Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A5F7A4

- NANH_VIBC3

UniProt

A5F7A4 - NANH_VIBC3

Protein

Sialidase

Gene

nanH

Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 2 (18 Mar 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections. Facilitates cholera toxin binding to host intestinal epithelial cells by converting cell surface polysialogangliosides to GM1 monogangliosides.

    Catalytic activityi

    Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

    Cofactori

    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei224 – 2241SubstrateBy similarity
    Active sitei250 – 2501Proton acceptorBy similarity
    Active sitei619 – 6191Sequence Analysis
    Binding sitei635 – 6351SubstrateBy similarity
    Binding sitei712 – 7121SubstrateBy similarity
    Active sitei740 – 7401NucleophileBy similarity

    GO - Molecular functioni

    1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
    2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
    3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
    4. sialic acid binding Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Calcium

    Protein family/group databases

    CAZyiCBM40. Carbohydrate-Binding Module Family 40.
    GH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase (EC:3.2.1.18)
    Alternative name(s):
    Neuraminidase
    Short name:
    NANase
    Gene namesi
    Name:nanH
    Ordered Locus Names:VC0395_A1381, VC395_1898
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
    Taxonomic identifieri345073 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000249: Chromosome 2, UP000001630: Chromosome I

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 781757SialidasePRO_0000323013Add
    BLAST

    Expressioni

    Inductioni

    May be controlled by sialic acid availability and a growth-phase-dependent mechanism.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi345073.VC0395_A1381.

    Structurei

    3D structure databases

    ProteinModelPortaliA5F7A4.
    SMRiA5F7A4. Positions 25-781.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati263 – 27412BNR 1Add
    BLAST
    Repeati585 – 59612BNR 2Add
    BLAST
    Repeati653 – 66412BNR 3Add
    BLAST
    Repeati718 – 72912BNR 4Add
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 4 BNR repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4409.
    HOGENOMiHOG000218204.
    KOiK01186.

    Family and domain databases

    Gene3Di2.120.10.10. 2 hits.
    2.60.120.200. 2 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    IPR015344. VCNA_lectin-like_dom.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PfamiPF09264. Sial-lect-inser. 2 hits.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 2 hits.
    SSF50939. SSF50939. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A5F7A4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRFKNVKKTA LMLAMFGMAT SSNAALFDYN ATGDTEFDSP AKQGWMQDNT    50
    NNGSGVLTNA DGMPAWLVQG IGGRAQWTYS LSTNQHAQAS SFGWRMTTEM 100
    KVLSGGMITN YYANGTQRVL PIISLDSSGN LVVEFEGQTG RTVLATGTAA 150
    TEYHKFELVF LPGSNPSASF YFDGKLIRDN IQPTASKQNM IVWGNGSSNT 200
    DGVAAYRDIK FEIQGDVIFR GPDRIPSIVA SSVTPGVVTA FAEKRVGGGD 250
    PGALSNTNDI ITRTSRDGGI TWDTELNLTE QINVSDEFDF SDPRPIYDPS 300
    SNTVLVSYAR WPTDAAQNGD RIKPWMPNGI FYSVYDVASG NWQAPIDVTD 350
    QVKERSFQIA GWGGSELYRR NTSLNSQQDW QSNAKIRIVD GAANQIQVAD 400
    GSRKYVVTLS IDESGGLVAN LNGVSAPIIL QSEHAKVHSF HDYELQYSAL 450
    NHTTTLFVDG QQITTWAGEV SQENNIQFGN ADAQIDGRLH VQKIVLTQQG 500
    HNLVEFDAFY LAQQTPEVEK DLEKLGWTKI KTGNTMSLYG NASVNPGPGH 550
    GITLTRQQNI SGSQNGRLIY PAIVLDRFFL NVMSIYSDDG GSNWQTGSTL 600
    PIPFRWKSSS ILETLEPSEA DMVELQNGDL LLTARLDFNQ IVNGVNYSPR 650
    QQFLSKDGGI TWSLLEANNA NVFSNISTGT VDASITRFEQ SDGSHFLLFT 700
    NPQGNPAGTN GRQNLGLWFS FDEGVTWKGP IQLVNGASAY SDIYQLDSEN 750
    AIVIVETDNS NMRILRMPIT LLKQKLTLSQ N 781
    Length:781
    Mass (Da):85,609
    Last modified:March 18, 2008 - v2
    Checksum:iFA85ED907FB20AF0
    GO

