SIA_ASPFU
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 03-AUG-2022, entry version 93.
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 Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
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 / Af293 / CBS 101355 / FGSC A1100;
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 4-methylumbelliferyl-alpha-D-N-
CC acetylneuraminylgalactopyranoside {ECO:0000269|PubMed:20652740};
CC KM=0.23 mM for 4-methylumbelliferyl 3-deoxy-D-glycero-alpha-D-
CC 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}.
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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; 746128.CADAFUBP00006890; -.
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; GRRHLYL; -.
DR OrthoDB; 877888at2759; -.
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 InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628; PTHR10628; 1.
DR Pfam; PF13088; BNR_2; 1.
DR SUPFAM; SSF50939; SSF50939; 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
