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 25-NOV-2008, entry version 56. DE RecName: Full=Sialidase; DE EC=3.2.1.18; DE AltName: Full=Neuraminidase; DE Flags: Precursor; OS Clostridium septicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1504; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NC 0054714; RX MEDLINE=91238693; 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 RT sequences in sialidases and other proteins."; RL Mol. Gen. Genet. 226:190-197(1991). CC -!- FUNCTION: Sialidases have been suggested to be pathogenic factors CC in microbial infections. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, CC alpha-(2->8)- glycosidic linkages of terminal sialic acid residues CC in oligosaccharides, glycoproteins, glycolipids, colominic acid CC and synthetic substrates. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. CC -!- SIMILARITY: Contains 4 BNR repeats. CC -!- SIMILARITY: Contains 1 F5/8 type C domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63266; CAA44916.1; -; Genomic_DNA. DR PIR; S15994; NMCLSS. DR HSSP; Q27701; 1SLL. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR002860; BNR. DR InterPro; IPR000421; Coagulation_factor_5/8-type_C. DR InterPro; IPR013320; ConA_like_subgrp. DR InterPro; IPR011490; FIVAR_sugar_bd. DR InterPro; IPR004124; Glyco_hydro_33_N. DR Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1. DR Pfam; PF02012; BNR; 4. DR Pfam; PF00754; F5_F8_type_C; 1. DR Pfam; PF07554; FIVAR; 1. DR Pfam; PF02973; Sialidase; 1. DR PROSITE; PS50022; FA58C_3; 1. PE 3: Inferred from homology; KW Glycosidase; Hydrolase; Repeat; Secreted; Signal. FT SIGNAL 1 26 Potential. FT CHAIN 27 1014 Sialidase. FT /FTId=PRO_0000012031. FT DOMAIN 39 186 F5/8 type C. FT REPEAT 431 442 BNR 1. FT REPEAT 563 574 BNR 2. FT REPEAT 627 638 BNR 3. FT REPEAT 700 711 BNR 4. FT ACT_SITE 421 421 Proton acceptor (By similarity). FT ACT_SITE 912 912 Nucleophile (By similarity). FT BINDING 396 396 Substrate (By similarity). FT BINDING 688 688 Substrate (By similarity). FT BINDING 873 873 Substrate (Potential). 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 //