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P00717

- LYG_CYGAT

UniProt

P00717 - LYG_CYGAT

Protein

Lysozyme g

Gene
N/A
Organism
Cygnus atratus (Black swan) (Anas atrata)
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 – 731By 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
    Goose-type lysozyme
    OrganismiCygnus atratus (Black swan) (Anas atrata)
    Taxonomic identifieri8868 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeCygnus

    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_0000193515Add
    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
    Helixi30 – 4617
    Helixi49 – 5911
    Helixi63 – 7412
    Helixi75 – 773
    Turni92 – 954
    Turni98 – 1003
    Helixi110 – 13021
    Helixi136 – 14914
    Helixi151 – 1533
    Turni158 – 1636
    Helixi165 – 1673
    Helixi169 – 18113
    Turni182 – 1843

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GBSX-ray1.50A1-185[»]
    1LSPX-ray2.45A1-185[»]
    ProteinModelPortaliP00717.
    SMRiP00717. Positions 1-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00717.

    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.

    P00717-1 [UniParc]FASTAAdd to Basket

    « Hide

    RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VPASKTIAER DLKAMDRYKT    50
    IIKKVGEKLC VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS 100
    HKPQGTWNGE VHITQGTTIL TDFIKRIQKK FPSWTKDQQL KGGISAYNAG 150
    AGNVRSYARM DIGTTHDDYA NDVVARAQYY KQHGY 185
    Length:185
    Mass (Da):20,400
    Last modified:July 21, 1986 - v1
    Checksum:i22358F632C98342A
    GO

    Sequence databases

    PIRiA00872. LZWSG.

    Cross-referencesi

    Sequence databases

    PIRi A00872. LZWSG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GBS X-ray 1.50 A 1-185 [» ]
    1LSP X-ray 2.45 A 1-185 [» ]
    ProteinModelPortali P00717.
    SMRi P00717. 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 P00717.

    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 the goose-type lysozyme from the egg white of the black swan."
      Simpson R.J., Begg G.S., Dorow D.S., Morgan F.J.
      Biochemistry 19:1814-1819(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Egg white.
    2. "Internal amino acid sequencing of proteins by in situ cyanogen bromide cleavage in polyacrylamide gels."
      Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J.
      Biochem. Biophys. Res. Commun. 166:139-145(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 46-68 AND 95-111.
    3. "A strategy for rapid and effective refinement applied to black swan lysozyme."
      Zao Z., Esnouf R., Isaacs N., Stuart D.
      Acta Crystallogr. D 51:331-336(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    4. "Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases."
      Karlsen S., Hough E., Rao Z.H., Isaacs N.W.
      Acta Crystallogr. D 52:105-114(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).

    Entry informationi

    Entry nameiLYG_CYGAT
    AccessioniPrimary (citable) accession number: P00717
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 79 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