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Database: UniProt/SWISS-PROT
Entry: NANH_VIBC3
LinkDB: NANH_VIBC3
Original site: NANH_VIBC3 
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   25-OCT-2017, entry version 74.
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;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1730470;
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
RT   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.,
RA   Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the
RT   cholera pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44, AND PROTEIN SEQUENCE OF
RP   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
RT   in Escherichia coli.";
RL   J. Bacteriol. 170:1495-1504(1988).
CC   -!- FUNCTION: Cleaves the terminal sialic acid (N-acetyl neuraminic
CC       acid) from carbohydrate chains in glycoproteins providing free
CC       sialic acid which can be used as carbon and energy sources.
CC       Sialidases have been suggested to be pathogenic factors in
CC       microbial infections. Facilitates cholera toxin binding to host
CC       intestinal epithelial cells by converting cell surface
CC       polysialogangliosides to GM1 monogangliosides.
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   -!- 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
CC       growth-phase-dependent mechanism.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {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};
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   ProteinModelPortal; A5F7A4; -.
DR   SMR; A5F7A4; -.
DR   STRING; 345073.VC0395_A1381; -.
DR   CAZy; CBM40; Carbohydrate-Binding Module Family 40.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   EnsemblBacteria; ABQ19703; ABQ19703; VC0395_A1381.
DR   EnsemblBacteria; ACP09894; ACP09894; VC395_1898.
DR   KEGG; vco:VC0395_A1381; -.
DR   KEGG; vcr:VC395_1898; -.
DR   PATRIC; fig|345073.21.peg.1838; -.
DR   eggNOG; ENOG4108478; Bacteria.
DR   eggNOG; COG4409; LUCA.
DR   HOGENOM; HOG000218204; -.
DR   KO; K01186; -.
DR   OrthoDB; POG091H0EBR; -.
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.
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; 2.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Repeat; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:2832365}.
FT   CHAIN        25    781       Sialidase.
FT                                /FTId=PRO_0000323013.
FT   REPEAT      263    274       BNR 1.
FT   REPEAT      585    596       BNR 2.
FT   REPEAT      653    664       BNR 3.
FT   REPEAT      718    729       BNR 4.
FT   ACT_SITE    250    250       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    619    619       {ECO:0000255}.
FT   ACT_SITE    740    740       Nucleophile. {ECO:0000250}.
FT   BINDING     224    224       Substrate. {ECO:0000250}.
FT   BINDING     635    635       Substrate. {ECO:0000250}.
FT   BINDING     712    712       Substrate. {ECO:0000250}.
FT   CONFLICT     22     22       S -> L (in Ref. 4; AAA27547).
FT                                {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
//
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