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P47228

- BPHC_BURXL

UniProt

P47228 - BPHC_BURXL

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Protein
Biphenyl-2,3-diol 1,2-dioxygenase
Gene
bphC, Bxeno_C1125, Bxe_C1191
Organism
Burkholderia xenovorans (strain LB400)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Shows a preference for catechols with groups immediately adjacent to the hydroxyl substituents.

Catalytic activityi

Biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate.

Cofactori

Binds 1 Fe2+ ion per subunit.

Kineticsi

Substrate inhibition occurs at 300 µM (+/- 20 µM).

  1. KM=7 µM for biphenyl-2,3-diol

pH dependencei

Optimum pH is 8.0.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi146 – 1461Iron
Metal bindingi210 – 2101Iron
Metal bindingi260 – 2601Iron

GO - Molecular functioni

  1. biphenyl-2,3-diol 1,2-dioxygenase activity Source: UniProtKB-EC
  2. ferrous iron binding Source: InterPro

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
  2. xenobiotic catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciBXEN266265:GJII-8843-MONOMER.
SABIO-RKP47228.
UniPathwayiUPA00155; UER00252.

Names & Taxonomyi

Protein namesi
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 namesi
Name:bphC
Ordered Locus Names:Bxeno_C1125
ORF Names:Bxe_C1191
OrganismiBurkholderia xenovorans (strain LB400)
Taxonomic identifieri266265 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000001817: Chromosome 3

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 298297Biphenyl-2,3-diol 1,2-dioxygenase
PRO_0000085033Add
BLAST

Interactioni

Subunit structurei

Homooctamer. The enzyme is composed of two planar tetramers rotated at 45 degrees relative to each other, with a channel in the middle.1 Publication

Protein-protein interaction databases

STRINGi266265.Bxe_C1191.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412
Helixi16 – 2510
Beta strandi30 – 356
Beta strandi38 – 4710
Beta strandi49 – 546
Beta strandi59 – 6911
Helixi70 – 8213
Helixi92 – 987
Beta strandi101 – 1077
Beta strandi113 – 1186
Beta strandi131 – 1333
Helixi140 – 1423
Beta strandi146 – 1505
Helixi154 – 16310
Beta strandi168 – 17811
Beta strandi181 – 19414
Beta strandi196 – 2005
Beta strandi205 – 21612
Helixi218 – 22912
Turni230 – 2323
Beta strandi234 – 24411
Beta strandi247 – 2526
Beta strandi258 – 2636
Beta strandi275 – 2784
Beta strandi280 – 2845

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HANX-ray1.90A2-298[»]
1KMYX-ray2.00A2-298[»]
1KNDX-ray1.90A2-298[»]
1KNFX-ray1.90A2-298[»]
1LGTX-ray1.70A2-298[»]
1LKDX-ray1.70A2-298[»]
ProteinModelPortaliP47228.
SMRiP47228. Positions 2-289.

Miscellaneous databases

EvolutionaryTraceiP47228.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0346.
HOGENOMiHOG000052193.
KOiK00462.
OMAiRIDSRAW.
OrthoDBiEOG64JFM4.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR017626. DiOHbiphenyl_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 2 hits.
TIGRFAMsiTIGR03213. 23dbph12diox. 1 hit.
PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P47228-1 [UniParc]FASTAAdd to Basket

« Hide

MSIRSLGYMG FAVSDVAAWR SFLTQKLGLM EAGTTDNGDL FRIDSRAWRI    50
AVQQGEVDDL AFAGYEVADA AGLAQMADKL KQAGIAVTTG DASLARRRGV 100
TGLITFADPF GLPLEIYYGA SEVFEKPFLP GAAVSGFLTG EQGLGHFVRC 150
VPDSDKALAF YTDVLGFQLS DVIDMKMGPD VTVPAYFLHC NERHHTLAIA 200
AFPLPKRIHH FMLEVASLDD VGFAFDRVDA DGLITSTLGR HTNDHMVSFY 250
ASTPSGVEVE YGWSARTVDR SWVVVRHDSP SMWGHKSVRD KAAARNKA 298
Length:298
Mass (Da):32,471
Last modified:January 23, 2007 - v2
Checksum:iADC0E4709E193FAB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66122 Genomic DNA. Translation: CAA46910.1.
CP000272 Genomic DNA. Translation: ABE37053.1.
PIRiJN0815.
RefSeqiWP_011494295.1. NC_007953.1.
YP_556403.1. NC_007953.1.

Genome annotation databases

EnsemblBacteriaiABE37053; ABE37053; Bxe_C1191.
GeneIDi4010703.
KEGGibxe:Bxe_C1191.
PATRICi19343367. VBIBurXen52548_8941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66122 Genomic DNA. Translation: CAA46910.1 .
CP000272 Genomic DNA. Translation: ABE37053.1 .
PIRi JN0815.
RefSeqi WP_011494295.1. NC_007953.1.
YP_556403.1. NC_007953.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HAN X-ray 1.90 A 2-298 [» ]
1KMY X-ray 2.00 A 2-298 [» ]
1KND X-ray 1.90 A 2-298 [» ]
1KNF X-ray 1.90 A 2-298 [» ]
1LGT X-ray 1.70 A 2-298 [» ]
1LKD X-ray 1.70 A 2-298 [» ]
ProteinModelPortali P47228.
SMRi P47228. Positions 2-289.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266265.Bxe_C1191.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE37053 ; ABE37053 ; Bxe_C1191 .
GeneIDi 4010703.
KEGGi bxe:Bxe_C1191.
PATRICi 19343367. VBIBurXen52548_8941.

Phylogenomic databases

eggNOGi COG0346.
HOGENOMi HOG000052193.
KOi K00462.
OMAi RIDSRAW.
OrthoDBi EOG64JFM4.

Enzyme and pathway databases

UniPathwayi UPA00155 ; UER00252 .
BioCyci BXEN266265:GJII-8843-MONOMER.
SABIO-RK P47228.

Miscellaneous databases

EvolutionaryTracei P47228.

Family and domain databases

Gene3Di 3.10.180.10. 2 hits.
InterProi IPR017626. DiOHbiphenyl_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view ]
Pfami PF00903. Glyoxalase. 1 hit.
[Graphical view ]
SUPFAMi SSF54593. SSF54593. 2 hits.
TIGRFAMsi TIGR03213. 23dbph12diox. 1 hit.
PROSITEi PS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic analysis of a Pseudomonas locus encoding a pathway for biphenyl/polychlorinated biphenyl degradation."
    Hofer B., Eltis L.D., Dowling D.N., Timmis K.N.
    Gene 130:47-55(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LB400.
  3. "Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase."
    Eltis L.D., Hofmann B., Hecht H.J., Luensdorf H., Timmis K.N.
    J. Biol. Chem. 268:2727-2732(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-32, SUBSTRATE CHARACTERIZATION, PRELIMINARY CRYSTALLIZATION, SUBUNIT.
  4. "Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad."
    Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T.
    Science 270:976-980(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  5. "Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol."
    Vaillancourt F.H., Han S., Fortin P.D., Bolin J.T., Eltis L.D.
    J. Biol. Chem. 273:34887-34895(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiBPHC_BURXL
AccessioniPrimary (citable) accession number: P47228
Secondary accession number(s): Q13FT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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