ID   SIA_ARTBC               Reviewed;         408 AA.
AC   D4B4P1;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Exo-alpha-sialidase ARB_03431 {ECO:0000305};
DE            EC=3.2.1.18 {ECO:0000250|UniProtKB:Q4WQS0};
DE   AltName: Full=Alpha-neuraminidase ARB_03431 {ECO:0000305};
DE   AltName: Full=N-acylneuraminate glycohydrolase ARB_03431 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_03431;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Sialidase is able to release sialic acid from a wide variety
CC       of natural substrates. {ECO:0000250|UniProtKB:Q4WQS0}.
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:0000250|UniProtKB:Q4WQS0};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
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; ABSU01000034; EFE30089.1; -; Genomic_DNA.
DR   RefSeq; XP_003010729.1; XM_003010683.1.
DR   AlphaFoldDB; D4B4P1; -.
DR   SMR; D4B4P1; -.
DR   GeneID; 9524842; -.
DR   KEGG; abe:ARB_03431; -.
DR   eggNOG; ENOG502QSIT; Eukaryota.
DR   HOGENOM; CLU_024620_1_0_1; -.
DR   OMA; RTIFMNS; -.
DR   OrthoDB; 5482010at2759; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; PF13859; BNR_3; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..408
FT                   /note="Exo-alpha-sialidase ARB_03431"
FT                   /id="PRO_5003054503"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         324..325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         333..334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         378..380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4WQS0"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   408 AA;  44403 MW;  92E2434E1EAB1BC5 CRC64;
     MGIKQWLLSL VVVAISATAT QARVDDPAGK AAQYHKEYAL FRSANMPSPD KLASGVGFHS
     FRIPAVVRTN TGRILAFAEG RRHNNRDYGD INLVYKRTKS PTNNGENPTD WESLREVVGT
     GPHTWGNPTP VVDGNTIYLF LSMNDGAYSQ NGGNTLPDGT KTKTIDSTWV GRRHLYLTTS
     TDDGDTWTKP VDMTKTLTPD GQAWDAVGPG NGIKLSTGEL VIPAQGRNII GHGPSGNRTW
     SMQVLKGAGS EGTICQTPDG KLMRNDRPGP MGHRSVARGT LAGFGPFATD NGLPDPACQG
     SILSYNSDEP ARTIFMNSAS TDRRTAMRVR ISYDKDAAKF NFGRELKDAP LGNVGNEGGY
     SSMTKTSDYK IGALVESDWY EDKGGEKSHR CIIWRRFNLS WIINGPNN
//