ID A0A0Q1H7X2_9FLAO Unreviewed; 432 AA.
AC A0A0Q1H7X2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:KQC29799.1};
GN ORFNames=AAY42_07795 {ECO:0000313|EMBL:KQC29799.1};
OS Allomuricauda eckloniae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=346185 {ECO:0000313|EMBL:KQC29799.1, ECO:0000313|Proteomes:UP000050827};
RN [1] {ECO:0000313|EMBL:KQC29799.1, ECO:0000313|Proteomes:UP000050827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK169 {ECO:0000313|EMBL:KQC29799.1,
RC ECO:0000313|Proteomes:UP000050827};
RA Kwon Y.M., Kim S.-J.;
RT "Complete genome of flavobacterium.";
RL Submitted (APR-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:KQC29799.1}.
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DR EMBL; LCTZ01000002; KQC29799.1; -; Genomic_DNA.
DR RefSeq; WP_055393943.1; NZ_LCTZ01000002.1.
DR AlphaFoldDB; A0A0Q1H7X2; -.
DR STRING; 346185.AAY42_07795; -.
DR PATRIC; fig|1547436.3.peg.1603; -.
DR Proteomes; UP000050827; 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:UP000050827};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..432
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006190484"
FT SITE 276
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 432 AA; 49954 MW; B97DE461B5CD4C14 CRC64;
MKKVILILMC FWATLTVNAQ KFYDYPMPEY TPTQGNLEAR ATFQDMKFGM FIHWGVYSVL
GDGEWVMHQQ KIPLETYKKL PKFFDPEDFN AEEWVKIAKS AGMKYITITS RHHDSFSMFD
TNATDYDIID ATRFDRDPLK ELAEACKKEG IQLNFYYSLL DWAREDYKNG RKGDEEAWKD
YIKFMKTQLT ELLTNYGEIG CIWFDGHWDR KQANWHYDEI YALIHELSPN TLIANNHHIQ
PIPGEDIQTF ERDLPGENQG GYSAGVQVSQ LPLESCATMG KAWGFNLNDK KYKTTKQLIH
FLVNAAGKNG NLLLNVGPMP NGEIQPEFVD TLGEIGEWTS TYGESIYGTR GNVIKSQEWG
TMTRKGKTLY MHILNPSSKP YFFIPELNEK IVSVKTFDGK RVKFKQIKEG VFIYMDSKKI
DGIDEVLKLN IK
//
