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P29768

- NANH_SALTY

UniProt

P29768 - NANH_SALTY

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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

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
Complete GO annotation...

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 – 95Combined sources
Helixi29 – 313Combined sources
Beta strandi35 – 439Combined sources
Beta strandi49 – 5810Combined sources
Beta strandi62 – 643Combined sources
Beta strandi66 – 7813Combined sources
Beta strandi81 – 866Combined sources
Turni93 – 953Combined sources
Beta strandi97 – 10812Combined sources
Beta strandi111 – 12313Combined sources
Helixi128 – 1303Combined sources
Beta strandi133 – 1364Combined sources
Beta strandi141 – 1499Combined sources
Beta strandi155 – 1573Combined sources
Helixi161 – 1688Combined sources
Beta strandi170 – 1767Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi189 – 1979Combined sources
Beta strandi204 – 21916Combined sources
Beta strandi232 – 2376Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi254 – 2618Combined sources
Turni267 – 2715Combined sources
Beta strandi283 – 2897Combined sources
Beta strandi292 – 3009Combined sources
Beta strandi312 – 3176Combined sources
Turni319 – 3213Combined sources
Beta strandi324 – 3318Combined sources
Beta strandi343 – 3508Combined sources
Beta strandi353 – 36210Combined sources
Beta strandi365 – 3706Combined sources
Helixi372 – 3743Combined sources
Helixi375 – 3795Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTVEKSVVFK AEGEHFTDQK GNTIVGSGSG GTTKYFRIPA MCTTSKGTIV
60 70 80 90 100
VFADARHNTA SDQSFIDTAA ARSTDGGKTW NKKIAIYNDR VNSKLSRVMD
110 120 130 140 150
PTCIVANIQG RETILVMVGK WNNNDKTWGA YRDKAPDTDW DLVLYKSTDD
160 170 180 190 200
GVTFSKVETN IHDIVTKNGT ISAMLGGVGS GLQLNDGKLV FPVQMVRTKN
210 220 230 240 250
ITTVLNTSFI YSTDGITWSL PSGYCEGFGS ENNIIEFNAS LVNNIRNSGL
260 270 280 290 300
RRSFETKDFG KTWTEFPPMD KKVDNRNHGV QGSTITIPSG NKLVAAHSSA
310 320 330 340 350
QNKNNDYTRS DISLYAHNLY SGEVKLIDDF YPKVGNASGA GYSCLSYRKN
360 370 380
VDKETLYVVY EANGSIEFQD LSRHLPVIKS YN
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. Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 120 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