ID   Q8XMY5_CLOPE            Unreviewed;      1173 AA.
AC   Q8XMY5;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   Name=nanJ {ECO:0000313|EMBL:BAB80259.1};
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB80259.1, ECO:0000313|Proteomes:UP000000818};
RN   [1] {ECO:0000313|EMBL:BAB80259.1, ECO:0000313|Proteomes:UP000000818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2] {ECO:0007829|PDB:2V72}
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 42-180 IN COMPLEX WITH CALCIUM
RP   AND GALACTOSE.
RX   PubMed=17850114; DOI=10.1021/bi701317g;
RA   Boraston A.B., Ficko-Blean E., Healey M.;
RT   "Carbohydrate recognition by a large sialidase toxin from Clostridium
RT   perfringens.";
RL   Biochemistry 46:11352-11360(2007).
CC   -!- INTERACTION:
CC       Q8XMY5; P26831: nagH; NbExp=2; IntAct=EBI-15722735, EBI-15722600;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
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DR   EMBL; BA000016; BAB80259.1; -; Genomic_DNA.
DR   RefSeq; WP_011009886.1; NC_003366.1.
DR   PDB; 2V72; X-ray; 2.25 A; A=41-180.
DR   PDBsum; 2V72; -.
DR   AlphaFoldDB; Q8XMY5; -.
DR   SMR; Q8XMY5; -.
DR   DIP; DIP-46267N; -.
DR   IntAct; Q8XMY5; 3.
DR   STRING; 195102.gene:10489810; -.
DR   CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR   CAZy; CBM40; Carbohydrate-Binding Module Family 40.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   KEGG; cpe:CPE0553; -.
DR   HOGENOM; CLU_273833_0_0_9; -.
DR   EvolutionaryTrace; Q8XMY5; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   CDD; cd08547; Type_II_cohesin; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.680; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR004124; Glyco_hydro_33_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR023364; Trans_sialidase_dom3.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02973; Sialidase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2V72}; Calcium {ECO:0007829|PDB:2V72};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Metal-binding {ECO:0007829|PDB:2V72};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          36..181
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          1088..1173
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         71
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         79
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         82
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         110
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         115
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         174
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:2V72"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:2V72"
SQ   SEQUENCE   1173 AA;  128782 MW;  276A1E0A43A788CA CRC64;
     MKSKKIIATL VASLVISNMG GYLVKANPNV NHKAVIIEDR QAIIETAIPQ SEMTASATSE
     EGQDPASSAI DGNINTMWHT KWNGSDALPQ SLSVNLGKAR KVSSIAITPR TSGNNGFITK
     YEIHAINNGV ETLVAEGTWE ENNLVKTVTF DSPIDAEEIK ITAIQGVGGF ASIAELNVYE
     IKGEVDEIAN YGNLKITKEE ERLNITGDLE KFSSLDEGTI VTRFNMNDTS IQSLIGLSDG
     NKANNYFSLY VSGGKVGYEL RRQEGNGDFN VHHSADVTFN KGINTLALKI EKGVGAKIFL
     NGSLVKTVSD PNIKFLNAIN LNSGFIGKTD RANGYNEYLF RGNIDFMNIY DKPVSDNYLL
     RKTGETKAPS EDSLLPDDVY KTQPVELFYP GYLESRGYRI PALETTKKGT VLASIDVRNN
     GDHDAPNNNI DVGIRRKEVN GEWEEGKVIL DYPGKSAAID TSLMSATIEE NGIEKERIFL
     IVTHFPEGYG FPNTEGGSGY KEIDGKYYFI LKDAQNNEYT VREDGIVYNS EGNQTDYVMK
     NDKTLIQNGE EVGNALLSNS PLKAVGTAHI EMIYSDDDGK TWSEPEDLNP GLKKEWMKFF
     GTAPGKGIQI KNGEHKGRLV FPIYYTNQNN FQSSAVIYSD DFGETWKLGE SPIDTASVSS
     ETVSSGTQLT ECQVVEMPNG QLKLFMRNTG SYTKIATSFD GGATWHDEVP EDTSLREPYC
     QLSVINYSGK INGKDAIIFS NPDASSRVNG SVKVGLINEN GTYDNGEPRY EFDWIYNKTV
     KPGSFAYSCL TELPDGNLGL FYEGEGAGRM AYTEFDLNYL KFNASEDSPS ASVQSIEVLD
     EDLAYNSGEE VSIKVNFNQL VSIIGDRKIT LDIGGVDVPL NMVNYEGKSS AIFKGTIPEG
     INQGNYEIKL KENNTLELNT VYNKVSTFNG LDNTGINVQI GELKTTVGNS TIKVNDEVQV
     GSAFEAILGI EGLNGDTEVY SAEYLFEYNV EAFILNEITS FNDSLFVKSK EVEPGKVRIL
     VASLGNEIEK DSDLVKVNLT PKISSELEVL GLTTALVGAG DGNTHDLELS SKEVKINEEA
     SGEIVVNPVQ NFEIPEINKK NVKLTWNAPI TTEGLEGYVI YKDGKKLSEV PAESTEFVVS
     KLNRHTIYNF KVAAKYSNGE LSAKESKTIR TAR
//