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Database: UniProt
Entry: F4C3L9_SPHS2
LinkDB: F4C3L9_SPHS2
Original site: F4C3L9_SPHS2 
ID   F4C3L9_SPHS2            Unreviewed;       604 AA.
AC   F4C3L9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Glycoside hydrolase family 29 (Alpha-L-fucosidase) {ECO:0000313|EMBL:ADZ79407.1};
GN   OrderedLocusNames=Sph21_2860 {ECO:0000313|EMBL:ADZ79407.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ79407.1};
RN   [1] {ECO:0000313|EMBL:ADZ79407.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ79407.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) 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; CP002584; ADZ79407.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4C3L9; -.
DR   STRING; 743722.Sph21_2860; -.
DR   KEGG; shg:Sph21_2860; -.
DR   PATRIC; fig|743722.3.peg.3054; -.
DR   eggNOG; COG3669; Bacteria.
DR   HOGENOM; CLU_002934_0_1_10; -.
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   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, ECO:0000313|EMBL:ADZ79407.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..604
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003306017"
SQ   SEQUENCE   604 AA;  68964 MW;  E5D688A65F6B184F CRC64;
     MKNWTTLYSR KYQRCIVICV FLFGMTAHAQ TMDEMWESRS SGKEHANIQW FKDAKFGLFI
     HWGLYSHLGG EWKGKRYYGS GEWIMNQAKI PVREYEATAA TFNPSRFNAD EWAQLAKDAG
     IKYVVITAKH HEGFAMYDSK VSTFDIVDAT PFKQDPMKLL ADAVRKRGMH FGFYYSQFQD
     WHNPNGGKNT WDFDESKKDY QKYYRQKAIP QLKELMSNYG DLSIVWFDTP GGLSKEQTQQ
     FIDSLRLLQP KSLFSSRVGH GLGDYRDYGD SEMPAMPING AWESIYTHND SWGYMKHDMN
     FKTPETIIRL LAEAASKGGN LMLNVGPDGS GRIPAYSAQF LRETGRWLQV NGESIYGTTQ
     GLIPQQPWGV TTSKPGKQYL HVWTRPRSGK LLIPNANMQV QKVYALADGQ PVKWHKRGDA
     IWIDLPITLS DAKNTVFVLE YAGEAPTYNK NAPITISNQF DENEIKAAFA KTTGNARIES
     LTYSHYYGDW KHTNCVVGMA DREKDIIEFD TQLMESGNYR ITLEYACEPE SANQEGTLSI
     NGQNFYFRTL HTGSFDKKAP LLFVRHDVAT ISINKPGRYT LDIRPLSGKS ELFKLKAVII
     KPID
//
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