Reviewed, UniProtKB/Swiss-Prot P00704 (LYSC_NUMME)

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

Numida meleagris (Helmeted guineafowl)

Taxonomic identifier

8996 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Numididae › Numida

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
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	lysozyme activity Inferred from electronic annotation. Source: EC
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_0000208868

Sites

Active site

35

1

Active site

52

1

Amino acid modifications

Disulfide bond

6 ↔ 127

Disulfide bond

30 ↔ 115

Disulfide bond

64 ↔ 80

Disulfide bond

76 ↔ 94

Secondary structure

1

.

.

.

.

.

.

.

.

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.

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.

.

.

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.

.

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.

.

.

129

Helix Strand Turn

Details...

Helix

5 – 14

10

Helix

25 – 36

12

Beta strand

43 – 45

3

Beta strand

51 – 53

3

Turn

54 – 57

4

Turn

60 – 63

4

Helix

80 – 84

5

Helix

89 – 101

13

Helix

104 – 107

4

Helix

109 – 114

6

Turn

115 – 117

3

Helix

121 – 124

4

Sequences

	Sequence		Length	Mass (Da)
	P00704-1 [UniParc]. Last modified March 1, 1992. Version 2. Checksum: 6D5917000E7D8CFD	FASTA	129	14,309
	10 20 30 40 50 60 KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS TDYGVLQINS 70 80 90 100 110 120 RWWCNDGRTP GSRNLCNIPC SALQSSDITA TANCAKKIVS DGNGMNAWVA WRKHCKGTDV RVWIKGCRL

References

[1]	"Amino acid sequence of guinea-hen egg-white lysozyme." Jolles J., van Leemputten E., Mouton A., Jolles P. Biochim. Biophys. Acta 257:497-510(1972) [PubMed: 5063251] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Egg white.
[2]	"1H-NMR study on the structure of lysozyme from guinea hen egg white." Fukamizo T., Ikeda Y., Torikata T., Araki T., Kuramoto M., Goto S. J. Biochem. 110:997-1003(1991) [PubMed: 1794991] [Abstract] Cited for: STRUCTURE BY NMR.
[3]	"Crystal structures of pheasant and guinea fowl egg-white lysozymes." Lescar J., Souchon H., Alzari P.M. Protein Sci. 3:788-798(1994) [PubMed: 8061608] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

LZUH. A00859.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FBI	X-ray	3.00	X/Y	1-129	[»]
1HHL	X-ray	1.90	A	1-129	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Phylogenomic databases

HOVERGEN

P00704.

Enzyme and pathway databases

BRENDA

3.2.1.17. 303472.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
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]

ProtoNet

Search...

Entry information

Entry name

LYSC_NUMME

Accession

Primary (citable) accession number: P00704

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)