ID L5M343_MYODS Unreviewed; 304 AA.
AC L5M343;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN ORFNames=MDA_GLEAN10026174 {ECO:0000313|EMBL:ELK32680.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK32680.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC (2->8)- glycosidic linkages of terminal sialic acid residues in
CC oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC synthetic substrates.; EC=3.2.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000427};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
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DR EMBL; KB105166; ELK32680.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M343; -.
DR eggNOG; ENOG502QSFT; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR PANTHER; PTHR10628:SF22; SIALIDASE-4; 1.
DR Pfam; PF13088; BNR_2; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 3: Inferred from homology;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 68..241
FT /note="Sialidase"
FT /evidence="ECO:0000259|Pfam:PF13088"
SQ SEQUENCE 304 AA; 33275 MW; 51F6EB6D7552DEA9 CRC64;
MIRTGGSRSL EHWELRTWPL PSPRRGKLFQ SDFSATEQGT QQAFLVPWLV RRTLYTVLPP
GDLSSLGKPG PVKTDWATFA VGPGHGIQLR SGRLLVPAYT YHVDRRECFG KICRTSPHAF
TFYSDDHGQT WRHGGLLSNL RSGECQLAVV DGGRAGSVLY CNARSPLGSR VQALSTDEGT
SFLPGELVPT LAETARGCQG SILGFPAPHS NRPGDEGWSP LDPHSWTEPW VIYQGPSGYS
DLASIGPTPE GSLTFACLYE SGTRVSYEEI SFCVFSLREV LENVLPGPEP TGLGNKPWEQ
CWPS
//
