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Q4WQS0

- SIA_ASPFU

UniProt

Q4WQS0 - SIA_ASPFU

Protein

Exo-alpha-sialidase

Gene

AFUA_4G13800

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    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.1 Publication

    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.2 Publications

    Kineticsi

    1. KM=3.3 mM for 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid (MUN)2 Publications
    2. KM=3.1 mM for 4-methylumbelliferyl-alpha-D-N-acetylneuraminylgalactopyranoside2 Publications
    3. KM=0.23 mM for 4-methylumbelliferyl 3-deoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid (KDN-MU)2 Publications

    pH dependencei

    Optimum pH is 3.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei59 – 591Substrate1 Publication
    Binding sitei78 – 781Substrate1 Publication
    Binding sitei84 – 841Substrate1 Publication
    Binding sitei148 – 1481Substrate1 Publication
    Binding sitei265 – 2651Substrate1 Publication
    Binding sitei322 – 3221Substrate1 Publication
    Binding sitei337 – 3371Substrate; via carbonyl oxygen1 Publication
    Binding sitei358 – 3581Substrate1 Publication
    Binding sitei376 – 3761Substrate1 Publication

    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
    4. exo-alpha-sialidase activity Source: ASPGD

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Protein family/group databases

    mycoCLAPiNEU33A_ASPFU.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exo-alpha-sialidase (EC:3.2.1.18)
    Alternative name(s):
    Alpha-neuraminidase
    N-acylneuraminate glycohydrolase
    Gene namesi
    ORF Names:AFUA_4G13800
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 4

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Exo-alpha-sialidasePRO_0000429425Add
    BLAST
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

    Expression is increased during conidial swelling and germination in presence of human serum.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00008433.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 274
    Beta strandi32 – 387
    Beta strandi43 – 453
    Beta strandi56 – 6510
    Beta strandi71 – 8212
    Beta strandi84 – 10017
    Helixi105 – 1073
    Beta strandi112 – 1154
    Beta strandi118 – 12912
    Beta strandi135 – 1428
    Beta strandi146 – 1505
    Turni167 – 1693
    Beta strandi172 – 1809
    Helixi192 – 1954
    Beta strandi218 – 2225
    Beta strandi225 – 2328
    Beta strandi237 – 2426
    Beta strandi248 – 2547
    Beta strandi260 – 2645
    Beta strandi267 – 27812
    Beta strandi286 – 2938
    Beta strandi299 – 30810
    Beta strandi310 – 3167
    Beta strandi318 – 3203
    Beta strandi325 – 3306
    Helixi344 – 3474
    Beta strandi350 – 3523
    Beta strandi354 – 36310
    Beta strandi369 – 3768
    Turni379 – 3824
    Beta strandi388 – 3958
    Helixi397 – 4015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XCYX-ray1.84A/B21-406[»]
    2XZIX-ray1.45A/B21-406[»]
    2XZJX-ray1.84A/B21-406[»]
    2XZKX-ray1.50A/B21-406[»]
    ProteinModelPortaliQ4WQS0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ4WQS0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni322 – 3232Substrate binding
    Regioni331 – 3322Substrate binding
    Regioni376 – 3783Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000216842.
    KOiK01186.
    OrthoDBiEOG7T4MW1.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    SUPFAMiSSF50939. SSF50939. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q4WQS0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSMRFMILA LLVQFLPAWA INDPAKSAAP YHDEFPLFRS ANMASPDKLS    50
    TGIGFHSFRI PAVVRTTTGR ILAFAEGRRH TNQDFGDINL VYKRTKTTAN 100
    NGASPSDWEP LREVVGSGAG TWGNPTPVVD DDNTIYLFLS WNGATYSQNG 150
    KDVLPDGTVT KKIDSTWEGR RHLYLTESRD DGNTWSKPVD LTKELTPDGW 200
    AWDAVGPGNG IRLTTGELVI PAMGRNIIGR GAPGNRTWSV QRLSGAGAEG 250
    TIVQTPDGKL YRNDRPSQKG YRMVARGTLE GFGAFAPDAG LPDPACQGSV 300
    LRYNSDAPAR TIFLNSASGT SRRAMRVRIS YDADAKKFNY GRKLEDAKVS 350
    GAGHEGGYSS MTKTGDYKIG ALVESDFFND GTGKNSYRAI IWRRFNLSWI 400
    LNGPNN 406
    Length:406
    Mass (Da):44,414
    Last modified:April 17, 2007 - v2
    Checksum:i45D8820EE1EF671A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000005 Genomic DNA. Translation: EAL89414.2.
    RefSeqiXP_751452.2. XM_746359.2.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00008433; CADAFUAP00008433; CADAFUAG00008433.
    GeneIDi3509581.
    KEGGiafm:AFUA_4G13800.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000005 Genomic DNA. Translation: EAL89414.2 .
    RefSeqi XP_751452.2. XM_746359.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XCY X-ray 1.84 A/B 21-406 [» ]
    2XZI X-ray 1.45 A/B 21-406 [» ]
    2XZJ X-ray 1.84 A/B 21-406 [» ]
    2XZK X-ray 1.50 A/B 21-406 [» ]
    ProteinModelPortali Q4WQS0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00008433.

    Protein family/group databases

    mycoCLAPi NEU33A_ASPFU.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00008433 ; CADAFUAP00008433 ; CADAFUAG00008433 .
    GeneIDi 3509581.
    KEGGi afm:AFUA_4G13800.

    Phylogenomic databases

    HOGENOMi HOG000216842.
    KOi K01186.
    OrthoDBi EOG7T4MW1.

    Miscellaneous databases

    EvolutionaryTracei Q4WQS0.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    SUPFAMi SSF50939. SSF50939. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiSIA_ASPFU
    AccessioniPrimary (citable) accession number: Q4WQS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 11, 2014
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 57 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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