Lysozyme g - Cygnus atratus (Black swan)

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Reviewed, UniProtKB/Swiss-Prot P00717 (LYG_CYGAT)

Last modified June 16, 2009. Version 67. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier	8868 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › 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

185

Lysozyme g

PRO_0000193515

Sites

Active site

1

By similarity

Amino acid modifications

Disulfide bond

Disulfide bond

Secondary structure

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185

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P00717-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 22358F632C98342A
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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: 7378374] [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: 2302197] [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: 15299299] [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: 15299731] [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	[»]

ModBase

Protein family/group databases

CAZy

GH23. Glycoside Hydrolase Family 23.

Phylogenomic databases

HOVERGEN

Enzyme and pathway databases

BRENDA

3.2.1.17. 290484.

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

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:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents