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P17297

- BPHC_PSES1

UniProt

P17297 - BPHC_PSES1

Protein

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

Gene

bphC

Organism
Pseudomonas sp. (strain KKS102)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Fe2+ ion.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi146 – 1461Iron
    Metal bindingi210 – 2101Iron
    Metal bindingi261 – 2611Iron

    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

    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
    OrganismiPseudomonas sp. (strain KKS102)
    Taxonomic identifieri307 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 293292Biphenyl-2,3-diol 1,2-dioxygenasePRO_0000085035Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.

    Structurei

    Secondary structure

    1
    293
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1410
    Helixi16 – 2510
    Beta strandi30 – 356
    Beta strandi38 – 4710
    Beta strandi49 – 546
    Beta strandi59 – 668
    Helixi70 – 8314
    Beta strandi87 – 893
    Helixi92 – 987
    Beta strandi101 – 1077
    Helixi109 – 1113
    Beta strandi113 – 1186
    Beta strandi131 – 1333
    Helixi140 – 1423
    Beta strandi146 – 1505
    Helixi154 – 16310
    Beta strandi168 – 17811
    Beta strandi181 – 19414
    Beta strandi196 – 2005
    Beta strandi205 – 21713
    Helixi218 – 23013
    Beta strandi238 – 2447
    Beta strandi247 – 2526
    Beta strandi259 – 2646
    Beta strandi277 – 2793
    Beta strandi281 – 2855

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DHYX-ray2.30A2-293[»]
    1EILX-ray2.00A2-293[»]
    1EIQX-ray2.00A2-293[»]
    1EIRX-ray2.00A2-293[»]
    1KW3X-ray1.45B2-293[»]
    1KW6X-ray1.45B2-293[»]
    1KW8X-ray2.00B2-293[»]
    1KW9X-ray1.95B2-293[»]
    1KWBX-ray2.00B2-293[»]
    1KWCX-ray2.10B2-293[»]
    ProteinModelPortaliP17297.
    SMRiP17297. Positions 2-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17297.

    Family & Domainsi

    Sequence similaritiesi

    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.

    P17297-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIERLGYLG FAVKDVPAWD HFLTKSVGLM AAGSAGDAAL YRADQRAWRI    50
    AVQPGELDDL AYAGLEVDDA AALERMADKL RQAGVAFTRG DEALMQQRKV 100
    MGLLCLQDPF GLPLEIYYGP AEIFHEPFLP SAPVSGFVTG DQGIGHFVRC 150
    VPDTAKAMAF YTEVLGFVLS DIIDIQMGPE TSVPAHFLHC NGRHHTIALA 200
    AFPIPKRIHH FMLQANTIDD VGYAFDRLDA AGRITSLLGR HTNDQTLSFY 250
    ADTPSPMIEV EFGWGPRTVD SSWTVARHSR TAMWGHKSVR GQR 293
    Length:293
    Mass (Da):32,245
    Last modified:January 23, 2007 - v3
    Checksum:i53EF1B24502E3B24
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26433 Genomic DNA. Translation: AAA25750.1.
    D17319 Genomic DNA. Translation: BAA04141.1.
    PIRiA32312. DAPSPC.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26433 Genomic DNA. Translation: AAA25750.1 .
    D17319 Genomic DNA. Translation: BAA04141.1 .
    PIRi A32312. DAPSPC.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DHY X-ray 2.30 A 2-293 [» ]
    1EIL X-ray 2.00 A 2-293 [» ]
    1EIQ X-ray 2.00 A 2-293 [» ]
    1EIR X-ray 2.00 A 2-293 [» ]
    1KW3 X-ray 1.45 B 2-293 [» ]
    1KW6 X-ray 1.45 B 2-293 [» ]
    1KW8 X-ray 2.00 B 2-293 [» ]
    1KW9 X-ray 1.95 B 2-293 [» ]
    1KWB X-ray 2.00 B 2-293 [» ]
    1KWC X-ray 2.10 B 2-293 [» ]
    ProteinModelPortali P17297.
    SMRi P17297. Positions 2-290.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00155 ; UER00252 .

    Miscellaneous databases

    EvolutionaryTracei P17297.

    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. "Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102."
      Kimbara K., Hashimoto T., Fukuda M., Koana T., Takagi M., Oishi M., Yano K.
      J. Bacteriol. 171:2740-2747(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Identification of the bphA and bphB genes of Pseudomonas sp. strains KKS102 involved in degradation of biphenyl and polychlorinated biphenyls."
      Fukuda M., Yasukochi Y., Kikuchi Y., Nagata Y., Kimbara K., Horiuchi H., Takagi M., Yano K.
      Biochem. Biophys. Res. Commun. 202:850-856(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    3. "Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102."
      Senda T., Sugiyama K., Narita H., Yamamoto T., Kimbara K., Fukuda M., Sato M., Yano K., Mitsui Y.
      J. Mol. Biol. 255:735-752(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    4. "Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase."
      Uragami Y., Senda T., Sugimoto K., Sato N., Nagarajan V., Masai E., Fukuda M., Mitsui Y.
      J. Inorg. Biochem. 83:269-279(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    5. "Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase."
      Sato N., Uragami Y., Nishizaki T., Takahashi Y., Sazaki G., Sugimoto K., Nonaka T., Masai E., Fukuda M., Senda T.
      J. Mol. Biol. 321:621-636(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF NATIVE ENZYME; SUBSTRATE COMPLEXES AND H145A MUTANT.

    Entry informationi

    Entry nameiBPHC_PSES1
    AccessioniPrimary (citable) accession number: P17297
    Secondary accession number(s): Q52441
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 97 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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