ID A0A0G9H8P0_9GAMM Unreviewed; 455 AA.
AC A0A0G9H8P0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:KLD66130.1};
GN ORFNames=Y882_00130 {ECO:0000313|EMBL:KLD66130.1};
OS Dyella japonica DSM 16301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1440762 {ECO:0000313|EMBL:KLD66130.1, ECO:0000313|Proteomes:UP000035481};
RN [1] {ECO:0000313|EMBL:KLD66130.1, ECO:0000313|Proteomes:UP000035481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16301 {ECO:0000313|EMBL:KLD66130.1,
RC ECO:0000313|Proteomes:UP000035481};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
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:KLD66130.1}.
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DR EMBL; JPLA01000001; KLD66130.1; -; Genomic_DNA.
DR RefSeq; WP_046969839.1; NZ_JPLA01000001.1.
DR AlphaFoldDB; A0A0G9H8P0; -.
DR STRING; 1440762.Y882_00130; -.
DR PATRIC; fig|1440762.4.peg.25; -.
DR Proteomes; UP000035481; 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; 1.
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; PF00754; F5_F8_type_C; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..455
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002575946"
FT DOMAIN 340..439
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|Pfam:PF00754"
SQ SEQUENCE 455 AA; 51057 MW; B87C066326F182DD CRC64;
MKRLVRTFLG AALALSLYSQ AASAQTAADT KPSPQQVHWQ DLEFGVIVHF GTNTFLDREW
GDGTADPKVF NPDHVDAAQW ARASRAAGAR YMVMVAKHHD GFALFPTAQS DYSVKSSPWM
NGKGDLVRLA SDAARAEGLE FGVYLSPWDR HEPRYKQPQE YDVYYRAQVE ELAQHYGPLV
EWWLDGAGSA GHVYDFPRYI ETLRTYQPNA MVFADMGLFE YGDLRWVGQE DGYIRGENWN
VIDRHGYQRW RPVEVDTPLH DLHWFWHPND EATLKSVAKL VDTWENSVGR GGQLMLGIAP
DRHGRLPDAD VARLDAFGKA LRARYGDASN LARHHVGADE NVEAALDGNK DTFWSAPAGA
RHATLEVDFG HPVSFDRTLS MEWLDDGQHV RKYAIEVFDG KAWHAVAGAE AIGHTKIDVF
PRVTAQRVRL NILSSVGDAS IREFQVFDAG PLPSN
//
