ID   LYG_PAROL               Reviewed;         195 AA.
AC   Q90VZ3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Lysozyme g;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
OS   Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC   Paralichthys.
OX   NCBI_TaxID=8255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11470157; DOI=10.1016/s0167-4781(01)00248-2;
RA   Hikima J., Minagawa S., Hirono I., Aoki T.;
RT   "Molecular cloning, expression and evolution of the Japanese flounder
RT   goose-type lysozyme gene, and the lytic activity of its recombinant
RT   protein.";
RL   Biochim. Biophys. Acta 1520:35-44(2001).
CC   -!- FUNCTION: Possesses lytic activity against M.lysodeikticus and several
CC       fish pathogenic bacteria.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0.;
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11470157}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family. {ECO:0000305}.
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DR   EMBL; AB050591; BAB62407.1; -; Genomic_DNA.
DR   EMBL; AB050590; BAB62406.1; -; mRNA.
DR   AlphaFoldDB; Q90VZ3; -.
DR   SMR; Q90VZ3; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   InterPro; IPR002152; Glyco_hydro_23.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF01464; SLT; 1.
DR   PIRSF; PIRSF001065; Lysozyme_g; 1.
DR   PRINTS; PR00749; LYSOZYMEG.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase.
FT   CHAIN           1..195
FT                   /note="Lysozyme g"
FT                   /id="PRO_0000193520"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   195 AA;  21385 MW;  511DAF31876F662F CRC64;
     MSYGQIRLVE TSGASGATSQ QDNLGYSGVK ASHKMAEIDS GRMSKYKSKI NKVGQSYGIE
     PALIAAIISR ESRAGNQLKD GWGDWNPQRQ AYNAWGLMQV DVNPNGGGHT AVGGWDSEDH
     LRQATGILVT FIERIRTKFP GWSKEKQLKG GIAAYNMGDK NVHSYEGVDE NTTGRDYSND
     VTARAQWYRD NGYSG