ID   W4NBL6_9BIFI            Unreviewed;       497 AA.
AC   W4NBL6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:ETY71851.1};
GN   ORFNames=BMOU_0589 {ECO:0000313|EMBL:ETY71851.1};
OS   Bifidobacterium moukalabense DSM 27321.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1435051 {ECO:0000313|EMBL:ETY71851.1, ECO:0000313|Proteomes:UP000019155};
RN   [1] {ECO:0000313|EMBL:ETY71851.1, ECO:0000313|Proteomes:UP000019155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27321 {ECO:0000313|EMBL:ETY71851.1,
RC   ECO:0000313|Proteomes:UP000019155};
RX   PubMed=24558236;
RA   Lugli G.A., Duranti S., Milani C., Turroni F., Viappiani A., Mangifesta M.,
RA   van Sinderen D., Ventura M.;
RT   "The Genome Sequence of Bifidobacterium moukalabense DSM 27321 Highlights
RT   the Close Phylogenetic Relatedness with the Bifidobacterium dentium
RT   Taxon.";
RL   Genome Announc. 2:e00048-e00014(2014).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETY71851.1}.
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DR   EMBL; AZMV01000002; ETY71851.1; -; Genomic_DNA.
DR   RefSeq; WP_034874713.1; NZ_AZMV01000002.1.
DR   AlphaFoldDB; W4NBL6; -.
DR   STRING; 1435051.BMOU_0589; -.
DR   PATRIC; fig|1435051.3.peg.585; -.
DR   eggNOG; COG3669; Bacteria.
DR   OrthoDB; 5526311at2; -.
DR   Proteomes; UP000019155; Unassembled WGS sequence.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR000933; Glyco_hydro_29.
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   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
SQ   SEQUENCE   497 AA;  56781 MW;  43A4A3FA538F438A CRC64;
     MIDMNTVEAV IASGPYADTW ESLSQAPTPA WFNDAKFGIF THWGLYTVPE YRNEWYSRNM
     YIEGYPEFEH HVSAYGPQNR FGYKDFIPMF TAERFDADEW LDLFAAAGAR YYFPVSEHHD
     GYQMYRSELS HWNTFETGPH RDVLGELRDA TCAHGLHFAT SNHRAEHWWF MGHGKDFDSD
     IKEPLQKGDF YWPAMPEPNE FDIHSTPAPS AEYLEDWLLR VCEIIDNYRP ELLYFDWWVQ
     HESFKPYMRK LVAFYYNRGV QWGRNVSICY KYDGLAWGAG IVDVERGGFA DATPFAWQTD
     TAIARNSWCY TNSLDYKTLA ELIVSLIDAV SKNGNLLLNV GPRADGSIAD HDRELLLGIG
     DWLRANGEGI YGTRPWRLTQ EGPTKQAEGM FADQQPTAWT AADWRFTTKN GAIYAFCLNP
     DDIADNHETS CETLTMSTFA AYHDGIKPPF NGIVASVEQL GAGSVRFRRG DEALEISPLP
     REPDQKGLPI GFKITVG
//