ID   NANH_CLOPF              Reviewed;         382 AA.
AC   P10481;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Sialidase;
DE            EC=3.2.1.18;
DE   AltName: Full=Neuraminidase;
GN   Name=nanH;
OS   Clostridium perfringens.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 8-27.
RC   STRAIN=A99;
RX   PubMed=2901987; DOI=10.1016/0014-5793(88)80219-9;
RA   Roggentin P., Rothe B., Lottspeich F., Schauer R.;
RT   "Cloning and sequencing of a Clostridium perfringens sialidase gene.";
RL   FEBS Lett. 238:31-34(1988).
CC   -!- FUNCTION: Sialidases have been suggested to be pathogenic factors in
CC       microbial infections.
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://www.worthington-biochem.com/NEUP/";
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DR   EMBL; Y00963; CAA68780.1; -; Genomic_DNA.
DR   PIR; S01339; S01339.
DR   AlphaFoldDB; P10481; -.
DR   SMR; P10481; -.
DR   BindingDB; P10481; -.
DR   ChEMBL; CHEMBL5189; -.
DR   DrugCentral; P10481; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   BioCyc; MetaCyc:MON-18998; -.
DR   BRENDA; 3.2.1.18; 1503.
DR   SABIO-RK; P10481; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR008377; Sialidase_trypan.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   Pfam; PF13859; BNR_3; 1.
DR   PRINTS; PR01803; TCSIALIDASE.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Repeat; Secreted.
FT   CHAIN           1..382
FT                   /note="Sialidase"
FT                   /id="PRO_0000208908"
FT   REPEAT          71..82
FT                   /note="BNR 1"
FT   REPEAT          140..151
FT                   /note="BNR 2"
FT   REPEAT          208..219
FT                   /note="BNR 3"
FT   REPEAT          255..266
FT                   /note="BNR 4"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        347
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   382 AA;  42813 MW;  D50857BB50A4E886 CRC64;
     MCNKNNTFEK NLDISHKPEP LILFNKDNNI WNSKYFRIPN IQLLNDGTIL TFSDIRYNGP
     DDHAYIDIAS ARSTDFGKTW SYNIAMKNNR IDSTYSRVMD STTVITNTGR IILIAGSWNT
     NGNWAMTTST RRSDWSVQMI YSDDNGLTWS NKIDLTKDSS KVKNQPSNTI GWLGGVGSGI
     VMDDGTIVMP AQISLRENNE NNYYSLIIYS KDNGETWTMG NKVPNSNTSE NMVIELDGAL
     IMSTRYDYSG YRAAYISHDL GTTWEIYEPL NGKILTGKGS GCQGSFIKAT TSNGHRIGLI
     SAPKNTKGEY IRDNIAVYMI DFDDLSKGVQ EICIPYPEDG NKLGGGYSCL SFKNNHLGIV
     YEANGNIEYQ DLTPYYSLIN KQ