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Q4WQS0 (SIA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 55. Feed History...

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

Names and origin

Protein namesRecommended name:
Exo-alpha-sialidase

EC=3.2.1.18
Alternative name(s):
Alpha-neuraminidase
N-acylneuraminate glycohydrolase
Gene names
ORF Names:AFUA_4G13800
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sialidase is able to release sialic acid from a wide variety of natural substrates including bovine salivary mucin, colominic acid, bovine fetuin, a serum glycoprotein containing both alpha-2-6 and alpha-2-3-linkages in a ratio of about 3:2, and glycoproteins and glycolipids from thermally denatured human lung epithelial cells. Does not show any trans-sialidase activity since it is able to remove terminal sialic acid residues but is unable to catalyze their transfer to the acceptor substrate. 2-keto-3-deoxynononic acid (KDN) is the preferred substrate and A.fumigatus can utilize KDN as a sole carbon source. Ref.2

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. Ref.2 Ref.3

Induction

Expression is increased during conidial swelling and germination in presence of human serum. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Biophysicochemical properties

Kinetic parameters:

KM=3.3 mM for 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid (MUN) Ref.2 Ref.3

KM=3.1 mM for 4-methylumbelliferyl-alpha-D-N-acetylneuraminylgalactopyranoside

KM=0.23 mM for 4-methylumbelliferyl 3-deoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid (KDN-MU)

pH dependence:

Optimum pH is 3.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Exo-alpha-sialidase
PRO_0000429425
Signal peptide1 – 2020 Potential

Regions

Region322 – 3232Substrate binding
Region331 – 3322Substrate binding
Region376 – 3783Substrate binding

Sites

Binding site591Substrate
Binding site781Substrate
Binding site841Substrate
Binding site1481Substrate
Binding site2651Substrate
Binding site3221Substrate
Binding site3371Substrate; via carbonyl oxygen
Binding site3581Substrate
Binding site3761Substrate

Amino acid modifications

Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WQS0 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 45D8820EE1EF671A

FASTA40644,414
        10         20         30         40         50         60 
MQSMRFMILA LLVQFLPAWA INDPAKSAAP YHDEFPLFRS ANMASPDKLS TGIGFHSFRI 

        70         80         90        100        110        120 
PAVVRTTTGR ILAFAEGRRH TNQDFGDINL VYKRTKTTAN NGASPSDWEP LREVVGSGAG 

       130        140        150        160        170        180 
TWGNPTPVVD DDNTIYLFLS WNGATYSQNG KDVLPDGTVT KKIDSTWEGR RHLYLTESRD 

       190        200        210        220        230        240 
DGNTWSKPVD LTKELTPDGW AWDAVGPGNG IRLTTGELVI PAMGRNIIGR GAPGNRTWSV 

       250        260        270        280        290        300 
QRLSGAGAEG TIVQTPDGKL YRNDRPSQKG YRMVARGTLE GFGAFAPDAG LPDPACQGSV 

       310        320        330        340        350        360 
LRYNSDAPAR TIFLNSASGT SRRAMRVRIS YDADAKKFNY GRKLEDAKVS GAGHEGGYSS 

       370        380        390        400 
MTKTGDYKIG ALVESDFFND GTGKNSYRAI IWRRFNLSWI LNGPNN 

« Hide

References

« Hide 'large scale' references
[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]"Cloning and characterization of a sialidase from the filamentous fungus, Aspergillus fumigatus."
Warwas M.L., Yeung J.H., Indurugalla D., Mooers A.O., Bennet A.J., Moore M.M.
Glycoconj. J. 27:533-548(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
[3]"The Aspergillus fumigatus sialidase is a 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid hydrolase (KDNase): structural and mechanistic insights."
Telford J.C., Yeung J.H., Xu G., Kiefel M.J., Watts A.G., Hader S., Chan J., Bennet A.J., Moore M.M., Taylor G.L.
J. Biol. Chem. 286:10783-10792(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-406 IN COMPLEX WITH SUBSTRATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000005 Genomic DNA. Translation: EAL89414.2.
RefSeqXP_751452.2. XM_746359.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XCYX-ray1.84A/B21-406[»]
2XZIX-ray1.45A/B21-406[»]
2XZJX-ray1.84A/B21-406[»]
2XZKX-ray1.50A/B21-406[»]
ProteinModelPortalQ4WQS0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00008433.

Protein family/group databases

mycoCLAPNEU33A_ASPFU.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00008433; CADAFUAP00008433; CADAFUAG00008433.
GeneID3509581.
KEGGafm:AFUA_4G13800.

Phylogenomic databases

HOGENOMHOG000216842.
KOK01186.
OrthoDBEOG7T4MW1.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ4WQS0.

Entry information

Entry nameSIA_ASPFU
AccessionPrimary (citable) accession number: Q4WQS0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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