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Database: UniProt
Entry: L0FZG1_ECHVK
LinkDB: L0FZG1_ECHVK
Original site: L0FZG1_ECHVK 
ID   L0FZG1_ECHVK            Unreviewed;       484 AA.
AC   L0FZG1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:AGA78433.1};
GN   OrderedLocusNames=Echvi_2182 {ECO:0000313|EMBL:AGA78433.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA78433.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) 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; CP003346; AGA78433.1; -; Genomic_DNA.
DR   RefSeq; WP_015265991.1; NC_019904.1.
DR   AlphaFoldDB; L0FZG1; -.
DR   STRING; 926556.Echvi_2182; -.
DR   KEGG; evi:Echvi_2182; -.
DR   PATRIC; fig|926556.3.peg.2303; -.
DR   eggNOG; COG3669; Bacteria.
DR   HOGENOM; CLU_002934_0_1_10; -.
DR   Proteomes; UP000010796; Chromosome.
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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010796};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..484
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003942947"
SQ   SEQUENCE   484 AA;  55730 MW;  7182CA461E534298 CRC64;
     MMRKILSGIL VVSALFLGRI ASSTAQDIPN NTPRTSLALA HGAHRLGKRT DPMMERWRNY
     GLGQFIHWGV YAIPGGQWNG ASYGGAAEWI RSWKGMPKEA YDNLYKEFDP ENYDPSALAK
     QAKEMGAKYM IITTKHHDGF CLWPSEYTDY DVTNTPYGKD IIGPLVEAYD AEGIDVYLYF
     SVMDWNHPGY RSVLATEEDR SAYESFKEFT RNQLLELLER YPTTKGLWFD GTWDEAWKEQ
     AEFADNLATE MRKKIPGLII GSRFRPDDYG NRHFDSNGDL MGDYEQGWER KLPETYEDTN
     GNDWDCVMTI PENQWGYHSD WRGHVKTSYE LIEMLVKSVS LDGNFVLNFG PDAKGDIRME
     EKKLATEIGQ WMSKNKSAIY NCGHIDWEKQ DWGYYTQNRV TGEVNMVVFN KPINSVLRIK
     TSSKISLQKI YDLNDATKIY DPEEISQDEY IIQLGDEELA EPKVIVIKYD HSKGETKGYE
     KAKT
//
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