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Showing Protein Exo-alpha-sialidase (HMDBP14218)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP14218
Secondary Accession Numbers None
Name Exo-alpha-sialidase
Synonyms
  1. Alpha-neuraminidase
  2. N-acylneuraminate glycohydrolase
Gene Name (REFSEQ) EXTRACELLULAR SIALIDASE/NEURAMINIDASE
Protein Type Unknown
Biological Properties
General Function Not Available
Specific 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.
Pathways
  • Other glycan degradation
  • Sphingolipid metabolism
Reactions Not Available
GO Classification
Biological Process
ganglioside catabolic process
oligosaccharide catabolic process
Cellular Component
cytoplasm
membrane
intracellular membrane-bounded organelle
Molecular Function
exo-alpha-(2->3)-sialidase activity
exo-alpha-(2->6)-sialidase activity
exo-alpha-(2->8)-sialidase activity
exo-alpha-sialidase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 406
Molecular Weight 44413.365
Theoretical pI 9.388
Pfam Domain Function
Signals
  • 1-20;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q4WQS0
UniProtKB/Swiss-Prot Entry Name SIA_ASPFU
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Nierman WC, Pain A, Anderson MJ, Wortman JR, Kim HS, Arroyo J, Berriman M, Abe K, Archer DB, Bermejo C, Bennett J, Bowyer P, Chen D, Collins M, Coulsen R, Davies R, Dyer PS, Farman M, Fedorova N, Fedorova N, Feldblyum TV, Fischer R, Fosker N, Fraser A, Garcia JL, Garcia MJ, Goble A, Goldman GH, Gomi K, Griffith-Jones S, Gwilliam R, Haas B, Haas H, Harris D, Horiuchi H, Huang J, Humphray S, Jimenez J, Keller N, Khouri H, Kitamoto K, Kobayashi T, Konzack S, Kulkarni R, Kumagai T, Lafon A, Latge JP, Li W, Lord A, Lu C, Majoros WH, May GS, Miller BL, Mohamoud Y, Molina M, Monod M, Mouyna I, Mulligan S, Murphy L, O'Neil S, Paulsen I, Penalva MA, Pertea M, Price C, Pritchard BL, Quail MA, Rabbinowitsch E, Rawlins N, Rajandream MA, Reichard U, Renauld H, Robson GD, Rodriguez de Cordoba S, Rodriguez-Pena JM, Ronning CM, Rutter S, Salzberg SL, Sanchez M, Sanchez-Ferrero JC, Saunders D, Seeger K, Squares R, Squares S, Takeuchi M, Tekaia F, Turner G, Vazquez de Aldana CR, Weidman J, White O, Woodward J, Yu JH, Fraser C, Galagan JE, Asai K, Machida M, Hall N, Barrell B, Denning DW: Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus. Nature. 2005 Dec 22;438(7071):1151-6. doi: 10.1038/nature04332. [PubMed:16372009 ]
  2. Warwas ML, Yeung JH, Indurugalla D, Mooers AO, Bennet AJ, Moore MM: Cloning and characterization of a sialidase from the filamentous fungus, Aspergillus fumigatus. Glycoconj J. 2010 Jul;27(5):533-48. doi: 10.1007/s10719-010-9299-9. Epub 2010 Jul 23. [PubMed:20652740 ]
  3. Telford JC, Yeung JH, Xu G, Kiefel MJ, Watts AG, Hader S, Chan J, Bennet AJ, Moore MM, Taylor GL: The Aspergillus fumigatus sialidase is a 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid hydrolase (KDNase): structural and mechanistic insights. J Biol Chem. 2011 Mar 25;286(12):10783-92. doi: 10.1074/jbc.M110.207043. Epub 2011 Jan 19. [PubMed:21247893 ]