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P00704

- LYSC_NUMME

UniProt

P00704 - LYSC_NUMME

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Protein

Lysozyme C

Gene

LYZ

Organism
Numida meleagris (Helmeted guineafowl)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351
Active sitei52 – 521

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
OrganismiNumida meleagris (Helmeted guineafowl)
Taxonomic identifieri8996 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesNumididaeNumida

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Lysozyme CPRO_0000208868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 127
Disulfide bondi30 ↔ 115
Disulfide bondi64 ↔ 80
Disulfide bondi76 ↔ 94

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00704.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Helixi25 – 3612Combined sources
Beta strandi37 – 393Combined sources
Beta strandi43 – 453Combined sources
Beta strandi51 – 533Combined sources
Turni54 – 574Combined sources
Turni60 – 634Combined sources
Helixi80 – 845Combined sources
Helixi89 – 10113Combined sources
Helixi104 – 1074Combined sources
Helixi109 – 1146Combined sources
Turni115 – 1173Combined sources
Helixi121 – 1244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBIX-ray3.00X/Y1-129[»]
1HHLX-ray1.90A1-129[»]
ProteinModelPortaliP00704.
SMRiP00704. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00704.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00704-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS
60 70 80 90 100
TDYGVLQINS RWWCNDGRTP GSRNLCNIPC SALQSSDITA TANCAKKIVS
110 120
DGNGMNAWVA WRKHCKGTDV RVWIKGCRL
Length:129
Mass (Da):14,309
Last modified:March 1, 1992 - v2
Checksum:i6D5917000E7D8CFD
GO

Sequence databases

PIRiA00859. LZUH.

Cross-referencesi

Sequence databases

PIRi A00859. LZUH.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FBI X-ray 3.00 X/Y 1-129 [» ]
1HHL X-ray 1.90 A 1-129 [» ]
ProteinModelPortali P00704.
SMRi P00704. Positions 1-129.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P00704.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052297.

Miscellaneous databases

EvolutionaryTracei P00704.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiLYSC_NUMME
AccessioniPrimary (citable) accession number: P00704
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: November 26, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3