AFCA_ASPNC
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 25-MAY-2022, entry version 70.
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 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=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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}.
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DR EMBL; AM270362; CAK48586.1; -; Genomic_DNA.
DR AlphaFoldDB; A2R797; -.
DR SMR; A2R797; -.
DR CAZy; GH95; Glycoside Hydrolase Family 95.
DR PaxDb; A2R797; -.
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 Pfam; PF14498; Glyco_hyd_65N_2; 1.
DR PIRSF; PIRSF007663; UCP007663; 1.
DR SUPFAM; SSF48208; SSF48208; 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
