ID   NANH_VIBC3              Reviewed;         781 AA.
AC   A5F7A4; C3M1H8; P37060; Q9KR59;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Sialidase;
DE            EC=3.2.1.18;
DE   AltName: Full=Neuraminidase;
DE            Short=NANase;
DE   Flags: Precursor;
GN   Name=nanH; OrderedLocusNames=VC0395_A1381, VC395_1898;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1730470; DOI=10.1128/iai.60.2.406-415.1992;
RA   Galen J.E., Ketley J.M., Fasano A., Richardson S.H., Wasserman S.S.,
RA   Kaper J.B.;
RT   "Role of Vibrio cholerae neuraminidase in the function of cholera toxin.";
RL   Infect. Immun. 60:406-415(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44, AND PROTEIN SEQUENCE OF 25-44.
RX   PubMed=2832365; DOI=10.1128/jb.170.4.1495-1504.1988;
RA   Vimr E.R., Lawrisuk L., Galen J.E., Kaper J.B.;
RT   "Cloning and expression of the Vibrio cholerae neuraminidase gene nanH in
RT   Escherichia coli.";
RL   J. Bacteriol. 170:1495-1504(1988).
CC   -!- FUNCTION: Cleaves the terminal sialic acid (N-acetyl neuraminic acid)
CC       from carbohydrate chains in glycoproteins providing free sialic acid
CC       which can be used as carbon and energy sources. Sialidases have been
CC       suggested to be pathogenic factors in microbial infections. Facilitates
CC       cholera toxin binding to host intestinal epithelial cells by converting
CC       cell surface polysialogangliosides to GM1 monogangliosides.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: May be controlled by sialic acid availability and a growth-
CC       phase-dependent mechanism.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ19703.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ACP09894.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M83562; AAA27546.1; -; Genomic_DNA.
DR   EMBL; CP000627; ABQ19703.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001235; ACP09894.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M19268; AAA27547.1; -; Genomic_DNA.
DR   PIR; A27734; A27734.
DR   PIR; A43866; A43866.
DR   RefSeq; WP_001211290.1; NZ_JAACZH010000016.1.
DR   AlphaFoldDB; A5F7A4; -.
DR   SMR; A5F7A4; -.
DR   STRING; 345073.VC395_1898; -.
DR   CAZy; CBM40; Carbohydrate-Binding Module Family 40.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   EnsemblBacteria; ABQ19703; ABQ19703; VC0395_A1381.
DR   GeneID; 57740427; -.
DR   KEGG; vco:VC0395_A1381; -.
DR   KEGG; vcr:VC395_1898; -.
DR   PATRIC; fig|345073.21.peg.1838; -.
DR   eggNOG; COG4409; Bacteria.
DR   HOGENOM; CLU_376807_0_0_6; -.
DR   Proteomes; UP000000249; Chromosome 2.
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:0033691; F:sialic acid binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR015344; VCNA_lectin-like_dom.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   Pfam; PF09264; Sial-lect-inser; 2.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Glycosidase; Hydrolase; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:2832365"
FT   CHAIN           25..781
FT                   /note="Sialidase"
FT                   /id="PRO_0000323013"
FT   REPEAT          263..274
FT                   /note="BNR 1"
FT   REPEAT          585..596
FT                   /note="BNR 2"
FT   REPEAT          653..664
FT                   /note="BNR 3"
FT   REPEAT          718..729
FT                   /note="BNR 4"
FT   ACT_SITE        250
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        619
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        740
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         635
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         712
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        22
FT                   /note="S -> L (in Ref. 4; AAA27547)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   781 AA;  85609 MW;  FA85ED907FB20AF0 CRC64;
     MRFKNVKKTA LMLAMFGMAT SSNAALFDYN ATGDTEFDSP AKQGWMQDNT NNGSGVLTNA
     DGMPAWLVQG IGGRAQWTYS LSTNQHAQAS SFGWRMTTEM KVLSGGMITN YYANGTQRVL
     PIISLDSSGN LVVEFEGQTG RTVLATGTAA TEYHKFELVF LPGSNPSASF YFDGKLIRDN
     IQPTASKQNM IVWGNGSSNT DGVAAYRDIK FEIQGDVIFR GPDRIPSIVA SSVTPGVVTA
     FAEKRVGGGD PGALSNTNDI ITRTSRDGGI TWDTELNLTE QINVSDEFDF SDPRPIYDPS
     SNTVLVSYAR WPTDAAQNGD RIKPWMPNGI FYSVYDVASG NWQAPIDVTD QVKERSFQIA
     GWGGSELYRR NTSLNSQQDW QSNAKIRIVD GAANQIQVAD GSRKYVVTLS IDESGGLVAN
     LNGVSAPIIL QSEHAKVHSF HDYELQYSAL NHTTTLFVDG QQITTWAGEV SQENNIQFGN
     ADAQIDGRLH VQKIVLTQQG HNLVEFDAFY LAQQTPEVEK DLEKLGWTKI KTGNTMSLYG
     NASVNPGPGH GITLTRQQNI SGSQNGRLIY PAIVLDRFFL NVMSIYSDDG GSNWQTGSTL
     PIPFRWKSSS ILETLEPSEA DMVELQNGDL LLTARLDFNQ IVNGVNYSPR QQFLSKDGGI
     TWSLLEANNA NVFSNISTGT VDASITRFEQ SDGSHFLLFT NPQGNPAGTN GRQNLGLWFS
     FDEGVTWKGP IQLVNGASAY SDIYQLDSEN AIVIVETDNS NMRILRMPIT LLKQKLTLSQ
     N