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O58925

- O58925_PYRHO

UniProt

O58925 - O58925_PYRHO

Protein
Submitted name:

458aa long hypothetical endo-1,4-beta-glucanase

Gene

PH1171

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Zinc 1Imported
    Metal bindingi62 – 621Zinc 1; via pros nitrogenImported
    Binding sitei190 – 1901Phosphate 3
    Binding sitei191 – 1911Phosphate 2; via amide nitrogen
    Metal bindingi321 – 3211Zinc 2Imported
    Metal bindingi325 – 3251Zinc 2; via tele nitrogenImported
    Metal bindingi372 – 3721Zinc 1Imported
    Metal bindingi373 – 3731Zinc 1Imported

    GO - Molecular functioni

    1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Ligandi

    Metal-bindingImported, ZincImported

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-1162-MONOMER.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    458aa long hypothetical endo-1,4-beta-glucanaseImported
    Gene namesi
    Ordered Locus Names:PH1171Imported
    OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)Imported
    Taxonomic identifieri70601 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000000752: Chromosome

    Interactioni

    Protein-protein interaction databases

    STRINGi70601.PH1171.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZUMX-ray1.95A1-458[»]
    2ZUNX-ray2.00A/B/C1-458[»]
    3AXXX-ray1.90A/B/C1-458[»]
    3QHMX-ray2.01A/B/C1-458[»]
    3QHNX-ray1.99A/B/C1-458[»]
    3QHOX-ray1.65A/B/C1-458[»]
    3VVGX-ray1.90A/B/C34-410[»]
    3W6LX-ray1.75A/B/C34-410[»]
    3W6MX-ray1.95A/B/C34-410[»]
    4DM1X-ray1.75A/B/C34-410[»]
    4DM2X-ray1.95A/B/C34-410[»]
    ProteinModelPortaliO58925.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO58925.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000225207.
    KOiK01179.
    OMAiKYKNDDT.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR027552. CGP_CTERM.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR04288. CGP_CTERM. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O58925-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGNTILKIV LICTILAGLF GQVVPVYAEN TTYQTPTGIY YEVRGDTIYM    50
    INVTSGEETP IHLFGVNWFG FETPNHVVHG LWKRNWEDML LQIKSLGFNA 100
    IRLPFCTESV KPGTQPIGID YSKNPDLRGL DSLQIMEKII KKAGDLGIFV 150
    LLDYHRIGCT HIEPLWYTED FSEEDFINTW IEVAKRFGKY WNVIGADLKN 200
    EPHSVTSPPA AYTDGTGATW GMGNPATDWN LAAERIGKAI LKVAPHWLIF 250
    VEGTQFTNPK TDSSYKWGYN AWWGGNLMAV KDYPVNLPRN KLVYSPHVYG 300
    PDVYNQPYFG PAKGFPDNLP DIWYHHFGYV KLELGYSVVI GEFGGKYGHG 350
    GDPRDVIWQN KLVDWMIENK FCDFFYWSWN PDSGDTGGIL QDDWTTIWED 400
    KYNNLKRLMD SCSKSSSSTQ SVIRSTTPTK SNTSKKICGP AILIILAVFS 450
    LLLRRAPR 458
    Length:458
    Mass (Da):51,930
    Last modified:August 1, 1998 - v1
    Checksum:iCAE48AD43A8EE654
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA30271.1.
    PIRiE71059.
    RefSeqiNP_143072.1. NC_000961.1.
    WP_010885255.1. NC_000961.1.

    Genome annotation databases

    EnsemblBacteriaiBAA30271; BAA30271; BAA30271.
    GeneIDi1443490.
    KEGGipho:PH1171.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA30271.1 .
    PIRi E71059.
    RefSeqi NP_143072.1. NC_000961.1.
    WP_010885255.1. NC_000961.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZUM X-ray 1.95 A 1-458 [» ]
    2ZUN X-ray 2.00 A/B/C 1-458 [» ]
    3AXX X-ray 1.90 A/B/C 1-458 [» ]
    3QHM X-ray 2.01 A/B/C 1-458 [» ]
    3QHN X-ray 1.99 A/B/C 1-458 [» ]
    3QHO X-ray 1.65 A/B/C 1-458 [» ]
    3VVG X-ray 1.90 A/B/C 34-410 [» ]
    3W6L X-ray 1.75 A/B/C 34-410 [» ]
    3W6M X-ray 1.95 A/B/C 34-410 [» ]
    4DM1 X-ray 1.75 A/B/C 34-410 [» ]
    4DM2 X-ray 1.95 A/B/C 34-410 [» ]
    ProteinModelPortali O58925.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 70601.PH1171.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA30271 ; BAA30271 ; BAA30271 .
    GeneIDi 1443490.
    KEGGi pho:PH1171.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000225207.
    KOi K01179.
    OMAi KYKNDDT.

    Enzyme and pathway databases

    BioCyci PHOR70601:GJWR-1162-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O58925.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR027552. CGP_CTERM.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    TIGRFAMsi TIGR04288. CGP_CTERM. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3Imported.
    2. "Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii."
      Kim H.-W., Ishikawa K.
      Submitted (OCT-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
    3. "Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii."
      Kim H.W., Ishikawa K.
      Proteins 78:496-500(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC.
    4. "Functional analysis of hyperthermophilic endocellulase from Pyrococcus horikoshii by crystallographic snapshots."
      Kim H.W., Ishikawa K.
      Biochem. J. 437:223-230(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    5. "Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase."
      Kim H.-W., Ishikawa K.
      Submitted (FEB-2012) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 34-410.
    6. "The Crystal Structure of Cellulase-Inhibitor Complex."
      Ishikawa K., Maeno Y., Kataoka M.
      Submitted (JUL-2012) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 34-410.
    7. "The role of disulfide bond in hyperthermophilic endocellulase."
      Kim H.W., Ishikawa K.
      Extremophiles 17:593-599(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 34-410.

    Entry informationi

    Entry nameiO58925_PYRHO
    AccessioniPrimary (citable) accession number: O58925
    Entry historyi
    Integrated into UniProtKB/TrEMBL: August 1, 1998
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteomeImported

    External Data

    Dasty 3