SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q4WQS0

- SIA_ASPFU

UniProt

Q4WQS0 - SIA_ASPFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

pH dependencei

Optimum pH is 3.5.

Sites

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

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
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: Chromosome 4

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Exo-alpha-sialidase
PRO_0000429425Add
BLAST
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiQ4WQS0.

Family & Domainsi

Region

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

Sequence similaritiesi

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

« 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: September 3, 2014
This is version 56 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