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P00718

- LYG_ANSAN

UniProt

P00718 - LYG_ANSAN

Protein

Lysozyme g

Gene
N/A
Organism
Anser anser anser (Western graylag goose)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei73 – 731
    Active sitei86 – 861

    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
    Goose-type lysozyme
    OrganismiAnser anser anser (Western graylag goose)
    Taxonomic identifieri8844 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnser

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 185185Lysozyme gPRO_0000193513Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi4 ↔ 60
    Disulfide bondi18 ↔ 29

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103
    Helixi18 – 214
    Helixi22 – 243
    Helixi31 – 4010
    Helixi42 – 465
    Helixi49 – 5911
    Helixi63 – 7412
    Turni75 – 795
    Turni92 – 954
    Turni98 – 1003
    Helixi110 – 13021
    Helixi136 – 14914
    Helixi151 – 1533
    Turni158 – 1636
    Helixi165 – 1673
    Helixi169 – 18214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    153LX-ray1.60A1-185[»]
    154LX-ray1.60A1-185[»]
    ProteinModelPortaliP00718.
    SMRiP00718. Positions 1-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00718.

    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.

    P00718-1 [UniParc]FASTAAdd to Basket

    « Hide

    RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VSASKKIAER DLQAMDRYKT    50
    IIKKVGEKLC VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS 100
    HKPQGTWNGE VHITQGTTIL INFIKTIQKK FPSWTKDQQL KGGISAYNAG 150
    AGNVRSYARM DIGTTHDDYA NDVVARAQYY KQHGY 185
    Length:185
    Mass (Da):20,373
    Last modified:July 21, 1986 - v1
    Checksum:i0B2F0C9B2A66C324
    GO

    Sequence databases

    PIRiA00873. LZGSG.

    Cross-referencesi

    Sequence databases

    PIRi A00873. LZGSG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    153L X-ray 1.60 A 1-185 [» ]
    154L X-ray 1.60 A 1-185 [» ]
    ProteinModelPortali P00718.
    SMRi P00718. Positions 1-185.
    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.

    Miscellaneous databases

    EvolutionaryTracei P00718.

    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. "Complete amino acid sequence of Embden goose (Anser anser) egg-white lysozyme."
      Simpson R.J., Morgan F.J.
      Biochim. Biophys. Acta 744:349-351(1983)
      Cited for: PROTEIN SEQUENCE.
      Strain: Embden breed.
      Tissue: Egg white.
    2. "Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?"
      Gruetter M.G., Weaver L.H., Matthews B.W.
      Nature 303:828-831(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    3. "The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the 'goose-type' lysozymes lack a catalytic aspartate residue."
      Weaver L.H., Gruetter M.G., Matthews B.W.
      J. Mol. Biol. 245:54-68(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

    Entry informationi

    Entry nameiLYG_ANSAN
    AccessioniPrimary (citable) accession number: P00718
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    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 programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Shows preference for N-acetylmuramic acid residues that are substituted with a peptide moiety. It acts only as a glycanohydrolase.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    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