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Protein

Lysozyme g

Gene
N/A
Organism
Cygnus atratus (Black swan) (Anas atrata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeCygnus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

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 – 103Combined sources
Helixi18 – 214Combined sources
Helixi22 – 243Combined sources
Helixi30 – 4617Combined sources
Helixi49 – 5911Combined sources
Helixi63 – 7412Combined sources
Helixi75 – 773Combined sources
Turni92 – 954Combined sources
Turni98 – 1003Combined sources
Helixi110 – 13021Combined sources
Helixi136 – 14914Combined sources
Helixi151 – 1533Combined sources
Turni158 – 1636Combined sources
Helixi165 – 1673Combined sources
Helixi169 – 18113Combined sources
Turni182 – 1843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VPASKTIAER DLKAMDRYKT
60 70 80 90 100
IIKKVGEKLC VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS
110 120 130 140 150
HKPQGTWNGE VHITQGTTIL TDFIKRIQKK FPSWTKDQQL KGGISAYNAG
160 170 180
AGNVRSYARM DIGTTHDDYA NDVVARAQYY KQHGY
Length:185
Mass (Da):20,400
Last modified:July 21, 1986 - v1
Checksum:i22358F632C98342A
GO

Sequence databases

PIRiA00872. LZWSG.

Cross-referencesi

Sequence databases

PIRiA00872. LZWSG.

3D structure databases

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

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006299.

Miscellaneous databases

EvolutionaryTraceiP00717.

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.
ProtoNetiSearch...

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: February 4, 2015
This is version 83 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.