Reviewed, UniProtKB/Swiss-Prot P47232 (BPHC2_RHOGO)

Names and origin

Protein names

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

Gene names

Name:

bphC2

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	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O.
Cofactor	Fe2+ ion.
Pathway	Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 3/4.
Subunit structure	Homohexamer.
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
Technical term	Direct protein sequencing
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 Ref.1
	Chain	2 – 190	189	Biphenyl-2,3-diol 1,2-dioxygenase 2		PRO_0000085038
Sites
	Metal binding	9	1	Iron By similarity
	Metal binding	72	1	Iron By similarity
	Metal binding	120	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47232-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F0B362C3BECF3679	FASTA	190	20,844
	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

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], PROTEIN SEQUENCE OF 2-28, CHARACTERIZATION. Strain: P6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75634 Genomic DNA. Translation: CAA53298.1.
PIR	C53419.
3D structure databases
SMR	P47232. Positions 6-152.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.13.11.39. 189189.
Family and domain databases
InterPro	IPR004360. Glyas_bleo-R_dOase. IPR000486. Xdiol_ring_cleave_dOase_1/2. [Graphical view]
Pfam	PF00903. Glyoxalase. 1 hit. [Graphical view]
PROSITE	PS00082. EXTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BPHC2_RHOGO

Accession

Primary (citable) accession number: P47232

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
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)