Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

    GO - Biological processi

    Complete GO annotation...

    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 Componenti: Chromosome 4

    Organism-specific databases

    EuPathDBiFungiDB:Afu4g13800.

    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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4M4NX-ray1.84A/B1-406[»]
    4M4UX-ray1.84A/B1-406[»]
    4M4VX-ray1.84A/B1-406[»]
    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.
    InParanoidiQ4WQS0.
    KOiK01186.
    OMAiGTWGNPT.
    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

            10         20         30         40         50
    MQSMRFMILA LLVQFLPAWA INDPAKSAAP YHDEFPLFRS ANMASPDKLS
    60 70 80 90 100
    TGIGFHSFRI PAVVRTTTGR ILAFAEGRRH TNQDFGDINL VYKRTKTTAN
    110 120 130 140 150
    NGASPSDWEP LREVVGSGAG TWGNPTPVVD DDNTIYLFLS WNGATYSQNG
    160 170 180 190 200
    KDVLPDGTVT KKIDSTWEGR RHLYLTESRD DGNTWSKPVD LTKELTPDGW
    210 220 230 240 250
    AWDAVGPGNG IRLTTGELVI PAMGRNIIGR GAPGNRTWSV QRLSGAGAEG
    260 270 280 290 300
    TIVQTPDGKL YRNDRPSQKG YRMVARGTLE GFGAFAPDAG LPDPACQGSV
    310 320 330 340 350
    LRYNSDAPAR TIFLNSASGT SRRAMRVRIS YDADAKKFNY GRKLEDAKVS
    360 370 380 390 400
    GAGHEGGYSS MTKTGDYKIG ALVESDFFND GTGKNSYRAI IWRRFNLSWI

    LNGPNN
    Length:406
    Mass (Da):44,414
    Last modified:April 17, 2007 - v2
    Checksum:i45D8820EE1EF671A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAHF01000005 Genomic DNA. Translation: EAL89414.2.
    RefSeqiXP_751452.2. XM_746359.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4M4NX-ray1.84A/B1-406[»]
    4M4UX-ray1.84A/B1-406[»]
    4M4VX-ray1.84A/B1-406[»]
    ProteinModelPortaliQ4WQS0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    mycoCLAPiNEU33A_ASPFU.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    EuPathDBiFungiDB:Afu4g13800.

    Phylogenomic databases

    HOGENOMiHOG000216842.
    InParanoidiQ4WQS0.
    KOiK01186.
    OMAiGTWGNPT.
    OrthoDBiEOG7T4MW1.

    Miscellaneous databases

    EvolutionaryTraceiQ4WQS0.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 64 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.