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Protein

Lysozyme g

Gene
N/A
Organism
Anser anser anser (Western greylag goose)
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 – 731
Active sitei86 – 861

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.17. 360.

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 greylag goose)
Taxonomic identifieri8844 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnser

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 – 103Combined sources
Helixi18 – 214Combined sources
Helixi22 – 243Combined sources
Helixi31 – 4010Combined sources
Helixi42 – 465Combined sources
Helixi49 – 5911Combined sources
Helixi63 – 7412Combined sources
Turni75 – 795Combined sources
Turni92 – 954Combined sources
Turni98 – 1003Combined sources
Helixi110 – 13021Combined sources
Helixi136 – 14914Combined sources
Helixi151 – 1533Combined sources
Turni158 – 1636Combined sources
Helixi165 – 1673Combined sources
Helixi169 – 18214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VSASKKIAER DLQAMDRYKT
60 70 80 90 100
IIKKVGEKLC VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS
110 120 130 140 150
HKPQGTWNGE VHITQGTTIL INFIKTIQKK FPSWTKDQQL KGGISAYNAG
160 170 180
AGNVRSYARM DIGTTHDDYA NDVVARAQYY KQHGY
Length:185
Mass (Da):20,373
Last modified:July 21, 1986 - v1
Checksum:i0B2F0C9B2A66C324
GO

Sequence databases

PIRiA00873. LZGSG.

Cross-referencesi

Sequence databases

PIRiA00873. LZGSG.

3D structure databases

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

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006299.

Enzyme and pathway databases

BRENDAi3.2.1.17. 360.

Miscellaneous databases

EvolutionaryTraceiP00718.

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 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: April 1, 2015
This is version 80 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.