ID SIA_ASPFU Reviewed; 406 AA. AC Q4WQS0; DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 27-MAR-2024, entry version 98. DE RecName: Full=Exo-alpha-sialidase; DE EC=3.2.1.18 {ECO:0000269|PubMed:20652740, ECO:0000269|PubMed:21247893}; DE AltName: Full=Alpha-neuraminidase; DE AltName: Full=N-acylneuraminate glycohydrolase; DE Flags: Precursor; GN ORFNames=AFUA_4G13800; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION. RX PubMed=20652740; DOI=10.1007/s10719-010-9299-9; RA Warwas M.L., Yeung J.H., Indurugalla D., Mooers A.O., Bennet A.J., RA Moore M.M.; RT "Cloning and characterization of a sialidase from the filamentous fungus, RT Aspergillus fumigatus."; RL Glycoconj. J. 27:533-548(2010). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-406 IN COMPLEX WITH SUBSTRATE, RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=21247893; DOI=10.1074/jbc.m110.207043; RA Telford J.C., Yeung J.H., Xu G., Kiefel M.J., Watts A.G., Hader S., RA Chan J., Bennet A.J., Moore M.M., Taylor G.L.; RT "The Aspergillus fumigatus sialidase is a 3-deoxy-D-glycero-D-galacto-2- RT nonulosonic acid hydrolase (KDNase): structural and mechanistic insights."; RL J. Biol. Chem. 286:10783-10792(2011). CC -!- FUNCTION: Sialidase is able to release sialic acid from a wide variety CC of natural substrates including bovine salivary mucin, colominic acid, CC bovine fetuin, a serum glycoprotein containing both alpha-2-6 and CC alpha-2-3-linkages in a ratio of about 3:2, and glycoproteins and CC glycolipids from thermally denatured human lung epithelial cells. Does CC not show any trans-sialidase activity since it is able to remove CC terminal sialic acid residues but is unable to catalyze their transfer CC to the acceptor substrate. 2-keto-3-deoxynononic acid (KDN) is the CC preferred substrate and A.fumigatus can utilize KDN as a sole carbon CC source. {ECO:0000269|PubMed:20652740, ECO:0000269|PubMed:21247893}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- CC (2->8)- glycosidic linkages of terminal sialic acid residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates.; EC=3.2.1.18; CC Evidence={ECO:0000269|PubMed:20652740, ECO:0000269|PubMed:21247893}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.3 mM for 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid CC (MUN) {ECO:0000269|PubMed:20652740}; CC KM=3.1 mM for CC 4-methylumbelliferyl-alpha-D-N-acetylneuraminylgalactopyranoside CC {ECO:0000269|PubMed:20652740}; CC KM=0.23 mM for 4-methylumbelliferyl CC 3-deoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid (KDN-MU) CC {ECO:0000269|PubMed:21247893}; CC pH dependence: CC Optimum pH is 3.5. {ECO:0000269|PubMed:20652740, CC ECO:0000269|PubMed:21247893}; CC -!- INDUCTION: Expression is increased during conidial swelling and CC germination in presence of human serum. {ECO:0000269|PubMed:20652740}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000005; EAL89414.2; -; Genomic_DNA. DR RefSeq; XP_751452.2; XM_746359.2. DR PDB; 2XCY; X-ray; 1.84 A; A/B=21-406. DR PDB; 2XZI; X-ray; 1.45 A; A/B=21-406. DR PDB; 2XZJ; X-ray; 1.84 A; A/B=21-406. DR PDB; 2XZK; X-ray; 1.50 A; A/B=21-406. DR PDB; 4M4N; X-ray; 1.84 A; A/B=1-406. DR PDB; 4M4U; X-ray; 1.84 A; A/B=1-406. DR PDB; 4M4V; X-ray; 1.84 A; A/B=1-406. DR PDBsum; 2XCY; -. DR PDBsum; 2XZI; -. DR PDBsum; 2XZJ; -. DR PDBsum; 2XZK; -. DR PDBsum; 4M4N; -. DR PDBsum; 4M4U; -. DR PDBsum; 4M4V; -. DR AlphaFoldDB; Q4WQS0; -. DR SMR; Q4WQS0; -. DR STRING; 330879.Q4WQS0; -. DR CLAE; NEU33A_ASPFU; -. DR EnsemblFungi; EAL89414; EAL89414; AFUA_4G13800. DR GeneID; 3509581; -. DR KEGG; afm:AFUA_4G13800; -. DR VEuPathDB; FungiDB:Afu4g13800; -. DR eggNOG; ENOG502QSIT; Eukaryota. DR HOGENOM; CLU_024620_1_0_1; -. DR InParanoid; Q4WQS0; -. DR OMA; RTIFMNS; -. DR OrthoDB; 5482010at2759; -. DR BRENDA; 3.2.1.18; 508. DR EvolutionaryTrace; Q4WQS0; -. DR Proteomes; UP000002530; Chromosome 4. