ID   C4LL83_CORK4            Unreviewed;       795 AA.
AC   C4LL83;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   10-JUN-2026, entry version 85.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   Name=nanI {ECO:0000313|EMBL:ACR18588.1};
GN   OrderedLocusNames=ckrop_1872 {ECO:0000313|EMBL:ACR18588.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR18588.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR18588.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR18588.1; -; Genomic_DNA.
DR   RefSeq; WP_012732475.1; NC_012704.1.
DR   AlphaFoldDB; C4LL83; -.
DR   STRING; 645127.ckrop_1872; -.
DR   GeneID; 78092060; -.
DR   KEGG; ckp:ckrop_1872; -.
DR   eggNOG; COG4409; Bacteria.
DR   HOGENOM; CLU_368301_0_0_11; -.
DR   OrthoDB; 7294637at2; -.
DR   Proteomes; UP000001473; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006689; P:ganglioside catabolic process; IEA:TreeGrafter.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.40.220.10; Intramolecular Trans-sialidase, Domain 3; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR023364; Trans_sialidase_dom3.
DR   PANTHER; PTHR10628:SF30; EXO-ALPHA-SIALIDASE; 1.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:ACR18588.1};
KW   Hydrolase {ECO:0000313|EMBL:ACR18588.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT   DOMAIN          516..760
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
FT   REGION          440..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..462
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000256|PIRSR:PIRSR626856-1"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR626856-2"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR626856-2"
SQ   SEQUENCE   795 AA;  85138 MW;  D4AF0B4B9542D9A8 CRC64;
     MSTLRTTPYP AGSILARVRT TIDGPLIGAH TSAGELSIRI EDDHPHITTR TPDRVQDLDV
     EDATTITDGQ WHSIALIVGP EGTKFYLDGY QAFCGTATAF LADVQAEELT IADAPVDVAD
     VVCTGTVLSD NDVLAHATPP QPMVQFAANH LADYDTRRVA RLGAGTTLTR FRVRGVGQGG
     TILSAGYVEA DGEDSSSAER LRLSVSDTGL TYEVLTSEDE WRTFVVDGHW ADGTWHDVVI
     RAGEGAVDLY VDGFREARIP GQAFFADASP VNTITIGQDI HGRRLFGEVA RAAIYPTPLT
     DGAIKRLSHV DPVHTQALFD RGMHGAVSYR IPSLLTLPSG TVIAGADQRT TIANDAPNDI
     NFVIRRSLDG GDHWEDMQTI LTYPGSGATG ASVIDSCTVY DEDTGTVHLL IDHFPGAIGQ
     PNNVHGVGQD SEGRLILTDT SAGGASDAEP SPAASSPAAS SPATYVLNAD GSVVTEDGKT
     TEFSVDKEGW VTRAGKPAGN IYLADGEDPN QTLLTRRTSY IVHVTSDDEG ATWSAPELIN
     HQVKEEWMAF LGTSPGTGVQ LRHGEHAGRL VIPVYYSGDN PKHFSCAVIY SDDHGETWHR
     GASPNDGRLF KGATIDSRTL ADDEASTHES TLMELKDGRL MVLMRNQHPS GRVGTAISED
     GGETWGEVTY HPDIPEIFSQ PNAIAIDGRA GGSGSGGADA SPQAGSPLYV FANASQLMPY
     RGNGVLRVST DEGETWPIAR TFNPGHYVYQ SMTYLPSGKI GLLWENEWQG LYLTQIPLSW
     FGPELQKHGG SVHVD
//