082. EXTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BPHC3_RHOGO

Accession

Primary (citable) accession number: P47233

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)