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IDA:AspGD. DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central. DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central. DR CDD; cd00260; Sialidase; 1. DR Gene3D; 2.120.10.10; -; 1. DR InterPro; IPR011040; Sialidase. DR InterPro; IPR026856; Sialidase_fam. DR InterPro; IPR036278; Sialidase_sf. DR PANTHER; PTHR10628; SIALIDASE; 1. DR PANTHER; PTHR10628:SF25; SIALIDASE-1; 1. DR Pfam; PF13088; BNR_2; 1. DR SUPFAM; SSF50939; Sialidases; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase; KW Hydrolase; Reference proteome; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..406 FT /note="Exo-alpha-sialidase" FT /id="PRO_0000429425" FT BINDING 59 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 84 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 265 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 322..323 FT /ligand="substrate" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 331..332 FT /ligand="substrate" FT BINDING 337 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 358 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT BINDING 376..378 FT /ligand="substrate" FT BINDING 376 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21247893" FT CARBOHYD 235 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 396 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 32..38 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 56..65 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 71..82 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 84..100 FT /evidence="ECO:0007829|PDB:2XZI" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 112..115 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 118..129 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 146..150 FT /evidence="ECO:0007829|PDB:2XZI" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 172..180 FT /evidence="ECO:0007829|PDB:2XZI" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 218..222 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 225..232 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 248..254 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 260..264 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 267..278 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 286..293 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 299..308 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 310..316 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 325..330 FT /evidence="ECO:0007829|PDB:2XZI" FT HELIX 344..347 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 354..363 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 369..376 FT /evidence="ECO:0007829|PDB:2XZI" FT TURN 379..382 FT /evidence="ECO:0007829|PDB:2XZI" FT STRAND 388..395 FT /evidence="ECO:0007829|PDB:2XZI" FT HELIX 397..401 FT /evidence="ECO:0007829|PDB:2XZI" SQ SEQUENCE 406 AA; 44414 MW; 45D8820EE1EF671A CRC64; MQSMRFMILA LLVQFLPAWA INDPAKSAAP YHDEFPLFRS ANMASPDKLS TGIGFHSFRI PAVVRTTTGR ILAFAEGRRH TNQDFGDINL VYKRTKTTAN NGASPSDWEP LREVVGSGAG TWGNPTPVVD DDNTIYLFLS WNGATYSQNG KDVLPDGTVT KKIDSTWEGR RHLYLTESRD DGNTWSKPVD LTKELTPDGW AWDAVGPGNG IRLTTGELVI PAMGRNIIGR GAPGNRTWSV QRLSGAGAEG TIVQTPDGKL YRNDRPSQKG YRMVARGTLE GFGAFAPDAG LPDPACQGSV LRYNSDAPAR TIFLNSASGT SRRAMRVRIS YDADAKKFNY GRKLEDAKVS GAGHEGGYSS MTKTGDYKIG ALVESDFFND GTGKNSYRAI IWRRFNLSWI LNGPNN //