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UniProtKB/Swiss-Prot entry P29768


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NANH_SALTY
Primary accession number P29768
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 73)
Name and origin of the protein
Protein name Sialidase
Synonyms EC 3.2.1.18
Neuraminidase
NANase
N-acylneuraminate glycohydrolase
STNA
Gene name
Name: nanH
OrderedLocusNames: STM0928
From
Salmonella typhimurium [TaxID: 602] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-40.
STRAIN=LT2;
PubMed=1602967 [NCBI, ExPASy, EBI, Israel, Japan]
Hoyer L.L., Hamilton A.C., Steenbergen S.M., Vimr E.R.;
"Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer.";
Mol. Microbiol. 6:873-884(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
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., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).
[3]
CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
STRAIN=LT2;
DOI=10.1016/0022-2836(92)91069-2; PubMed=1518058 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor G.L., Vimr E.R., Garman E.F., Laver W.G.;
"Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2.";
J. Mol. Biol. 226:1287-1290(1992).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SEQUENCE REVISION TO C-TERMINUS.
STRAIN=LT2;
PubMed=8234325 [NCBI, ExPASy, EBI, Israel, Japan]
Crennell S.J., Garman E.F., Laver W.G., Vimr E.R., Taylor G.L.;
"Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase.";
Proc. Natl. Acad. Sci. U.S.A. 90:9852-9856(1993).
[5]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
STRAIN=LT2;
DOI=10.1006/jmbi.1996.0318; PubMed=8656428 [NCBI, ExPASy, EBI, Israel, Japan]
Crennell S.J., Garman E.F., Philippon C., Vasella A., Laver W.G., Vimr E.R., Taylor G.L.;
"The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution.";
J. Mol. Biol. 259:264-280(1996).
[6]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
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.
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: Monomer.
  • SIMILARITY: Belongs to the glycosyl hydrolase 33 family [view classification].
  • SIMILARITY: Contains 4 BNR repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M55342; AAA27168.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008737; AAL19864.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_459905.1; -.
3D structure databases
PDB
1DIL; X-ray; 1.90 A; A=1-382.[ExPASy / RCSB / EBI]
1DIM; X-ray; 1.60 A; A=1-382.[ExPASy / RCSB / EBI]
2SIL; X-ray; 1.60 A; A=1-382.[ExPASy / RCSB / EBI]
2SIM; X-ray; 1.60 A; A=1-382.[ExPASy / RCSB / EBI]
3SIL; X-ray; 1.05 A; A=4-382.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DIL; -.
1DIM; -.
2SIL; -.
2SIM; -.
3SIL; -.
ModBase P29768.
Enzyme and pathway databases
BioCyc STYP99287:STM0928-MON; -.
Organism-specific databases
StyGene SG10244; nanH.
Ontologies
GO
GO:0004308; Molecular function: exo-alpha-sialidase activity (inferred from electronic annotation from EC).
GO:0008152; Biological process: metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002860; BNR.
Graphical view of domain structure.
Pfam PF02012; BNR; 4.
Pfam graphical view of domain structure.
BLOCKS P29768.
ProtoNet P29768.
Genome annotation databases
GeneID 1252447; -.
GenomeReviews AE006468_GR; STM0928.
KEGG stm:STM0928; -.
NMPDR fig|99287.1.peg.895; -.
Phylogenomic databases
HOGENOM P29768; -.
Other
LinkHub P29768; -.
Genome annotation databases
CMR P29768; STM0928.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Glycosidase; Hydrolase; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   382  381     Sialidase. PRO_0000208909
REPEAT   71    82  12     BNR 1. 
REPEAT   145   156  12     BNR 2. 
REPEAT   210   220  11     BNR 3. 
REPEAT   254   265  12     BNR 4. 
ACT_SITE   62    62        Proton acceptor (By similarity). 
ACT_SITE   342   342        Nucleophile (By similarity). 
ACT_SITE   361   361         
BINDING   37    37        Substrate. 
BINDING   246   246        Substrate. 
BINDING   309   309        Substrate. 
DISULFID   42   103         
CONFLICT   329   329        D -> A (in Ref. 1; AAA27168). 
STRAND   5     9  5      
HELIX   29    31  3      
STRAND   35    43  9      
STRAND   49    58  10      
STRAND   62    64  3      
STRAND   66    78  13      
STRAND   81    86  6      
TURN   93    95  3      
STRAND   97   108  12      
STRAND   111   123  13      
HELIX   128   130  3      
STRAND   133   136  4      
STRAND   141   149  9      
STRAND   155   157  3      
HELIX   161   168  8      
STRAND   170   176  7      
STRAND   178   180  3      
STRAND   189   197  9      
STRAND   204   219  16      
STRAND   232   237  6      
STRAND   240   245  6      
STRAND   248   250  3      
STRAND   254   261  8      
TURN   267   271  5      
STRAND   283   289  7      
STRAND   292   300  9      
STRAND   312   317  6      
TURN   319   321  3      
STRAND   324   331  8      
STRAND   343   350  8      
STRAND   353   362  10      
STRAND   365   370  6      
HELIX   372   374  3      
HELIX   375   379  5      
Sequence information
Length: 382 AA [This is the length of the unprocessed precursor] Molecular weight: 42073 Da [This is the MW of the unprocessed precursor] CRC64: C15515CF9C15597E [This is a checksum on the sequence]
        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 

P29768 in FASTA format

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