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P29768 (NANH_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sialidase

EC=3.2.1.18
Alternative name(s):
N-acylneuraminate glycohydrolase
Neuraminidase
Short name=NANase
STNA
Gene names
Name:nanH
Ordered Locus Names:STM0928
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length382 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.

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.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 4 BNR repeats.

Sequence caution

The sequence AAL19864.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 382381Sialidase
PRO_0000208909

Regions

Repeat71 – 8212BNR 1
Repeat145 – 15612BNR 2
Repeat210 – 22011BNR 3
Repeat254 – 26512BNR 4

Sites

Active site621Proton acceptor By similarity
Active site3421Nucleophile By similarity
Active site3611
Binding site371Substrate
Binding site2461Substrate
Binding site3091Substrate

Amino acid modifications

Disulfide bond42 ↔ 103

Experimental info

Sequence conflict3291D → A in AAA27168. Ref.1

Secondary structure

.................................................................... 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29768 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: C15515CF9C15597E

FASTA38242,073
        10         20         30         40         50         60 
MTVEKSVVFK AEGEHFTDQK GNTIVGSGSG GTTKYFRIPA MCTTSKGTIV VFADARHNTA 

        70         80         90        100        110        120 
SDQSFIDTAA ARSTDGGKTW NKKIAIYNDR VNSKLSRVMD PTCIVANIQG RETILVMVGK 

       130        140        150        160        170        180 
WNNNDKTWGA YRDKAPDTDW DLVLYKSTDD GVTFSKVETN IHDIVTKNGT ISAMLGGVGS 

       190        200        210        220        230        240 
GLQLNDGKLV FPVQMVRTKN ITTVLNTSFI YSTDGITWSL PSGYCEGFGS ENNIIEFNAS 

       250        260        270        280        290        300 
LVNNIRNSGL RRSFETKDFG KTWTEFPPMD KKVDNRNHGV QGSTITIPSG NKLVAAHSSA 

       310        320        330        340        350        360 
QNKNNDYTRS DISLYAHNLY SGEVKLIDDF YPKVGNASGA GYSCLSYRKN VDKETLYVVY 

       370        380 
EANGSIEFQD LSRHLPVIKS YN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer."
Hoyer L.L., Hamilton A.C., Steenbergen S.M., Vimr E.R.
Mol. Microbiol. 6:873-884(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-40.
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"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 (1.8 ANGSTROMS).
Strain: LT2.
[4]"Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase."
Crennell S.J., Garman E.F., Laver W.G., Vimr E.R., Taylor G.L.
Proc. Natl. Acad. Sci. U.S.A. 90:9852-9856(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO C-TERMINUS.
Strain: LT2.
[5]"The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution."
Crennell S.J., Garman E.F., Philippon C., Vasella A., Laver W.G., Vimr E.R., Taylor G.L.
J. Mol. Biol. 259:264-280(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Strain: LT2.
[6]Garman E.F., Wouters J., Schneider T.R., Vimr E.R., Laver W.G., Sheldrick G.M.
Submitted (JUL-1998) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55342 Genomic DNA. Translation: AAA27168.1.
AE006468 Genomic DNA. Translation: AAL19864.1. Different initiation.
RefSeqNP_459905.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DILX-ray1.90A2-382[»]
1DIMX-ray1.60A2-382[»]
2SILX-ray1.60A2-382[»]
2SIMX-ray1.60A2-382[»]
3SILX-ray1.05A4-381[»]
ProteinModelPortalP29768.
SMRP29768. Positions 2-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0928.

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

Proteomic databases

PaxDbP29768.
PRIDEP29768.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19864; AAL19864; STM0928.
GeneID1252447.
KEGGstm:STM0928.
PATRIC32380261. VBISalEnt20916_0978.

Phylogenomic databases

eggNOGCOG4409.
KOK01186.
OMAYEANGNI.
OrthoDBEOG67DPK3.
ProtClustDBCLSK516277.

Enzyme and pathway databases

BioCycSENT99287:GCTI-934-MONOMER.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR026948. Sialidase/anhydrosialidase.
IPR026856. Sialidase_fam.
IPR008377. Sialidase_trypan.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF5. PTHR10628:SF5. 1 hit.
PRINTSPR01803. TCSIALIDASE.
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP29768.

Entry information

Entry nameNANH_SALTY
AccessionPrimary (citable) accession number: P29768
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries