ID   AFCA_ASPOR              Reviewed;         723 AA.
AC   Q2USL3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   24-JAN-2024, entry version 67.
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=AO090005000382;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE55452.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007151; BAE55452.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2USL3; -.
DR   SMR; Q2USL3; -.
DR   STRING; 510516.Q2USL3; -.
DR   CAZy; GH95; Glycoside Hydrolase Family 95.
DR   GlyCosmos; Q2USL3; 10 sites, No reported glycans.
DR   OrthoDB; 1387368at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
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   Gene3D; 2.70.98.50; putative glycoside hydrolase family protein from bacillus halodurans; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR049053; AFCA-like_C.
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   Pfam; PF21307; Glyco_hydro_95_C; 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..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..723
FT                   /note="Probable alpha-fucosidase A"
FT                   /id="PRO_0000394703"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        558
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        595
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   723 AA;  78538 MW;  8F22F67C3367E604 CRC64;
     MRSLVLLGMS SLATANSLWS SKAASWDTTN EAYTLGNGKL GVMPFGEPGA EKLNLNHDEL
     WEGGPFEVNG YRGGNPNSSM TEILSEVRDE IWKKGTGNDS RLHGDTDGYG SFHSLANLTI
     AIDGIDKVSD YTRSLDLGTG IHTTTYSTGK GKYTTDVYCS YPAQVCIYKL NSTATLSKVT
     IYFDQLVEES SLWNATCDSD FARLRGVTQE GPPRGMTYDT IARSSIPGRC DSSTGKLAIN
     ARNSSSLTIV IGAGTDFDGT KGTAATDYTF KGEDPAEYVE KITSSALSQS ESKLRTEHIE
     DYSGLMSAFT LDLPDTQDST GTELSTLITN YNANKTDGDP YLEKLLFDYG RHLFISSSRA
     NSLPPNLQGV WSPTKNAAWS GDYHANINLQ MNLWGAEATG LGELTVAVFN YMEQNWMPRG
     AETAELLYGG AGWVTHDEMN IFGHTGSLVV NPCTSPEQGP TTFGCTHWQQ LIHQVYENAI
     QGAEIAGETD STLLKDIKDQ LPRLDKGLHI GTWGQIKEWK LPDSYDYEKE GNEHRHLSHL
     VGWYPGWSLS SYFNGYNNAT IQSAVNTSLI SRGVGLYTNA GWEKVWRSAC WARLNNTEKA
     HYELRLTIDQ NIGQSGLSLY SGGDTPSGAF QIDANFGYLG AVLSMLVVDM PLDSTHSEDD
     VRTVVLGPAI PAAWAGGSVK GLRLRGGGSV DFSWDSEGLV DKASATGVSS NVRIVNVEGT
     VLV
//