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Reviewed, UniProtKB/Swiss-Prot P00719 (LYG_STRCA)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lysozyme g
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase
    Goose-type lysozyme
OrganismStruthio camelus (Ostrich)
Taxonomic identifier8801 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeStruthioniformesStruthionidaeStruthio

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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.

Subcellular location

Secreted.

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 23 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Lysozyme g
PRO_0000193516

Sites

Active site731 By similarity
Active site861 By similarity

Amino acid modifications

Disulfide bond4 ↔ 60 By similarity
Disulfide bond18 ↔ 29 By similarity

Sequences

Sequence LengthMass (Da)Tools
P00719-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 02B78AF5D526B5DC

FASTA18520,563
        10         20         30         40         50         60 
RTGCYGDVNR VDTTGASCKS AKPEKLNYCG VAASRKIAER DLQSMDRYKA LIKKVGQKLC 

        70         80         90        100        110        120 
VDPAVIAGII SRESHAGKAL RNGWGDNGNG FGLMQVDRRS HKPVGEWNGE RHLMQGTEIL 

       130        140        150        160        170        180 
ISMIKAIQKK FPRWTKEQQL KGGISAYNAG PGNVRSYERM DIGTTHDDYA NDVVARAQYY 


KQHGY 

« Hide

References

[1]"Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose-type lysozyme."
Schoentgen F., Jolles J., Jolles P.
Eur. J. Biochem. 123:489-497(1982) [PubMed: 7075596] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Egg white.
[2]"The ostrich (Struthio camelus) egg-white lysozyme."
Jolles J., Perin J.-P., Jolles P.
Mol. Cell. Biochem. 17:39-44(1977) [PubMed: 904618] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-34.
Tissue: Egg white.

Cross-references

Sequence databases

PIRLZOSG. A00874.

3D structure databases

HSSPHSSP built from PDB template 153L based on UniProtKB P00718.
SMRP00719. Positions 1-185.
ModBaseSearch...

Protein family/group databases

CAZyGH23. Glycoside Hydrolase Family 23.

Phylogenomic databases

HOVERGENP00719.

Enzyme and pathway databases

BRENDA3.2.1.17. 39275.

Family and domain databases

InterProIPR002152. Glyco_hydro_23.
IPR008258. Lytic_TGlycosylase-like_cat.
[Graphical view]
PfamPF01464. SLT. 1 hit.
[Graphical view]
PIRSFPIRSF001065. Lysozyme_g. 1 hit.
PRINTSPR00749. LYSOZYMEG.
ProtoNetSearch...

Entry information

Entry nameLYG_STRCA
AccessionPrimary (citable) accession number: P00719
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents