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Database: UniProt
Entry: A0A0E9LX53_9BACT
LinkDB: A0A0E9LX53_9BACT
Original site: A0A0E9LX53_9BACT 
ID   A0A0E9LX53_9BACT        Unreviewed;       487 AA.
AC   A0A0E9LX53;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:GAO29844.1};
GN   ORFNames=JCM15548_12073 {ECO:0000313|EMBL:GAO29844.1};
OS   Geofilum rubicundum JCM 15548.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Geofilum.
OX   NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO29844.1, ECO:0000313|Proteomes:UP000032900};
RN   [1] {ECO:0000313|EMBL:GAO29844.1, ECO:0000313|Proteomes:UP000032900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO29844.1};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(2015).
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:GAO29844.1}.
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DR   EMBL; BAZW01000014; GAO29844.1; -; Genomic_DNA.
DR   RefSeq; WP_062124443.1; NZ_BAZW01000014.1.
DR   AlphaFoldDB; A0A0E9LX53; -.
DR   STRING; 1236989.JCM15548_12073; -.
DR   OrthoDB; 1389336at2; -.
DR   Proteomes; UP000032900; 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:SF37; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   PIRSF; PIRSF001092; Alpha-L-fucosidase; 2.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032900}.
FT   SITE            320
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ   SEQUENCE   487 AA;  56086 MW;  056F7BBEBB03E279 CRC64;
     MKFILFIAVW MLGQMICAQA IYEDERYVPE TDPVVLQKLE QWQDLKFGLL MHWGHYSQWG
     IVESWSICAE DEDWCRRPHE DYVAYKEAYH NLQKTFDPVS FDPEKWALAA ENAGMKYVVF
     TTKHHDGFSM FDSKYTDYKV TSPDCPFHTN PKANITKEVF DAFRAKGLWA GAYFSKPDWH
     NENYWWSNFA TPDRNVNYDP EAYPERWENF VQFTHNQIME LMTDYGDVDI LWLDGGWVAK
     KSPEFIREWY GRKMENNTSG FIKAQIVNQD IRMDELVDKA REKQPGLIVV DRAVHGKNQN
     YLTPENRVPE HSLPYPWESC IISGGGWSHT PDATYMSGRE GVHLLVDIVA KGGNLLLNVA
     PGPDGTWQQG AYDLLEEMGE WMQVNSEAIY ETRAIAPFKI GNVALTQKNN REIYCIYMAD
     EGESRMPSKI VVPQIQPVPG AKVSLLGSDV ALKWKPQGDG FVIDIPAGLR KSPPSRYAWS
     FKVSEIE
//
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