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Database: UniProt
Entry: F4WMR9_ACREC
LinkDB: F4WMR9_ACREC
Original site: F4WMR9_ACREC 
ID   F4WMR9_ACREC            Unreviewed;       388 AA.
AC   F4WMR9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN   ORFNames=G5I_07053 {ECO:0000313|EMBL:EGI64546.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI64546.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC       1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC       carbohydrate moieties of glycoproteins.
CC       {ECO:0000256|ARBA:ARBA00004071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0) + H2O = a
CC         neolactoside nLc4Cer(d18:0) + L-fucose; Xref=Rhea:RHEA:49308,
CC         ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:91119,
CC         ChEBI:CHEBI:91121; Evidence={ECO:0000256|ARBA:ARBA00000419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC         Evidence={ECO:0000256|ARBA:ARBA00000419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + H2O = a
CC         neolactoside nLc4Cer(d18:1(4E)) + L-fucose; Xref=Rhea:RHEA:48224,
CC         ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006,
CC         ChEBI:CHEBI:28691; Evidence={ECO:0000256|ARBA:ARBA00000321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC         Evidence={ECO:0000256|ARBA:ARBA00000321};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951}.
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DR   EMBL; GL888218; EGI64546.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WMR9; -.
DR   STRING; 103372.F4WMR9; -.
DR   EnsemblMetazoa; XM_011057737.1; XP_011056039.1; LOC105147022.
DR   eggNOG; KOG3340; Eukaryota.
DR   InParanoid; F4WMR9; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR031919; Fucosidase_C.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR018526; Glyco_hydro_29_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   Pfam; PF16757; Fucosidase_C; 1.
DR   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..388
FT                   /note="alpha-L-fucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003318727"
FT   DOMAIN          303..385
FT                   /note="Alpha-L-fucosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16757"
SQ   SEQUENCE   388 AA;  44846 MW;  F6DA88D831CCEB91 CRC64;
     MMLFVHIIVC IVLIFCVSVK ADYTVIVRTE EENFVSILTK TPKYVPTWPS LDSRPLPVWY
     DVAKFGIFIH WGVFSVPSFG SEWFWNNWKS ELAEAIRSKT DLKFGLYHSM YEWYNPLYVT
     DKQNNFTTDR FVIHKIIPEL YELIETYKPE VVWSDGDWEA SDSYWKSKEF LAWLYNKSPV
     KDTVVVNDRW GSNIPCHHGD FFTCTDRFNP GVLLPHKWEN CMTIDKKSWG YRRNAVLSEY
     YTLVGLVKEL VITVSCGGNL LMNVGPTKDG IITPIFEERL RGMGAWLAVN GEAIYDTKPW
     TVQNDTLTGS VWYTLSKNEK QLYASILEWP DDNILLLGSL KLSKNSQIHL LGYSSIIPWK
     QSDNKLVITL PANAHRGEPA WVLRIGTL
//
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