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Q9ZF13

- Q9ZF13_THEFU

UniProt

Q9ZF13 - Q9ZF13_THEFU

Protein
Submitted name:

Beta-mannanase

Gene

man

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei28 – 281Beta-D-mannoseImported
    Binding sitei57 – 571Beta-D-mannoseImported
    Sitei125 – 1251Important for catalytic activityImported
    Sitei126 – 1261Important for catalytic activityImported
    Sitei194 – 1941Important for catalytic activityImported
    Sitei196 – 1961Important for catalytic activityImported
    Sitei223 – 2231Important for catalytic activityImported

    GO - Molecular functioni

    1. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    GlycosidaseUniRule annotationImported, Hydrolase

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Beta-mannanaseImported (EC:3.2.1.78Imported)
    Gene namesi
    Name:manImported
    OrganismiThermobifida fusca (Thermomonospora fusca)Imported
    Taxonomic identifieri2021 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQCX-ray1.50A1-279[»]
    2MANX-ray1.90A1-279[»]
    3MANX-ray1.60A1-279[»]
    ProteinModelPortaliQ9ZF13.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZF13.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni257 – 2582Mannose bindingImported

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 5 family.UniRule annotation

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    Q9ZF13-1 [UniParc]FASTAAdd to Basket

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    GLHVKNGRLY EANGQEFIIR GVSHPHNWYP QHTQAFADIK SHGANTVRVV    50
    LSNGVRWSKN GPSDVANVIS LCKQNRLICM LEVHDTTGYG EQSGASTLDQ 100
    AVDYWIELKS VLQGEEDYVL INIGNEPYGN DSATVAAGAW DTSAAIQRLR 150
    AAGFEHTLVV DAPNWGQDWT NTMRNNADQV YASDPTGNTV FSIHMYGVYS 200
    QASTITSYLE HFVNAGLPLI IGEFGHDHSD GNPDEDTIMA EAERLKLGYI 250
    GWSWSGNGGG VEYLDMVYNF DGDNLSPWG 279
    Length:279
    Mass (Da):30,657
    Last modified:May 1, 1999 - v1
    Checksum:i98A2850FAE013DB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11Imported
    Non-terminal residuei279 – 2791Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006227 Genomic DNA. Translation: CAA06924.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006227 Genomic DNA. Translation: CAA06924.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BQC X-ray 1.50 A 1-279 [» ]
    2MAN X-ray 1.90 A 1-279 [» ]
    3MAN X-ray 1.60 A 1-279 [» ]
    ProteinModelPortali Q9ZF13.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9ZF13.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Crystallization and preliminary crystallographic analysis of two beta-mannanase isoforms from Thermomonospora fusca KW3."
      Hilge M., Gloor S., Winterhalter K., Piontek K.
      Acta Crystallogr. 52:1224-1225(1996)
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: KW3Imported.
    2. "High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5."
      Hilge M., Gloor S.M., Rypniewski W., Sauer O., Heightman T.D., Zimmermann W., Winterhalter K., Piontek K.
      Structure 6:1433-1444(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: KW3Imported.

    Entry informationi

    Entry nameiQ9ZF13_THEFU
    AccessioniPrimary (citable) accession number: Q9ZF13
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 1, 1999
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3