SIA_ARTBC
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 03-AUG-2022, entry version 48.
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}.
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DR EMBL; ABSU01000034; EFE30089.1; -; Genomic_DNA.
DR RefSeq; XP_003010729.1; XM_003010683.1.
DR AlphaFoldDB; D4B4P1; -.
DR SMR; D4B4P1; -.
DR STRING; 663331.D4B4P1; -.
DR EnsemblFungi; EFE30089; EFE30089; ARB_03431.
DR GeneID; 9524842; -.
DR KEGG; abe:ARB_03431; -.
DR eggNOG; ENOG502QSIT; Eukaryota.
DR HOGENOM; CLU_024620_1_0_1; -.
DR OMA; GRRHLYL; -.
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 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 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
