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P49663 (LYSC_PHAVE) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Lysozyme C

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
Gene names
Name:LYZ
OrganismPhasianus versicolor (Green pheasant)
Taxonomic identifier9055 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaePhasianus

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents By similarity.

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.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted.

Miscellaneous

Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 130130Lysozyme C
PRO_0000208871

Sites

Active site361 By similarity
Active site531 By similarity

Amino acid modifications

Disulfide bond7 ↔ 128 By similarity
Disulfide bond31 ↔ 116 By similarity
Disulfide bond65 ↔ 81 By similarity
Disulfide bond77 ↔ 95 By similarity

Sequences

Sequence LengthMass (Da)Tools
P49663-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9BA9EDD7625B48F4

FASTA13014,314
        10         20         30         40         50         60 
GKVYGRCELA AAMKRMGLDN YRGYSLGNWV CAAKFESNFN TGATNRNTDG STDYGILQIN 

        70         80         90        100        110        120 
SRWWCNDGRT PGSKNLCHIP CSALLSSDIT ASVNCAKKIV SDGDGMNAWV AWRKHCKGTD 

       130 
VNVWIRGCRL 

« Hide

References

[1]Araki T., Kuramoto M., Torikata T.
Submitted (OCT-1993) to the PIR data bank
Cited for: PROTEIN SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRJU0178.

3D structure databases

ProteinModelPortalP49663.
SMRP49663. Positions 2-130.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Phylogenomic databases

HOVERGENHBG052297.

Enzyme and pathway databases

BRENDA3.2.1.17. 269189.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC_PHAVE
AccessionPrimary (citable) accession number: P49663
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: August 10, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families