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P0C6E9 (NANH_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialidase
EC=3.2.1.18
Alternative name(s):
Neuraminidase
Short name=NANase
Gene names
Name:nanH
Ordered Locus Names:VC_1784
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Cofactor

Calcium.

Subunit structure

Monomer Probable.

Subcellular location

Secreted.

Induction

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

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 4 BNR repeats.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 781757Sialidase
PRO_0000012033

Regions

Repeat263 – 27412BNR 1
Repeat585 – 59612BNR 2
Repeat653 – 66412BNR 3
Repeat718 – 72912BNR 4

Sites

Active site2501Proton acceptor By similarity
Active site6191 Potential
Active site7401Nucleophile By similarity
Binding site2241Substrate By similarity
Binding site6351Substrate By similarity
Binding site7121Substrate By similarity

Secondary structure

1 .................................................................................................................................................. 781
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C6E9 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: FA85ED907FB20AF0

FASTA78185,609
        10         20         30         40         50         60 
MRFKNVKKTA LMLAMFGMAT SSNAALFDYN ATGDTEFDSP AKQGWMQDNT NNGSGVLTNA 

        70         80         90        100        110        120 
DGMPAWLVQG IGGRAQWTYS LSTNQHAQAS SFGWRMTTEM KVLSGGMITN YYANGTQRVL 

       130        140        150        160        170        180 
PIISLDSSGN LVVEFEGQTG RTVLATGTAA TEYHKFELVF LPGSNPSASF YFDGKLIRDN 

       190        200        210        220        230        240 
IQPTASKQNM IVWGNGSSNT DGVAAYRDIK FEIQGDVIFR GPDRIPSIVA SSVTPGVVTA 

       250        260        270        280        290        300 
FAEKRVGGGD PGALSNTNDI ITRTSRDGGI TWDTELNLTE QINVSDEFDF SDPRPIYDPS 

       310        320        330        340        350        360 
SNTVLVSYAR WPTDAAQNGD RIKPWMPNGI FYSVYDVASG NWQAPIDVTD QVKERSFQIA 

       370        380        390        400        410        420 
GWGGSELYRR NTSLNSQQDW QSNAKIRIVD GAANQIQVAD GSRKYVVTLS IDESGGLVAN 

       430        440        450        460        470        480 
LNGVSAPIIL QSEHAKVHSF HDYELQYSAL NHTTTLFVDG QQITTWAGEV SQENNIQFGN 

       490        500        510        520        530        540 
ADAQIDGRLH VQKIVLTQQG HNLVEFDAFY LAQQTPEVEK DLEKLGWTKI KTGNTMSLYG 

       550        560        570        580        590        600 
NASVNPGPGH GITLTRQQNI SGSQNGRLIY PAIVLDRFFL NVMSIYSDDG GSNWQTGSTL 

       610        620        630        640        650        660 
PIPFRWKSSS ILETLEPSEA DMVELQNGDL LLTARLDFNQ IVNGVNYSPR QQFLSKDGGI 

       670        680        690        700        710        720 
TWSLLEANNA NVFSNISTGT VDASITRFEQ SDGSHFLLFT NPQGNPAGTN GRQNLGLWFS 

       730        740        750        760        770        780 
FDEGVTWKGP IQLVNGASAY SDIYQLDSEN AIVIVETDNS NMRILRMPIT LLKQKLTLSQ 


N

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. expand/collapse author list , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003852 Genomic DNA. Translation: AAF94933.1. Different initiation.
PIRE82158.
RefSeqNP_231419.1. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KITX-ray2.30A25-781[»]
1W0OX-ray1.90A1-781[»]
1W0PX-ray1.60A1-781[»]
2W68X-ray2.50A/B/C25-216[»]
ProteinModelPortalP0C6E9.
SMRP0C6E9. Positions 25-781.
ModBaseSearch...

Protein-protein interaction databases

STRING243277.VC1784.

Protocols and materials databases

DNASU2613664.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94933; AAF94933; VC_1784.
GeneID2613664.
KEGGvch:VC1784.
PATRIC20082616. VBIVibCho83274_1703.

Phylogenomic databases

eggNOGCOG4409.
KOK01186.
ProtClustDBCLSK794375.

Family and domain databases

Gene3D2.120.10.10. 2 hits.
2.60.120.200. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR015344. VCNA_lectin-like_dom.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PfamPF09264. Sial-lect-inser. 2 hits.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 2 hits.
SSF50939. Sialidase. 1 hit.
ProtoNetSearch...

Other

BindingDBP0C6E9.
ChEMBLCHEMBL1075100.
EvolutionaryTraceP0C6E9.

Entry information

Entry nameNANH_VIBCH
AccessionPrimary (citable) accession number: P0C6E9
Secondary accession number(s): P37060, Q9KR59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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