ID LYS1_MUSDO Reviewed; 141 AA. AC Q7YT16; Q7M437; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Lysozyme 1; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase 1; DE Flags: Precursor; OS Musca domestica (House fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea; OC Muscidae; Musca. OX NCBI_TaxID=7370; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Midgut epithelium; RA Chimoy P., Marana S.R., Ferreira C., Terra W.R.; RT "Cloning, sequencing and characterization of a digestive lysozyme from RT Musca domestica midgut."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 20-141. RC TISSUE=Larva; RX PubMed=8690715; DOI=10.1093/oxfordjournals.jbchem.a124943; RA Ito Y., Nakamura M., Hotani T., Imoto T.; RT "Insect lysozyme from house fly (Musca domestica) larvae: possible RT digestive function based on sequence and enzymatic properties."; RL J. Biochem. 118:546-551(1995). CC -!- FUNCTION: May not function as a self-defense protein, but as a CC digestive enzyme, probably in the gut of the insect body. Inactive CC towards Micrococcus luteus. Active toward glycol chitin. 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 Active at acidic pHs. Inactive above pH 7.; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. CC {ECO:0000255|PROSITE-ProRule:PRU00680}. 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 EMBL; AY344589; AAQ20048.1; -; mRNA. DR PIR; PC4062; PC4062. DR RefSeq; NP_001295901.1; NM_001308972.1. DR RefSeq; XP_005185827.1; XM_005185770.3. DR RefSeq; XP_005185835.1; XM_005185778.3. DR RefSeq; XP_019891658.1; XM_020036099.1. DR RefSeq; XP_019893133.1; XM_020037574.1. DR RefSeq; XP_019893140.1; XM_020037581.1. DR RefSeq; XP_019893141.1; XM_020037582.1. DR PDB; 2FBD; X-ray; 1.90 A; A/B=20-141. DR PDB; 2H5Z; X-ray; 1.92 A; A/B=20-141. DR PDBsum; 2FBD; -. DR PDBsum; 2H5Z; -. DR AlphaFoldDB; Q7YT16; -. DR SMR; Q7YT16; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR EnsemblMetazoa; MDOA012752-RB; MDOA012752-PB; MDOA012752. DR EnsemblMetazoa; MDOA012752-RD; MDOA012752-PD; MDOA012752. DR EnsemblMetazoa; MDOA012752-RE; MDOA012752-PE; MDOA012752. DR EnsemblMetazoa; MDOA012964-RB; MDOA012964-PB; MDOA012964. DR EnsemblMetazoa; MDOA013199-RA; MDOA013199-PA; MDOA013199. DR GeneID; 101892974; -. DR GeneID; 101893151; -. DR GeneID; 101894169; -. DR GeneID; 101894601; -. DR GeneID; 101895951; -. DR KEGG; mde:101892974; -. DR KEGG; mde:101893151; -. DR KEGG; mde:101895951; -. DR VEuPathDB; VectorBase:MDOA012752; -. DR VEuPathDB; VectorBase:MDOA012964; -. DR VEuPathDB; VectorBase:MDOA013199; -. DR eggNOG; ENOG502S1S1; Eukaryota. DR OrthoDB; 5361006at2759; -. DR BRENDA; 3.2.1.17; 3486. DR EvolutionaryTrace; Q7YT16; -. DR Proteomes; UP000095301; Unassembled WGS sequence. DR Proteomes; UP000694905; Unplaced. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR CDD; cd16899; LYZ_C_invert; 1. DR Gene3D; 1.10.530.10; -; 1. DR InterPro; IPR001916; Glyco_hydro_22. DR InterPro; IPR019799; Glyco_hydro_22_CS. DR InterPro; IPR000974; Glyco_hydro_22_lys. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR PANTHER; PTHR11407:SF36; GEO02684P1-RELATED; 1. DR PANTHER; PTHR11407; LYSOZYME C; 1. DR Pfam; PF00062; Lys; 1. DR PRINTS; PR00137; LYSOZYME. DR PRINTS; PR00135; LYZLACT. DR SMART; SM00263; LYZ1; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1. DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Glycosidase; Hydrolase; Reference proteome; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:8690715" FT CHAIN 20..141 FT /note="Lysozyme 1" FT /id="PRO_0000018508" FT DOMAIN 20..141 FT /note="C-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 51 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT ACT_SITE 69 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 25..140 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 46..130 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 81..97 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 93..111 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT HELIX 24..33 FT /evidence="ECO:0007829|PDB:2FBD" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:2FBD" FT HELIX 41..52 FT /evidence="ECO:0007829|PDB:2FBD" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:2FBD" FT TURN 71..74 FT /evidence="ECO:0007829|PDB:2FBD" FT TURN 77..80 FT /evidence="ECO:0007829|PDB:2FBD" FT HELIX 97..101 FT /evidence="ECO:0007829|PDB:2FBD" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:2FBD" FT HELIX 106..119 FT /evidence="ECO:0007829|PDB:2FBD" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:2FBD" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:2FBD" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:2FBD" SQ SEQUENCE 141 AA; 15733 MW; C640C6407AD80F0E CRC64; MKFFIVLVAA LALAAPAMGK TFTRCSLARE MYALGVPKSE LPQWTCIAEH ESSYRTNVVG PTNSNGSNDY GIFQINNYYW CQPSNGRFSY NECHLSCDAL LTDNISNSVT CARKIKSQQG WTAWSTWKYC SGSLPSINDC F //