P00717 (LYG_CYGAT) Reviewed, UniProtKB/Swiss-Prot

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	Cygnus atratus (Black swan) (Anas atrata)
Taxonomic identifier	8868 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Cygnus

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_0000193515

Sites

Active site

73

1

By similarity

Amino acid modifications

Disulfide bond

4 ↔ 60

Disulfide bond

18 ↔ 29

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

185

Helix Strand Turn

Details...

Helix

8 – 10

3

Helix

18 – 21

4

Helix

22 – 24

3

Helix

30 – 46

17

Helix

49 – 59

11

Helix

63 – 74

12

Helix

75 – 77

3

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 – 181

13

Turn

182 – 184

3

Sequences

	Sequence		Length	Mass (Da)
	P00717 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 22358F632C98342A	FASTA	185	20,400
	10 20 30 40 50 60 RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VPASKTIAER DLKAMDRYKT IIKKVGEKLC 70 80 90 100 110 120 VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS HKPQGTWNGE VHITQGTTIL 130 140 150 160 170 180 TDFIKRIQKK FPSWTKDQQL KGGISAYNAG AGNVRSYARM DIGTTHDDYA NDVVARAQYY KQHGY

References

[1]	"Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan." Simpson R.J., Begg G.S., Dorow D.S., Morgan F.J. Biochemistry 19:1814-1819(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Egg white.
[2]	"Internal amino acid sequencing of proteins by in situ cyanogen bromide cleavage in polyacrylamide gels." Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J. Biochem. Biophys. Res. Commun. 166:139-145(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 46-68 AND 95-111.
[3]	"A strategy for rapid and effective refinement applied to black swan lysozyme." Zao Z., Esnouf R., Isaacs N., Stuart D. Acta Crystallogr. D 51:331-336(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[4]	"Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases." Karlsen S., Hough E., Rao Z.H., Isaacs N.W. Acta Crystallogr. D 52:105-114(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).

Cross-references

Sequence databases

PIR

LZWSG. A00872.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GBS	X-ray	1.50	A	1-185	[»]
1LSP	X-ray	2.45	A	1-185	[»]

ProteinModelPortal

P00717.

SMR

P00717. Positions 1-185.

ModBase

Search...

Protein family/group databases

CAZy

GH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG006299.

Family and domain databases

InterPro

IPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. Lytic_TGlycosylase-like_cat.
[Graphical view]

Pfam

PF01464. SLT. 1 hit.
[Graphical view]

PIRSF

PIRSF001065. Lysozyme_g. 1 hit.

PRINTS

PR00749. LYSOZYMEG.

SUPFAM

SSF53955. SSF53955. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P00717.

Entry information

Entry name

LYG_CYGAT

Accession

Primary (citable) accession number: P00717

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program