ID A0A0Q1F218_9SPHI Unreviewed; 439 AA.
AC A0A0Q1F218;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:KQC00313.1};
GN ORFNames=AQF98_12560 {ECO:0000313|EMBL:KQC00313.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC00313.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQC00313.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQC00313.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-2015) 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:KQC00313.1}.
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DR EMBL; LLWP01000005; KQC00313.1; -; Genomic_DNA.
DR RefSeq; WP_055132303.1; NZ_LLWP01000005.1.
DR AlphaFoldDB; A0A0Q1F218; -.
DR STRING; 1740090.AQF98_12560; -.
DR OrthoDB; 107551at2; -.
DR Proteomes; UP000050543; 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 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:UP000050543};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..439
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006190033"
FT SITE 261
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 439 AA; 50211 MW; 9AC380E5FE35B263 CRC64;
MKKFIFMLCL VPFASWAQPK IKPADIEKKM QWFADAKLGI FIHWGIYSVG GVDESWSFYN
KKISYADYMK QLSGFTAKNY DPQAWADLIK ESGAQYSVIT TKHHDGVALW DTKEKHYDVV
NNTPAKRDLI KPFFDALRKN GIKCGAYFSI LDWSHPDYPG FLKDSVRYKI EDDYARWNRY
RSFFQNQLKE LSQNYNPDLW WFDGDWEHSA EEWESQKVRQ ILLKNNPKTI INGRLQGYGD
YETPEQNFPV SKPAFNWWEL CMTTNDNWGY HLNDNNWKTP YEVISIFVDA IANGGNLLLD
IGPKADGTMQ EEQVHILKEL GKWNKKHGEA VFSTVAGLPQ GHFYGPSTLS KDSTTVYLFL
PSKVSGQVAI RGLQNKIEKI TVVGNGAVLN PKIVGKISWS AVPGLVYIPV PANVQDEYVT
VLKVKLDGPL KLYRGHGGL
//
