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Protein

Lysozyme C

Gene

LYZ

Organism
Chrysolophus amherstiae (Lady Amherst's pheasant) (Phasianus amherstiae)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

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.

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)DescriptionActionsGraphical viewLength
Active sitei35PROSITE-ProRule annotation1
Active sitei52PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
OrganismiChrysolophus amherstiae (Lady Amherst's pheasant) (Phasianus amherstiae)
Taxonomic identifieri9088 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeChrysolophus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002088611 – 129Lysozyme CAdd BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi6 ↔ 127PROSITE-ProRule annotation
Disulfide bondi30 ↔ 115PROSITE-ProRule annotation
Disulfide bondi64 ↔ 80PROSITE-ProRule annotation
Disulfide bondi76 ↔ 94PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP22910.
SMRiP22910.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiView protein in InterPro
IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
PfamiView protein in Pfam
PF00062. Lys. 1 hit.
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiView protein in SMART
SM00263. LYZ1. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiView protein in PROSITE
PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P22910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KVYGRCELAA AMKRLGLDNY RGYSLGNWVC AAKFESNFNT HATNRNTDGS
60 70 80 90 100
TDYGILQINS RWWCNDGRTP GSRNLCHIPC SALLSSDITA SVNCAKKIVS
110 120
DGNGMNAWVA WRNRCKGTDV NAWTRGCRL
Length:129
Mass (Da):14,311
Last modified:August 1, 1991 - v1
Checksum:iE0A6D33123F39CF2
GO

Sequence databases

PIRiJH0211.

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 one 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.

Entry informationi

Entry nameiLYSC_CHRAM
AccessioniPrimary (citable) accession number: P22910
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: March 15, 2017
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families