Reviewed, UniProtKB/Swiss-Prot P00718 (LYG_ANSAN)

Names and origin

Protein names	Recommended name:     Lysozyme g     EC=3.2.1.17 Alternative name(s):     1,4-beta-N-acetylmuramidase     Goose-type lysozyme
Organism	Anser anser anser (Western graylag goose)
Taxonomic identifier	8844 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anser

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Secreted
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 peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 185

185

Lysozyme g

PRO_0000193513

Sites

Active site

73

1

Active site

86

1

Amino acid modifications

Disulfide bond

4 ↔ 60

Disulfide bond

18 ↔ 29

Secondary structure

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185

Helix Strand Turn

Details...

Helix

8 – 10

3

Helix

18 – 21

4

Helix

22 – 24

3

Helix

31 – 40

10

Helix

42 – 46

5

Helix

49 – 59

11

Helix

63 – 74

12

Turn

75 – 79

5

Turn

92 – 95

4

Turn

98 – 100

3

Helix

110 – 130

21

Helix

136 – 149

14

Helix

151 – 153

3

Turn

158 – 163

6

Helix

165 – 167

3

Helix

169 – 182

14

Sequences

	Sequence		Length	Mass (Da)
	P00718-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0B2F0C9B2A66C324	FASTA	185	20,373
	10 20 30 40 50 60 RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VSASKKIAER DLQAMDRYKT IIKKVGEKLC 70 80 90 100 110 120 VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS HKPQGTWNGE VHITQGTTIL 130 140 150 160 170 180 INFIKTIQKK FPSWTKDQQL KGGISAYNAG AGNVRSYARM DIGTTHDDYA NDVVARAQYY KQHGY

References

[1]	"Complete amino acid sequence of Embden goose (Anser anser) egg-white lysozyme." Simpson R.J., Morgan F.J. Biochim. Biophys. Acta 744:349-351(1983) Cited for: PROTEIN SEQUENCE. Strain: Embden breed. Tissue: Egg white.
[2]	"Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?" Gruetter M.G., Weaver L.H., Matthews B.W. Nature 303:828-831(1983) [PubMed: 6866082] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[3]	"The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the 'goose-type' lysozymes lack a catalytic aspartate residue." Weaver L.H., Gruetter M.G., Matthews B.W. J. Mol. Biol. 245:54-68(1995) [PubMed: 7823320] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Cross-references

Sequence databases

PIR

LZGSG. A00873.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
153L	X-ray	1.60	A	1-185	[»]
154L	X-ray	1.60	A	1-185	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH23. Glycoside Hydrolase Family 23.

Phylogenomic databases

HOVERGEN

P00718.

Family and domain databases

InterPro

IPR002152. Glyco_hydro_23.
IPR008258. Lytic_TGlycosylase-like_cat.
[Graphical view]

Pfam

PF01464. SLT. 1 hit.
[Graphical view]

PIRSF

PIRSF001065. Lysozyme_g. 1 hit.

PRINTS

PR00749. LYSOZYMEG.

ProtoNet

Search...

Entry information

Entry name

LYG_ANSAN

Accession

Primary (citable) accession number: P00718

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)