ID G0L8Y7_ZOBGA Unreviewed; 538 AA.
AC G0L8Y7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Alpha-L-fucosidase, family GH29 {ECO:0000313|EMBL:CAZ94270.1};
DE EC=3.2.1.51 {ECO:0000313|EMBL:CAZ94270.1};
GN Name=fucA10 {ECO:0000313|EMBL:CAZ94270.1};
GN OrderedLocusNames=zobellia_197 {ECO:0000313|EMBL:CAZ94270.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ94270.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ94270.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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; FP476056; CAZ94270.1; -; Genomic_DNA.
DR RefSeq; WP_013991583.1; NC_015844.1.
DR AlphaFoldDB; G0L8Y7; -.
DR STRING; 63186.ZOBELLIA_197; -.
DR KEGG; zga:ZOBELLIA_197; -.
DR PATRIC; fig|63186.3.peg.199; -.
DR HOGENOM; CLU_002934_6_1_10; -.
DR OrthoDB; 1095333at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
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 SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CAZ94270.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAZ94270.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..538
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003402310"
FT DOMAIN 449..531
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
SQ SEQUENCE 538 AA; 62160 MW; 35CAAEF287ADCD5A CRC64;
MNSKYHLFAL LLVQALIGPK SAFAQEIDFK PTYESLKQYT TPEWFRDAKF GIWSHWGPQS
VPERGDWYAR FMYLQGVLDW GEKFDVNESH TKRYGHPSEF GYKDLIPLFT AEKWNPEKLM
ELYQKAGARY FVSMGQHHDN FDMWNSKLQP WNSVNMGPKR DIVKEWQDAA KKNGMPFGVS
FHGEAAWTFF ESSRLSDHKG PFQGVPYDGW QTKEDGKGKW WEGYDPRDLY GQPHKPKLPA
NVKYAEEVVE EGEPPSDAFL DNFIGRVYDV LDQYHPELIY FDSGHFPAGK ARGTKLIADF
YNMSQKWNKG INQAVVNAKH LTDEEQQMFM LDFENTHSSE VRKLPWQTDI GFDGWFYLEK
EKEDYLPTQD VIHTLADIVS KNGNMLLNIT QSANGEIHPY AYQFLKEMTQ WMAINSEGIH
GTRPWIKFGE GPSRIEGEKD IEHESIDYSS KDFRFTTKGN VLYAILMKYP ESKKEISITS
LSKNEILWFG DIGNVSLLGH KGNLKWKRTA NGLVVSLPEK APCDYAYVIK ISSSKKSG
//
