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Q90VZ3

- LYG_PAROL

UniProt

Q90VZ3 - LYG_PAROL

Protein

Lysozyme g

Gene
N/A
Organism
Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Possesses lytic activity against M.lysodeikticus and several fish pathogenic bacteria.

    Catalytic activityi

    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.

    pH dependencei

    Optimum pH is 6.0.

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711By similarity
    Active sitei84 – 841By similarity

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. cytolysis Source: UniProtKB-KW
    3. defense response to bacterium Source: UniProtKB-KW
    4. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH23. Glycoside Hydrolase Family 23.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme g (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase
    OrganismiParalichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
    Taxonomic identifieri8255 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataCarangimorphariaePleuronectiformesPleuronectoideiParalichthyidaeParalichthys

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 195195Lysozyme gPRO_0000193520Add
    BLAST

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ90VZ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 23 family.Curated

    Phylogenomic databases

    HOVERGENiHBG006299.

    Family and domain databases

    InterProiIPR002152. Glyco_hydro_23.
    IPR023346. Lysozyme-like_dom.
    IPR008258. TGlycosylase-like_SLT.
    [Graphical view]
    PfamiPF01464. SLT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
    PRINTSiPR00749. LYSOZYMEG.
    SUPFAMiSSF53955. SSF53955. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q90VZ3-1 [UniParc]FASTAAdd to Basket

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    MSYGQIRLVE TSGASGATSQ QDNLGYSGVK ASHKMAEIDS GRMSKYKSKI    50
    NKVGQSYGIE PALIAAIISR ESRAGNQLKD GWGDWNPQRQ AYNAWGLMQV 100
    DVNPNGGGHT AVGGWDSEDH LRQATGILVT FIERIRTKFP GWSKEKQLKG 150
    GIAAYNMGDK NVHSYEGVDE NTTGRDYSND VTARAQWYRD NGYSG 195
    Length:195
    Mass (Da):21,385
    Last modified:December 1, 2001 - v1
    Checksum:i511DAF31876F662F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050591 Genomic DNA. Translation: BAB62407.1.
    AB050590 mRNA. Translation: BAB62406.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050591 Genomic DNA. Translation: BAB62407.1 .
    AB050590 mRNA. Translation: BAB62406.1 .

    3D structure databases

    ProteinModelPortali Q90VZ3.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH23. Glycoside Hydrolase Family 23.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG006299.

    Family and domain databases

    InterProi IPR002152. Glyco_hydro_23.
    IPR023346. Lysozyme-like_dom.
    IPR008258. TGlycosylase-like_SLT.
    [Graphical view ]
    Pfami PF01464. SLT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001065. Lysozyme_g. 1 hit.
    PRINTSi PR00749. LYSOZYMEG.
    SUPFAMi SSF53955. SSF53955. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein."
      Hikima J., Minagawa S., Hirono I., Aoki T.
      Biochim. Biophys. Acta 1520:35-44(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiLYG_PAROL
    AccessioniPrimary (citable) accession number: Q90VZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 45 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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