ID   NANH_CLOSE              Reviewed;        1014 AA.
AC   P29767;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Sialidase;
DE            EC=3.2.1.18;
DE   AltName: Full=Neuraminidase;
DE   Flags: Precursor;
OS   Clostridium septicum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1504;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NC 0054714;
RX   PubMed=2034213; DOI=10.1007/bf00273603;
RA   Rothe B., Rothe B., Roggentin P., Schauer R.;
RT   "The sialidase gene from Clostridium septicum: cloning, sequencing,
RT   expression in Escherichia coli and identification of conserved sequences in
RT   sialidases and other proteins.";
RL   Mol. Gen. Genet. 226:190-197(1991).
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}.
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DR   EMBL; X63266; CAA44916.1; -; Genomic_DNA.
DR   PIR; S15994; NMCLSS.
DR   AlphaFoldDB; P29767; -.
DR   SMR; P29767; -.
DR   STRING; 1504.GCA_900092375_02401; -.
DR   CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.40.220.10; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR004124; Glyco_hydro_33_N.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR023364; Trans_sialidase_dom3.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02973; Sialidase; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Repeat; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1014
FT                   /note="Sialidase"
FT                   /id="PRO_0000012031"
FT   DOMAIN          39..186
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   REPEAT          431..442
FT                   /note="BNR 1"
FT   REPEAT          563..574
FT                   /note="BNR 2"
FT   REPEAT          627..638
FT                   /note="BNR 3"
FT   REPEAT          700..711
FT                   /note="BNR 4"
FT   ACT_SITE        421
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        912
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         688
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         873
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1014 AA;  110653 MW;  C4F49233473A2FAD CRC64;
     MNKKKIMSIL VSAFLITNLS SNIIFADIKE NVYINQYSEG NRSQPIAEKL VPRSEIQASA
     TSALTGEGPE KAIDGNTSTL WHTPWAGVDI QINPQSLTLK LGKTRNISSI CVTPRQEGTN
     GMITDYKIYS GDDVIAEGKW KSDSSDKYVV FDNPISTDNI RIEAISTVGD ENNKHASIAE
     VEVYELADTP VKLAESNNKV INNGNGGNYE GDISEISLLE EGTAIIRFTN NGSSLFSISN
     NERTNEHFHV YINGGAIGYE LRKQSGNLAT GSVNKALNAG INTIAFKAEK GKGYSIYLNG
     EKILTSSSIT ANFLSTLEGL NTLSLGKTDR PSGSNEYNFT GEIDFFELYS KPLADRYLKE
     RTGETTSKDL PFPEGAVKTE PVDIFTPGEL GSNNFRIPAL YTTKDGTVLA SIDVRKGGGH
     DAPNNIDTGI KRSTDGGVTW DEGKIILDYP GASSAIDTSL LQDDETGRIF LIVTHFAEGY
     GFGNSKTGSG YVEIEGKRYL KLLGANDTIY TVREGVVYDS NGEATNYTVD NNNELYENGN
     RIGNVLLSNS PLKVMGTSFL SLIYSDDDGQ TWSDPIDLNK EVKTDWMRFL GTGPGKGHQI
     KTGRYAGRLL FPVYLTNASG FQSSAVIYSD DNGATWNIGE TATDGRLMDN GDRASAETIT
     TNTSGGVGQL TECQVVEMPN GQLKMFMRNT GGNSGRVRIA TSFDGGATWE DDVVRDENIK
     EPYCQLSVIN YSQKIDGKDA IIFAIPDANY PNRVNGTVRV GLITENGSYE NGEPRYDIEW
     RYNKVVAPGT YGYSCLSEMP NGEIGLFYEG RGSRQMSFTR MNIDYLKADL LQDVPAANIK
     SYTTNSENNI YDPGDKISLN VTFDQTVSLI GDRTITADIG GKEVLLTLAN SKGGSEYTFE
     GTVPADISNG NYTITIKGKS GLKIVNVVNK VTDITEDRNT GLNVQVGEEV QSVDKTLLQD
     LVDSTSNLIK EDYTEESWIL YEKALEVANK FLVNEIAVQE EVDAAKPTLE NAYK