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P29768

- NANH_SALTY

UniProt

P29768 - NANH_SALTY

Protein

Sialidase

Gene

nanH

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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.

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei37 – 371Substrate
    Active sitei62 – 621Proton acceptorBy similarity
    Binding sitei246 – 2461Substrate
    Binding sitei309 – 3091Substrate
    Active sitei342 – 3421NucleophileBy similarity
    Active sitei361 – 3611

    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

    GO - Biological processi

    1. pathogenesis Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-934-MONOMER.

    Protein family/group databases

    CAZyiGH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase (EC:3.2.1.18)
    Alternative name(s):
    N-acylneuraminate glycohydrolase
    Neuraminidase
    Short name:
    NANase
    STNA
    Gene namesi
    Name:nanH
    Ordered Locus Names:STM0928
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 382381SialidasePRO_0000208909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 103

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP29768.
    PRIDEiP29768.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi99287.STM0928.

    Structurei

    Secondary structure

    1
    382
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi29 – 313
    Beta strandi35 – 439
    Beta strandi49 – 5810
    Beta strandi62 – 643
    Beta strandi66 – 7813
    Beta strandi81 – 866
    Turni93 – 953
    Beta strandi97 – 10812
    Beta strandi111 – 12313
    Helixi128 – 1303
    Beta strandi133 – 1364
    Beta strandi141 – 1499
    Beta strandi155 – 1573
    Helixi161 – 1688
    Beta strandi170 – 1767
    Beta strandi178 – 1803
    Beta strandi189 – 1979
    Beta strandi204 – 21916
    Beta strandi232 – 2376
    Beta strandi240 – 2456
    Beta strandi248 – 2503
    Beta strandi254 – 2618
    Turni267 – 2715
    Beta strandi283 – 2897
    Beta strandi292 – 3009
    Beta strandi312 – 3176
    Turni319 – 3213
    Beta strandi324 – 3318
    Beta strandi343 – 3508
    Beta strandi353 – 36210
    Beta strandi365 – 3706
    Helixi372 – 3743
    Helixi375 – 3795

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DILX-ray1.90A2-382[»]
    1DIMX-ray1.60A2-382[»]
    2SILX-ray1.60A2-382[»]
    2SIMX-ray1.60A2-382[»]
    3SILX-ray1.05A4-382[»]
    ProteinModelPortaliP29768.
    SMRiP29768. Positions 2-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29768.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati71 – 8212BNR 1Add
    BLAST
    Repeati145 – 15612BNR 2Add
    BLAST
    Repeati210 – 22011BNR 3Add
    BLAST
    Repeati254 – 26512BNR 4Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG4409.
    KOiK01186.
    OMAiYEANGNI.
    OrthoDBiEOG67DPK3.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026856. Sialidase_fam.
    IPR008377. Sialidase_trypan.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF5. PTHR10628:SF5. 1 hit.
    PRINTSiPR01803. TCSIALIDASE.
    SUPFAMiSSF50939. SSF50939. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P29768-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVEKSVVFK AEGEHFTDQK GNTIVGSGSG GTTKYFRIPA MCTTSKGTIV    50
    VFADARHNTA SDQSFIDTAA ARSTDGGKTW NKKIAIYNDR VNSKLSRVMD 100
    PTCIVANIQG RETILVMVGK WNNNDKTWGA YRDKAPDTDW DLVLYKSTDD 150
    GVTFSKVETN IHDIVTKNGT ISAMLGGVGS GLQLNDGKLV FPVQMVRTKN 200
    ITTVLNTSFI YSTDGITWSL PSGYCEGFGS ENNIIEFNAS LVNNIRNSGL 250
    RRSFETKDFG KTWTEFPPMD KKVDNRNHGV QGSTITIPSG NKLVAAHSSA 300
    QNKNNDYTRS DISLYAHNLY SGEVKLIDDF YPKVGNASGA GYSCLSYRKN 350
    VDKETLYVVY EANGSIEFQD LSRHLPVIKS YN 382
    Length:382
    Mass (Da):42,073
    Last modified:January 23, 2007 - v4
    Checksum:iC15515CF9C15597E
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti329 – 3291D → A in AAA27168. (PubMed:1602967)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55342 Genomic DNA. Translation: AAA27168.1.
    AE006468 Genomic DNA. Translation: AAL19864.1. Different initiation.
    RefSeqiNP_459905.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL19864; AAL19864; STM0928.
    GeneIDi1252447.
    KEGGistm:STM0928.
    PATRICi32380261. VBISalEnt20916_0978.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55342 Genomic DNA. Translation: AAA27168.1 .
    AE006468 Genomic DNA. Translation: AAL19864.1 . Different initiation.
    RefSeqi NP_459905.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DIL X-ray 1.90 A 2-382 [» ]
    1DIM X-ray 1.60 A 2-382 [» ]
    2SIL X-ray 1.60 A 2-382 [» ]
    2SIM X-ray 1.60 A 2-382 [» ]
    3SIL X-ray 1.05 A 4-382 [» ]
    ProteinModelPortali P29768.
    SMRi P29768. Positions 2-382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM0928.

    Protein family/group databases

    CAZyi GH33. Glycoside Hydrolase Family 33.

    Proteomic databases

    PaxDbi P29768.
    PRIDEi P29768.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL19864 ; AAL19864 ; STM0928 .
    GeneIDi 1252447.
    KEGGi stm:STM0928.
    PATRICi 32380261. VBISalEnt20916_0978.

    Phylogenomic databases

    eggNOGi COG4409.
    KOi K01186.
    OMAi YEANGNI.
    OrthoDBi EOG67DPK3.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-934-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P29768.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR026856. Sialidase_fam.
    IPR008377. Sialidase_trypan.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF5. PTHR10628:SF5. 1 hit.
    PRINTSi PR01803. TCSIALIDASE.
    SUPFAMi SSF50939. SSF50939. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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).

    Entry informationi

    Entry nameiNANH_SALTY
    AccessioniPrimary (citable) accession number: P29768
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 119 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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