ID F2R486_STRVP Unreviewed; 436 AA.
AC F2R486;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:CCA53363.1};
DE EC=3.2.1.51 {ECO:0000313|EMBL:CCA53363.1};
GN OrderedLocusNames=SVEN_0075 {ECO:0000313|EMBL:CCA53363.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53363.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA53363.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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; FR845719; CCA53363.1; -; Genomic_DNA.
DR RefSeq; WP_015031283.1; NZ_JABVZO010000044.1.
DR AlphaFoldDB; F2R486; -.
DR STRING; 953739.SVEN_0075; -.
DR GeneID; 69862304; -.
DR KEGG; sve:SVEN_0075; -.
DR PATRIC; fig|953739.5.peg.3511; -.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_002934_0_2_11; -.
DR OrthoDB; 5526311at2; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
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 Glycosidase {ECO:0000313|EMBL:CCA53363.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCA53363.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT SITE 265
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 436 AA; 49615 MW; 4A750F0FC2142CF4 CRC64;
MTTTSADAAD ASAPAPAPDT TWFTHDRFGM FVHWGLYSLA ARHEWVKNRE RMTDEQYQVY
FDHFDPDRYD PVSWVRTAKA AGMRYVVLTT KHHDGFCLWD SRLTDYKVTR TPHGRDLVRP
FVEACRAEGL KVGFYHSLID WHHPSFPVDG THPQRDDEEF KAAAADRDIR AYQRYLHGQV
RELLTDYGRV DYLFFDFSYA GREWWGGKGP DDWDAPRLLE TVRELQPHIL VNDRAGLPGD
FVTPEQYQPS APMTVDGRPV LWEACQTLNG SWGYDRDNLD HKSPDLLIRM LVDGVSKGGN
LLLNVGPDGR GGLDPRDTAT LAEIGRWTDL HERSVRGCGP SPYTPPADCR YTQRGDRLYV
HLFAWPLRHL HLPGLEGRVA YAQLLNDGSE IARVPLDPDR PAMNTQMGGQ PPGTLTLRLP
VRCPDTPVPV IELFLR
//
