ID A0A3B3DE77_ORYME Unreviewed; 186 AA.
AC A0A3B3DE77;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lysozyme g {ECO:0000256|ARBA:ARBA00016485, ECO:0000256|PIRNR:PIRNR001065};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|PIRNR:PIRNR001065};
GN ORFNames=FQA47_011274 {ECO:0000313|EMBL:KAF6730280.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000027705.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000027705.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|EMBL:KAF6730280.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6730280.1};
RX PubMed=32938378;
RA Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT melastigma).";
RL BMC Genomics 21:0-0(0).
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; Evidence={ECO:0000256|ARBA:ARBA00000632,
CC ECO:0000256|PIRNR:PIRNR001065};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family.
CC {ECO:0000256|ARBA:ARBA00008902, ECO:0000256|PIRNR:PIRNR001065}.
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DR EMBL; WKFB01000241; KAF6730280.1; -; Genomic_DNA.
DR Ensembl; ENSOMET00000001275.1; ENSOMEP00000027705.1; ENSOMEG00000010329.1.
DR GeneTree; ENSGT00390000017614; -.
DR OMA; AVIDCWC; -.
DR OrthoDB; 2964133at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR Proteomes; UP000646548; Unassembled WGS sequence.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001065};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001065};
KW Reference proteome {ECO:0000313|Proteomes:UP000646548}.
FT DOMAIN 49..162
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT ACT_SITE 70
FT /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
SQ SEQUENCE 186 AA; 19908 MW; 5624FF0EA6AB6367 CRC64;
MNANINNVST TGASAQTARQ DRLGVSGVAA SHAMAKTDAG RMARYKNIIK ATGQKHGVDP
ALIAGIISRE SRAGNVLQNG WGDHGNAWGL MQVDVNPHGG GHRAVGAWDS EEHLSQATGI
LTHFIQRIEK KFPQCTKEQQ LKGGIAAYNA GDGRVHSCEN VDANTTGKDY ANDVVARAQW
YKQQGY
//
