ID   LYG_ANSAN               Reviewed;         185 AA.
AC   P00718;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Lysozyme g;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
DE   AltName: Full=Goose-type lysozyme;
OS   Anser anser anser (Western greylag goose).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anserinae; Anser.
OX   NCBI_TaxID=8844;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=Embden breed; TISSUE=Egg white;
RA   Simpson R.J., Morgan F.J.;
RT   "Complete amino acid sequence of Embden goose (Anser anser) egg-white
RT   lysozyme.";
RL   Biochim. Biophys. Acta 744:349-351(1983).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=6866082; DOI=10.1038/303828a0;
RA   Gruetter M.G., Weaver L.H., Matthews B.W.;
RT   "Goose lysozyme structure: an evolutionary link between hen and
RT   bacteriophage lysozymes?";
RL   Nature 303:828-831(1983).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=7823320; DOI=10.1016/s0022-2836(95)80038-7;
RA   Weaver L.H., Gruetter M.G., Matthews B.W.;
RT   "The refined structures of goose lysozyme and its complex with a bound
RT   trisaccharide show that the 'goose-type' lysozymes lack a catalytic
RT   aspartate residue.";
RL   J. Mol. Biol. 245:54-68(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Shows preference for N-acetylmuramic acid residues that
CC       are substituted with a peptide moiety. It acts only as a
CC       glycanohydrolase.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A00873; LZGSG.
DR   PDB; 153L; X-ray; 1.60 A; A=1-185.
DR   PDB; 154L; X-ray; 1.60 A; A=1-185.
DR   PDBsum; 153L; -.
DR   PDBsum; 154L; -.
DR   AlphaFoldDB; P00718; -.
DR   SMR; P00718; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   BRENDA; 3.2.1.17; 360.
DR   EvolutionaryTrace; P00718; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd01021; GEWL; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR002152; Glyco_hydro_23.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR31698:SF8; LYSOZYME G; 1.
DR   PANTHER; PTHR31698; LYSOZYME G FAMILY MEMBER; 1.
DR   Pfam; PF01464; SLT; 1.
DR   PIRSF; PIRSF001065; Lysozyme_g; 1.
DR   PRINTS; PR00749; LYSOZYMEG.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted.
FT   CHAIN           1..185
FT                   /note="Lysozyme g"
FT                   /id="PRO_0000193513"
FT   ACT_SITE        73
FT   ACT_SITE        86
FT   DISULFID        4..60
FT   DISULFID        18..29
FT   HELIX           8..10
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           18..21
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           31..40
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           42..46
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           49..59
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           63..74
FT                   /evidence="ECO:0007829|PDB:153L"
FT   TURN            75..79
FT                   /evidence="ECO:0007829|PDB:153L"
FT   TURN            92..95
FT                   /evidence="ECO:0007829|PDB:153L"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           110..130
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           136..149
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:153L"
FT   TURN            158..163
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:153L"
FT   HELIX           169..182
FT                   /evidence="ECO:0007829|PDB:153L"
SQ   SEQUENCE   185 AA;  20373 MW;  0B2F0C9B2A66C324 CRC64;
     RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VSASKKIAER DLQAMDRYKT IIKKVGEKLC
     VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS HKPQGTWNGE VHITQGTTIL
     INFIKTIQKK FPSWTKDQQL KGGISAYNAG AGNVRSYARM DIGTTHDDYA NDVVARAQYY
     KQHGY
//