P47231 (BPHC1_RHOGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:

bphC1

Organism

Rhodococcus globerulus

Taxonomic identifier

33008 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	291 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.
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 – 291	291	Biphenyl-2,3-diol 1,2-dioxygenase 1		PRO_0000085037
Sites
	Metal binding	146	1	Iron By similarity
	Metal binding	210	1	Iron By similarity
	Metal binding	260	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47231 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 104F189FE1EDDA6A	FASTA	291	32,081
	10 20 30 40 50 60 MSVQRLGYLG IEVSDVDAWR TYATMRLGAM EAPAPEGTAR FRLDSRAWRF MVTPGPADDL 70 80 90 100 110 120 SVAGYEVDSE GALMQVKTRL EAYGVKVTSE SSELAAERGV LGLISCVDPA GTRLEIYYGG 130 140 150 160 170 180 TEMFEVPFAS PTGVKEFRTD DQGMGHYVLA VPDVDAALDF YVQGLGFHLS DVIDWQVSPE 190 200 210 220 230 240 VSVRLHFLHC NGRHHTLAVV GMPSDKKMHH LMIETTNLDD VGLAYDRCVE DDAVILTLGR 250 260 270 280 290 HTNDHMVSFY GATPSGFAVE FGWGSRVVEP GWSVVRYDAI SIWGHKIMRG E

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75633 Genomic DNA. Translation: CAA53297.1.
PIR	B53419.
3D structure databases
ProteinModelPortal	P47231.
SMR	P47231. Positions 2-287.
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

BPHC1_RHOGO

Accession

Primary (citable) accession number: P47231

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	September 21, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program