ID B3C5Q7_9BACE Unreviewed; 481 AA.
AC B3C5Q7;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:EDV07464.1};
GN ORFNames=BACINT_00240 {ECO:0000313|EMBL:EDV07464.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV07464.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV07464.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07464.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDV07464.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07464.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2008) 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:EDV07464.1}.
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DR EMBL; ABJL02000002; EDV07464.1; -; Genomic_DNA.
DR AlphaFoldDB; B3C5Q7; -.
DR STRING; 471870.BACINT_00240; -.
DR eggNOG; COG3669; Bacteria.
DR OrthoDB; 1389336at2; -.
DR Proteomes; UP000004596; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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: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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..481
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002786576"
SQ SEQUENCE 481 AA; 56040 MW; C3E63117AB720E8E CRC64;
MKKILRVILL CSLFATTTFA QQQQQRQPLP AEQEIPLEYG ADHLGKRHDA AMQKFRDNRL
GAFIHWGLYA IPGGEWNGKV YNGAAEWLKS WAKVPADEWM KLMEQWNPEK FNAKTWAKMA
KKMGVKYVKI TTKHHEGFCL WPSKYSRYTV AQTPHKRDVL GEMVKAYNDE GIDVHFYFSV
MDWSNPDYRY DIKSKEDEVA FARFLEFTDN QLKELATRYP TVKDFWFDGT WDASIKKNGW
WTAHAERMLK EMLPGVTVNS RLRADDYGKR HFDSNGHLMG DYESGYERRL PHPVKDLKVT
RWDWEAVMTV PENQWGYHKD WSISYVKTPL EVLERIVHAV SMGGNMVVNF GPQPDGDFRA
EEKNLAEAIG KWMQRYGECI YGCDYAGWEK QSWGYFTRKD KQVYMVVFNP PYSQKLVVKT
PKGTKITKAE LPDGEEIGVI EIARNEYNVS MPRKQPTEPF VIRLQIEDAA SAADKYRDAL
T
//
