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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.2 Publications

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)1 Publication
  2. KM=3.1 mM for 4-methylumbelliferyl-alpha-D-N-acetylneuraminylgalactopyranoside1 Publication
  3. KM=0.23 mM for 4-methylumbelliferyl 3-deoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid (KDN-MU)1 Publication

    pH dependencei

    Optimum pH is 3.5.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei59Substrate1 Publication1
    Binding sitei78Substrate1 Publication1
    Binding sitei84Substrate1 Publication1
    Binding sitei148Substrate1 Publication1
    Binding sitei265Substrate1 Publication1
    Binding sitei322Substrate1 Publication1
    Binding sitei337Substrate; via carbonyl oxygen1 Publication1
    Binding sitei358Substrate1 Publication1
    Binding sitei376Substrate1 Publication1

    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:3.2.1.182 Publications)
    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
    Proteomesi
    • UP000002530 Componenti: Chromosome 4

    Organism-specific databases

    EuPathDBiFungiDB:Afu4g13800.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004294251 – 406Exo-alpha-sialidaseAdd BLAST406
    Signal peptidei1 – 20Sequence analysisAdd BLAST20

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi235N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi396N-linked (GlcNAc...)Sequence analysis1

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

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

    Structurei

    Secondary structure

    1406
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi24 – 27Combined sources4
    Beta strandi32 – 38Combined sources7
    Beta strandi43 – 45Combined sources3
    Beta strandi56 – 65Combined sources10
    Beta strandi71 – 82Combined sources12
    Beta strandi84 – 100Combined sources17
    Helixi105 – 107Combined sources3
    Beta strandi112 – 115Combined sources4
    Beta strandi118 – 129Combined sources12
    Beta strandi135 – 142Combined sources8
    Beta strandi146 – 150Combined sources5
    Turni167 – 169Combined sources3
    Beta strandi172 – 180Combined sources9
    Helixi192 – 195Combined sources4
    Beta strandi218 – 222Combined sources5
    Beta strandi225 – 232Combined sources8
    Beta strandi237 – 242Combined sources6
    Beta strandi248 – 254Combined sources7
    Beta strandi260 – 264Combined sources5
    Beta strandi267 – 278Combined sources12
    Beta strandi286 – 293Combined sources8
    Beta strandi299 – 308Combined sources10
    Beta strandi310 – 316Combined sources7
    Beta strandi318 – 320Combined sources3
    Beta strandi325 – 330Combined sources6
    Helixi344 – 347Combined sources4
    Beta strandi350 – 352Combined sources3
    Beta strandi354 – 363Combined sources10
    Beta strandi369 – 376Combined sources8
    Turni379 – 382Combined sources4
    Beta strandi388 – 395Combined sources8
    Helixi397 – 401Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiQ4WQS0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ4WQS0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni322 – 323Substrate binding2
    Regioni331 – 332Substrate binding2
    Regioni376 – 378Substrate binding3

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000216842.
    InParanoidiQ4WQS0.
    KOiK01186.
    OMAiGTWGNPT.
    OrthoDBiEOG092C2A0R.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PfamiPF13088. BNR_2. 1 hit.
    [Graphical view]
    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
    PDB 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.
    SMRiQ4WQS0.
    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.
    OrthoDBiEOG092C2A0R.

    Miscellaneous databases

    EvolutionaryTraceiQ4WQS0.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PfamiPF13088. BNR_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF50939. SSF50939. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 69 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

    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 one 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.