ID   Q93PB2_9BACT            Unreviewed;       540 AA.
AC   Q93PB2;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   02-SEP-2026, entry version 80.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
OS   Microscilla sp. PRE1.
OG   Plasmid pSD15 {ECO:0000313|EMBL:AAK62841.1}.
OC   Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC   Microscillaceae; Microscilla.
OX   NCBI_TaxID=155537 {ECO:0000313|EMBL:AAK62841.1};
RN   [1] {ECO:0000313|EMBL:AAK62841.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PRE1 {ECO:0000313|EMBL:AAK62841.1};
RC   PLASMID=pSD15 {ECO:0000313|EMBL:AAK62841.1};
RX   PubMed=11722934; DOI=10.1128/AEM.67.12.5771-5779.2001;
RA   Zhong Z., Toukdarian A., Helinski D., Knauf V., Sykes S., Wilkinson J.E.,
RA   O'Bryne C., Shea T., DeLoughery C., Caspi R.;
RT   "Sequence analysis of a 101-kilobase plasmid required for agar degradation
RT   by a Microscilla isolate.";
RL   Appl. Environ. Microbiol. 67:5771-5779(2001).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951}.
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DR   EMBL; AF339846; AAK62841.1; -; Genomic_DNA.
DR   RefSeq; WP_010925633.1; NC_002806.1.
DR   AlphaFoldDB; Q93PB2; -.
DR   BRENDA; 3.2.1.51; 9552.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR   GO; GO:0016139; P:glycoside catabolic process; IEA:TreeGrafter.
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; IPR031919; Fucosidase_C.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR057739; Glyco_hydro_29_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF37; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   Pfam; PF16757; Fucosidase_C; 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   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Plasmid {ECO:0000313|EMBL:AAK62841.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          47..419
FT                   /note="Glycoside hydrolase family 29 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01120"
FT   DOMAIN          453..537
FT                   /note="Alpha-L-fucosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16757"
SQ   SEQUENCE   540 AA;  62522 MW;  2C7943E3E91BFC37 CRC64;
     MMKHKKQMIK SNKFLYLILF VGVFFGGLSL ETTAQKKGEH NLSETTKEVA EQKRKYKEEW
     ASIAKHSTPE WFRDAKFGIY THYGPAVNAT QYQQTEWWGW AMYNIKEKYW TNEVRPDSPD
     TAKAFKLQLE KWGDPNEFGY KDFIMEFKPT AFDAEEWADL FHKAGAKFAG PMGTHHDNFM
     LWDSEVTRWN SVRTAGVDVV GDLEEAIRAK GMKYLITFHH AFSWWFFSES YKYDGGIPGN
     EDLYGRPHTF SSDGDSFAEY PDEEYEELWF RKLEEAAIKY SPDLYWFDMG LELLSENIRK
     KAFARLLNLA ERNNQEIGIS YKIKFQQCIP TSAGILDYEK GRSKGYREDP WLTDTPLAGW
     FYNGRKSRSA EAMIEILVDI VSKNGCLLLN VSPKPDGTIP EDQKKTLLGM GEWLEMNGEA
     IYNTRPWVIS GEGPTELAKD DHFNENWEAI YTEQDIRFTR SKDDNTLYLI VLDRPTQGSV
     TATLLADIYP YLDRNIQSVK LIGTESSEIS WSRNSKGLHL SFPNTAKGKH AWCYKLQLSE
//