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)

P0C6E9

- NANH_VIBCH

UniProt

P0C6E9 - NANH_VIBCH

Protein

Sialidase

Gene

nanH

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (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.

    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

    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:VC_1784
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 1

    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 – 2424By similarityAdd
    BLAST
    Chaini25 – 781757SialidasePRO_0000012033Add
    BLAST

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Monomer.Curated

    Protein-protein interaction databases

    STRINGi243277.VC1784.

    Structurei

    Secondary structure

    1
    781
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 305
    Helixi35 – 373
    Helixi40 – 434
    Beta strandi54 – 629
    Beta strandi64 – 7310
    Beta strandi75 – 795
    Helixi83 – 9210
    Beta strandi94 – 10613
    Beta strandi111 – 1133
    Beta strandi115 – 1195
    Beta strandi121 – 1255
    Beta strandi131 – 1355
    Beta strandi142 – 1454
    Helixi147 – 1515
    Beta strandi154 – 1618
    Beta strandi163 – 1653
    Beta strandi167 – 1726
    Beta strandi175 – 1817
    Beta strandi190 – 1956
    Beta strandi198 – 2003
    Beta strandi202 – 21312
    Beta strandi216 – 2194
    Beta strandi224 – 2307
    Beta strandi232 – 2343
    Beta strandi238 – 2469
    Beta strandi257 – 27115
    Beta strandi276 – 2794
    Helixi280 – 2823
    Beta strandi284 – 2863
    Beta strandi288 – 29811
    Turni299 – 3024
    Beta strandi303 – 31210
    Helixi318 – 3203
    Beta strandi329 – 3368
    Turni337 – 3404
    Beta strandi341 – 3477
    Helixi349 – 3524
    Beta strandi357 – 37115
    Beta strandi380 – 39213
    Beta strandi394 – 41118
    Beta strandi417 – 4215
    Beta strandi428 – 4314
    Helixi434 – 4374
    Beta strandi441 – 4488
    Turni449 – 4524
    Beta strandi453 – 4586
    Beta strandi461 – 4666
    Beta strandi474 – 4807
    Beta strandi483 – 4853
    Beta strandi487 – 49812
    Beta strandi501 – 5066
    Helixi508 – 5125
    Helixi522 – 5243
    Beta strandi528 – 5347
    Beta strandi536 – 5405
    Beta strandi542 – 5454
    Beta strandi568 – 57811
    Beta strandi580 – 59314
    Beta strandi595 – 5995
    Beta strandi604 – 6107
    Beta strandi612 – 6143
    Beta strandi616 – 6249
    Beta strandi630 – 6389
    Beta strandi649 – 66113
    Beta strandi663 – 6697
    Helixi670 – 6723
    Beta strandi684 – 6896
    Beta strandi695 – 7028
    Turni704 – 7085
    Beta strandi709 – 72214
    Beta strandi728 – 7325
    Beta strandi735 – 7373
    Beta strandi740 – 7456
    Beta strandi747 – 75610
    Helixi758 – 7603
    Beta strandi762 – 7687
    Helixi769 – 7724
    Helixi773 – 7753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KITX-ray2.30A25-781[»]
    1W0OX-ray1.90A1-781[»]
    1W0PX-ray1.60A1-781[»]
    2W68X-ray2.50A/B/C25-216[»]
    ProteinModelPortaliP0C6E9.
    SMRiP0C6E9. Positions 25-781.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C6E9.

    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.
    KOiK01186.
    OrthoDBiEOG64JFJ7.

    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.

    P0C6E9-1 [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 - v1
    Checksum:iFA85ED907FB20AF0
    GO

    Sequence cautioni

    The sequence AAF94933.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF94933.1. Different initiation.
    PIRiE82158.
    RefSeqiNP_231419.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF94933; AAF94933; VC_1784.
    GeneIDi2613664.
    KEGGivch:VC1784.
    PATRICi20082616. VBIVibCho83274_1703.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF94933.1 . Different initiation.
    PIRi E82158.
    RefSeqi NP_231419.1. NC_002505.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KIT X-ray 2.30 A 25-781 [» ]
    1W0O X-ray 1.90 A 1-781 [» ]
    1W0P X-ray 1.60 A 1-781 [» ]
    2W68 X-ray 2.50 A/B/C 25-216 [» ]
    ProteinModelPortali P0C6E9.
    SMRi P0C6E9. Positions 25-781.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VC1784.

    Chemistry

    BindingDBi P0C6E9.
    ChEMBLi CHEMBL1075100.

    Protocols and materials databases

    DNASUi 2613664.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF94933 ; AAF94933 ; VC_1784 .
    GeneIDi 2613664.
    KEGGi vch:VC1784.
    PATRICi 20082616. VBIVibCho83274_1703.

    Phylogenomic databases

    eggNOGi COG4409.
    KOi K01186.
    OrthoDBi EOG64JFJ7.

    Miscellaneous databases

    EvolutionaryTracei P0C6E9.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.
    2. "Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2."
      Taylor G.L., Vimr E.R., Garman E.F., Laver W.G.
      J. Mol. Biol. 226:1287-1290(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    3. "Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain."
      Crenells S., Garman E.F., Laver W.G., Vimr E.R., Taylor G.L.
      Structure 2:535-544(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiNANH_VIBCH
    AccessioniPrimary (citable) accession number: P0C6E9
    Secondary accession number(s): 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 42 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3