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P47228

- BPHC_BURXL

UniProt

P47228 - BPHC_BURXL

Protein

Biphenyl-2,3-diol 1,2-dioxygenase

Gene

bphC

Organism
Burkholderia xenovorans (strain LB400)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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-dioxygenasePRO_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

    1
    298
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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: October 1, 2014
    This is version 111 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, Reference proteome

    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