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Database: UniProt
Entry: Q5LEF6_BACFN
LinkDB: Q5LEF6_BACFN
Original site: Q5LEF6_BACFN 
ID   Q5LEF6_BACFN            Unreviewed;       420 AA.
AC   Q5LEF6;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:CAH07495.1};
GN   ORFNames=BF9343_1714 {ECO:0000313|EMBL:CAH07495.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH07495.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH07495.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC   Onslow {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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}.
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DR   EMBL; CR626927; CAH07495.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5LEF6; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   PaxDb; 272559-BF9343_1714; -.
DR   KEGG; bfs:BF9343_1714; -.
DR   eggNOG; COG3669; Bacteria.
DR   HOGENOM; CLU_002934_1_1_10; -.
DR   Proteomes; UP000006731; Chromosome.
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   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR000933; Glyco_hydro_29.
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   PIRSF; PIRSF001092; Alpha-L-fucosidase; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..420
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004259220"
FT   SITE            293
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ   SEQUENCE   420 AA;  48932 MW;  9966302B8C75FE2E CRC64;
     MKKYCLLLFC LICIPLMGQS TYKPDWESID KRPVPAWFEN AKFGIFIHWG LYSVPAWSPK
     GTYSEWYKYW LDKKTLMGNG NFTGTEIYDY HRKMYGEDFT YADFAPMFKA LSYDPEEWAD
     LFEHSGAKYV VLTTKHHDGF ALWPSREASI SYGRPWNSME IGAHRDLVGE YVNALRKTDI
     KVGCYFSLRE WDNPLYNKET MDLFYERHWF PQLQDLVNRY KPDLIWADGP DQINDKQWQA
     ERTLAWLYSE SPVKDSIVVN DRWANNTGKK HGDYYTREYS NTNSSYNKPW EECRGIGLSF
     GYNQNEDLGD YTSPKALILT LVNIVSQGGN LLLDIGPNAN GKIPPIMQER LLHIGQWLKV
     NGEAIYGTRA WVNSCQWSKG NREWKSKEKH YVSGDAILKQ TVDPDPGYAV KEVFFTKKLV
//
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