ID   AFCA_EMENI              Reviewed;         809 AA.
AC   Q5AU81; C8V6V7; Q1HFQ8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Alpha-fucosidase A;
DE            EC=3.2.1.51 {ECO:0000269|PubMed:16844780};
DE   AltName: Full=Alpha-L-fucoside fucohydrolase A;
DE   Flags: Precursor;
GN   Name=afcA; ORFNames=AN8149;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA   Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT   "Development and application of a suite of polysaccharide-degrading enzymes
RT   for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Alpha-fucosidase involved in degradation of fucosylated
CC       xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton
CC       xyloglucan oligomers but not active on paranitrophenyl-fucoside.
CC       {ECO:0000269|PubMed:16844780}.
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         Evidence={ECO:0000269|PubMed:16844780};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 95 family. {ECO:0000305}.
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DR   EMBL; DQ490516; ABF50892.1; -; mRNA.
DR   EMBL; AACD01000141; EAA59171.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF73981.1; -; Genomic_DNA.
DR   RefSeq; XP_681418.1; XM_676326.1.
DR   AlphaFoldDB; Q5AU81; -.
DR   SMR; Q5AU81; -.
DR   STRING; 162425.CADANIAP00004184; -.
DR   CAZy; GH95; Glycoside Hydrolase Family 95.
DR   EnsemblFungi; CBF73981; CBF73981; ANIA_08149.
DR   EnsemblFungi; EAA59171; EAA59171; AN8149.2.
DR   GeneID; 2869274; -.
DR   KEGG; ani:AN8149.2; -.
DR   VEuPathDB; FungiDB:AN8149; -.
DR   eggNOG; ENOG502QQ9E; Eukaryota.
DR   HOGENOM; CLU_004617_2_2_1; -.
DR   InParanoid; Q5AU81; -.
DR   OMA; KVWRGAC; -.
DR   OrthoDB; 614028at2759; -.
DR   BioCyc; MetaCyc:MON-18214; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010411; P:xyloglucan metabolic process; IDA:UniProtKB.
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   Pfam; PF14498; Glyco_hyd_65N_2; 1.
DR   PIRSF; PIRSF007663; UCP007663; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..809
FT                   /note="Alpha-fucosidase A"
FT                   /id="PRO_0000394704"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        614
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        642
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        681
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   809 AA;  88536 MW;  FDF201647A4BF899 CRC64;
     MRKTTLFLAV TFATSNAQGR ALRSSSPATY GTTDGSDYIL KTGYLIGNGK LGVIPFGPPD
     TEKLNLNVDS LWSGGPFEVE NYTGGNPSSP IYDALPGIRE RIFENGTGGM EELLGSGNHY
     GSSRVLGNIT IALDGVEAYS KYKRTLDLSD GVHRTSFTIA NRTTAALKSS IFCSYPDQVC
     VYHLESASDA RLPKVTISIE NLLVNQSLLQ TSCESEAKRA VLRHSGVTQA GPPEGMKYAA
     VAEVVNPRSS VTTCLGEGAL QISSRKKQLT IIIGAATNYD QKAGNAKSGW SFKNAKDPAS
     IVDGIASAAG WKGYQRLLDR HVKDYKKLMG DFSLELPDTT DSASKDTSEL IEKYSYASAT
     GNPYLENLLL DYARHLLVSS SRPNSLPANL QGRWTESLTP SWSADYHANI NLQMNYWLAD
     QTGLGETQHA LWNYMADTWV PRGTETARLL YNASGWVVHN EINIFGFTAM KEDAGWANYP
     AAAAWMMQHV WDNFDYTHDT AWLVSQGYAL LKGIASFWLS SLQEDKFFND GSLVVNPCNS
     PETGPTTFGC THYQQLIHQV FETVLAAQEY IHESDTKFVD SVASALERLD TGLHLSSWGG
     LKEWKLPDSY GYDNMSTHRH LSHLAGWYPG YSISSFAHGY RNKTIQDAVK ETLTARGMGN
     AADANAGWAK VWRAACWARL NDSSMAYDEL RYAIDENFVG NGLSMYWGAS PPFQIDANFG
     FAGAVLSMLV VDLPTPRSDP GQRTVVLGPA IPSAWGGGRA KGLRLRGGAK VDFGWDKRGV
     VNWVNIVKRG KGTSRVKLVN KEGDILAEM