ID   A0A1T5NIG6_9BACT        Unreviewed;       686 AA.
AC   A0A1T5NIG6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:SKD00241.1};
GN   ORFNames=SAMN05660461_1752 {ECO:0000313|EMBL:SKD00241.1};
OS   Chitinophaga ginsengisegetis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD00241.1, ECO:0000313|Proteomes:UP000190166};
RN   [1] {ECO:0000313|EMBL:SKD00241.1, ECO:0000313|Proteomes:UP000190166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD00241.1,
RC   ECO:0000313|Proteomes:UP000190166};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUZZ01000001; SKD00241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5NIG6; -.
DR   STRING; 393003.SAMN05660461_1752; -.
DR   Proteomes; UP000190166; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF37; ALPHA-L-FUCOSIDASE; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   Pfam; PF13290; CHB_HEX_C_1; 1.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS50022; FA58C_3; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190166};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..686
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012459581"
FT   DOMAIN          330..468
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          527..683
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
SQ   SEQUENCE   686 AA;  75433 MW;  BBD77C5AB48EF1FA CRC64;
     MKKNTLLLAG LLGFNMAMAQ EIKPYGALPS KAQVSWNDME YYMFIHFGPN TFTNKEWGHG
     DEDPKVFNPT HLDARQWART AKAAGMKGIV ITAKHHDGFC LWPSKYSTHT VRESAWKDGK
     GDVLAELSAA CKEYGLKFGV YLSPWDRNHP EYGKPGYNRV FANTLNEVLS SYGPVFEQWF
     DGANGGNIKQ PYDWNLFHSV VYKNQPNAVI FSDVGPGCRW VGNENGIAGT TNWSTLNVKG
     FAPGANGPAT KSLNEGNEDG EQWIPAECDV SIRPGWFYSP ETNDKVKSVS SLLDIYYGSV
     GRNGNLILNV PVDRDGLIHP NDSTRLMELR RVLDASFKNN LAKRAVVTAT NTRSNNKAVK
     VSNLNDGTNT TYWATTDDAT TTTITLTYKQ PVTFNRLVLQ EYIALGQRVK AFNVEVLEQG
     AWKQIASETT IGHKRILRLK DYTTTQVRIN ILDAKAAPVI SEVQLYKAPG LLTLPQIGRT
     ADGKVWIHSE SGDPDIHYTL DGSEPTVKSP KYISAETTVI NLPRGGVVRA KAFLDNGKTA
     SETVTTTFDI AAAKWKVISP EAAAKDNDPA KAIDGSNTTV YVAGNKGYPH ELQVDLGETL
     SLKGFTYTPP VGEGIIYGYE FYTSTDGKNW GSPVASGQFA NIKNNPVQQT VAFKKTSARY
     IRFVATSPAD EKQPQAAIAE LGVITR
//