    Sequence cautioni

    The sequence ABQ19703.1 differs from that shown. Reason: Erroneous initiation.
    The sequence ACP09894.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221S → L in AAA27547. (PubMed:2832365)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83562 Genomic DNA. Translation: AAA27546.1.
    CP000627 Genomic DNA. Translation: ABQ19703.1. Different initiation.
    CP001235 Genomic DNA. Translation: ACP09894.1. Different initiation.
    M19268 Genomic DNA. Translation: AAA27547.1.
    PIRiA27734.
    A43866.
    RefSeqiYP_001217324.1. NC_009457.1.
    YP_002820130.1. NC_012582.1.

    Genome annotation databases

    EnsemblBacteriaiABQ19703; ABQ19703; VC0395_A1381.
    ACP09894; ACP09894; VC395_1898.
    GeneIDi5137230.
    7775747.
    KEGGivco:VC0395_A1381.
    vcr:VC395_1898.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83562 Genomic DNA. Translation: AAA27546.1 .
    CP000627 Genomic DNA. Translation: ABQ19703.1 . Different initiation.
    CP001235 Genomic DNA. Translation: ACP09894.1 . Different initiation.
    M19268 Genomic DNA. Translation: AAA27547.1 .
    PIRi A27734.
    A43866.
    RefSeqi YP_001217324.1. NC_009457.1.
    YP_002820130.1. NC_012582.1.

    3D structure databases

    ProteinModelPortali A5F7A4.
    SMRi A5F7A4. Positions 25-781.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 345073.VC0395_A1381.

    Chemistry

    BindingDBi A5F7A4.

    Protein family/group databases

    CAZyi CBM40. Carbohydrate-Binding Module Family 40.
    GH33. Glycoside Hydrolase Family 33.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ19703 ; ABQ19703 ; VC0395_A1381 .
    ACP09894 ; ACP09894 ; VC395_1898 .
    GeneIDi 5137230.
    7775747.
    KEGGi vco:VC0395_A1381.
    vcr:VC395_1898.

    Phylogenomic databases

    eggNOGi COG4409.
    HOGENOMi HOG000218204.
    KOi K01186.

    Family and domain databases

    Gene3Di 2.120.10.10. 2 hits.
    2.60.120.200. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    IPR015344. VCNA_lectin-like_dom.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    Pfami PF09264. Sial-lect-inser. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 2 hits.
    SSF50939. SSF50939. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Role of Vibrio cholerae neuraminidase in the function of cholera toxin."
      Galen J.E., Ketley J.M., Fasano A., Richardson S.H., Wasserman S.S., Kaper J.B.
      Infect. Immun. 60:406-415(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Heidelberg J.
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39541 / Classical Ogawa 395 / O395.
    3. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
      Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
      PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39541 / Classical Ogawa 395 / O395.
    4. "Cloning and expression of the Vibrio cholerae neuraminidase gene nanH in Escherichia coli."
      Vimr E.R., Lawrisuk L., Galen J.E., Kaper J.B.
      J. Bacteriol. 170:1495-1504(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44, PROTEIN SEQUENCE OF 25-44.

    Entry informationi

    Entry nameiNANH_VIBC3
    AccessioniPrimary (citable) accession number: A5F7A4
    Secondary accession number(s): C3M1H8, P37060, Q9KR59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 50 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3