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P23473

- CHLY_PARTH

UniProt

P23473 - CHLY_PARTH

Protein

Bifunctional chitinase/lysozyme

Gene
N/A
Organism
Parthenocissus quinquefolia (Virginia creeper) (Hedera quinquefolia)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Bifunctional enzyme with lysozyme/chitinase activity.

    Catalytic activityi

    Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
    Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

    GO - Molecular functioni

    1. chitinase activity Source: UniProtKB-EC
    2. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. chitin catabolic process Source: UniProtKB-KW
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional chitinase/lysozyme
    Including the following 2 domains:
    Chitinase (EC:3.2.1.14)
    Lysozyme (EC:3.2.1.17)
    OrganismiParthenocissus quinquefolia (Virginia creeper) (Hedera quinquefolia)
    Taxonomic identifieri3607 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeParthenocissus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›47›47Bifunctional chitinase/lysozymePRO_0000077052Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP23473.
    SMRiP23473. Positions 1-47.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    P23473-1 [UniParc]FASTAAdd to Basket

    « Hide

    GGIAIYWGQN GNEGTLTQTC NTGKYSYVNI AFLNKFGNGQ TPEINLA      47
    Length:47
    Mass (Da):5,040
    Last modified:November 1, 1991 - v1
    Checksum:i1D9DCF2E7E3A0F51
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei47 – 471

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P23473.
    SMRi P23473. Positions 1-47.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH18. Glycoside Hydrolase Family 18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Purification and N-terminal amino-acid sequence of a basic lysozyme from Parthenocissus quinquifolia cultured in vitro."
      Bernasconi P., Locher R., Pilet P.E., Jolles J., Jolles P.
      Biochim. Biophys. Acta 915:254-260(1987)
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiCHLY_PARTH
    AccessioniPrimary (citable) accession number: P23473
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Multifunctional enzyme

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3