Reviewed, UniProtKB/Swiss-Prot P22910 (LYSC_CHRAM)

Names and origin

Protein names

Recommended name:
    Lysozyme C
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C

Gene names

Name:

LYZ

Organism

Chrysolophus amherstiae (Lady Amherst's pheasant)

Taxonomic identifier

9088 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Chrysolophus

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.
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

Keywords
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 129	129	Lysozyme C		PRO_0000208861
Sites
	Active site	35	1	By similarity
	Active site	52	1	By similarity
Amino acid modifications
	Disulfide bond	6 ↔ 127		By similarity
	Disulfide bond	30 ↔ 115		By similarity
	Disulfide bond	64 ↔ 80		By similarity
	Disulfide bond	76 ↔ 94		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22910-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: E0A6D33123F39CF2	FASTA	129	14,311
	10 20 30 40 50 60 KVYGRCELAA AMKRLGLDNY RGYSLGNWVC AAKFESNFNT HATNRNTDGS TDYGILQINS 70 80 90 100 110 120 RWWCNDGRTP GSRNLCHIPC SALLSSDITA SVNCAKKIVS DGNGMNAWVA WRNRCKGTDV NAWTRGCRL

References

[1]	"The amino acid sequence of Lady Amherst's pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes." Araki T., Kuramoto M., Torikata T. Agric. Biol. Chem. 54:2299-2308(1990) [PubMed: 1368578] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Egg white.

Cross-references

Sequence databases
PIR	JH0211.
3D structure databases
HSSP	HSSP built from PDB template 1UIB based on UniProtKB P00698.
SMR	P22910. Positions 1-129.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P22910.
Family and domain databases
InterPro	IPR001916. Glyco_hydro_22. IPR000974. Glyco_hydro_22_lys. [Graphical view]
Pfam	PF00062. Lys. 1 hit. [Graphical view]
PRINTS	PR00137. LYSOZYME. PR00135. LYZLACT.
SMART	SM00263. LYZ1. 1 hit. [Graphical view]
PROSITE	PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

LYSC_CHRAM

Accession

Primary (citable) accession number: P22910

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	November 4, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)