ID A0A2V3PTQ8_9BACT Unreviewed; 466 AA.
AC A0A2V3PTQ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:PXV69117.1};
GN ORFNames=CLV62_101386 {ECO:0000313|EMBL:PXV69117.1};
OS Dysgonomonas alginatilytica.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=1605892 {ECO:0000313|EMBL:PXV69117.1, ECO:0000313|Proteomes:UP000247973};
RN [1] {ECO:0000313|EMBL:PXV69117.1, ECO:0000313|Proteomes:UP000247973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100214 {ECO:0000313|EMBL:PXV69117.1,
RC ECO:0000313|Proteomes:UP000247973};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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 -!- 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:PXV69117.1}.
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DR EMBL; QICL01000001; PXV69117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3PTQ8; -.
DR Proteomes; UP000247973; 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; IPR031919; Fucosidase_C.
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 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 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016020982"
FT DOMAIN 389..463
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT SITE 279
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 466 AA; 53359 MW; ABC3E7B9BF2C30B2 CRC64;
MNLIMKKTRY LILMLIYLLA SFCSAYSQEK RAEIEWFSDA KLGLFIHWGL YSQAAGEWKG
KPTKGGEHFM LYERIPIKEY ELIANDFNPV GFDAAQWVKT AKDAGMKYVI ITAKHHDGFA
MYDSQSSDYT IIKRTAFKRD PIKELADVCK KEGLRFGFYY SLGRDWHDPD VPTNWPQKAG
RSNTWDYPDE DAKNLPAYIE CKVKPQLREL LTNYGTIAMV WFDTPELVTK QQSTEIRELI
LSLQPDCLIN SRIGNGLGDY SIIEQTLMAE IKRTPWEACL TMGRNWSYNK FDTLYKSPEA
TIRNFVDIVS KGGNLLLNVG PTGEGIFPPR STETFNGLHD WLKVNGEAIY GTRPWKVYGE
NLIEGTTEDA SQLSFHDAEF DGTPKVNVPD LRFTSKGNVV YVFARSIIDN KFVINSISKE
DKINKITLLG SKKNVKWKYF ESGLQIDMPL LDTNQIPVYV LKVELK
//
