ID AFCA_ASPNC Reviewed; 793 AA. AC A2R797; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 13-SEP-2023, entry version 74. DE RecName: Full=Probable alpha-fucosidase A; DE EC=3.2.1.51; DE AltName: Full=Alpha-L-fucoside fucohydrolase A; DE Flags: Precursor; GN Name=afcA; ORFNames=An16g02760; OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=425011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513; RX PubMed=17259976; DOI=10.1038/nbt1282; RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M., RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory Aspergillus RT niger CBS 513.88."; RL Nat. Biotechnol. 25:221-231(2007). CC -!- FUNCTION: Alpha-fucosidase involved in degradation of fucosylated CC xyloglucans. Hydrolyzes alpha-1,2-linked fucose (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose; CC Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 95 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; AM270362; CAK48586.1; -; Genomic_DNA. DR AlphaFoldDB; A2R797; -. DR SMR; A2R797; -. DR CAZy; GH95; Glycoside Hydrolase Family 95. DR GlyCosmos; A2R797; 13 sites, No reported glycans. DR EnsemblFungi; CAK48586; CAK48586; An16g02760. DR VEuPathDB; FungiDB:An16g02760; -. DR HOGENOM; CLU_004617_2_2_1; -. DR Proteomes; UP000006706; Chromosome 5R. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR016518; Alpha-L-fucosidase. DR InterPro; IPR027414; GH95_N_dom. DR PANTHER; PTHR31084:SF3; ALPHA-FUCOSIDASE A; 1. DR PANTHER; PTHR31084; ALPHA-L-FUCOSIDASE 2; 1. DR Pfam; PF14498; Glyco_hyd_65N_2; 1. DR PIRSF; PIRSF007663; UCP007663; 1. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; KW Polysaccharide degradation; Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..793 FT /note="Probable alpha-fucosidase A" FT /id="PRO_5000221152" FT CARBOHYD 30 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 179 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 199 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 234 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 323 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 597 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 622 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 660 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 757 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 793 AA; 86565 MW; 4F510561054875E2 CRC64; MLISGSSAAL CALALPFAAA KSLWSDSPGN YSSFITTAFP LGNGRLGAMP IGSYDKEIVN LNVDSLWRGG PFESPTYSGG NPNVSKAGAL PGIREWIFQN GTGNVSALLG EYPYYGSYQV LANLTIDMGE LSDIDGYRRN LDLDSAVYSD HFSTGETYIE REAFCSYPDN VCVYRLSSNS SLPEITFGLE NQLTSPAPNV SCHGNSISLY GQTYPVIGMI YNARVTVVVP GSSNTTDLCS SSTVKVPEGE KEVFLVFAAD TNYEASNGNS KASFSFKGEN PYMKVLQTAT NAAKKSYSAL KSSHVKDYQG VFNKFTLTLP DPNGSADRPT TELLSSYSQP GDPYVENLLF DYGRYLFISS SRPGSLPPNL QGLWTESYSP AWSGDYHANI NLQMNHWAVD QTGLGELTEP LWTYMAETWM PRGAETAELL YGTSEGWVTH DEMNTFGHTA MKDVAQWADY PATNAWMSHH VWDHFDYSQD SAWYRETGYP ILKGAAQFWL SQLVKDEYFK DGTLVVNPCN SPEHGPTLTP QTFGCTHYQQ LIWELFDHVL QGWTASGDDD TSFKNAITSK FSTLDPGIHI GSWGQIQEWK LDIDVKNDTH RHLSNLYGWY PGYIISSVHG SNKTITDAVE TTLYSRGTGV EDSNTGWAKV WRSACWALLN VTDEAYSELS LAIQDNFAEN GFDMYSGSPP FQIDANFGLV GAMVQMLIRD SDRSSADASA GKTQDVLLGP AIPAAWGGGS VGGLRLRGGG VVSFSWNDSG VVDSCKADLS ARGSDVSQVK FYVAGGRAID CSS //