ID C9ZBE6_STRSW Unreviewed; 671 AA.
AC C9ZBE6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Putative glycosyl hydrolase {ECO:0000313|EMBL:CBG67291.1};
GN OrderedLocusNames=SCAB_0631 {ECO:0000313|EMBL:CBG67291.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG67291.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG67291.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG67291.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN554889; CBG67291.1; -; Genomic_DNA.
DR AlphaFoldDB; C9ZBE6; -.
DR STRING; 680198.SCAB_0631; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR KEGG; scb:SCAB_0631; -.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_002934_6_0_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.60.20.10; Crystallins; 1.
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; IPR011024; G_crystallin-like.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49695; gamma-Crystallin-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBG67291.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT DOMAIN 535..610
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT DOMAIN 618..668
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
SQ SEQUENCE 671 AA; 73638 MW; CFF393A22913088F CRC64;
MKAAALAGGV AAFGLPQALW PATAEAYTVP SKMDWWYQAR FGMFIHFGSY SYLGQGEWAF
DSQQWSKANY QNQVTQNFNP TQFNAATIAE LAKNAGMKYL VITAKHHEGY AMWNSDVAGF
TDTTGTKLYN LRDFNGIQTD PLMNLKTECE SRGIKFCLYY SILDWNHPSQ TDRHESGLTT
MSSQAARTAY IADMKAQLQE LLDRYDPALL WFDGDWFAEP SSPTLEDWWL ESDGVDLYNW
LIARKPGLIV NERVKRDHGL GDYAVAEFGI PAEPMGRPWE RCATMNGAWG YQAGRENSYR
SVKDVVQELV TVVSRDGNLL LNIGPKGDGS VTAGTQTVLN GLASWMSTYS DSIHGTSGSP
FATEPAWGRV TKKSGKLFAH VFTWPTNGQL RIPVIDNTIS RVYLLNNPSV SLPYTVTDQI
NVTVPATAPN ANASVVCVEV QGMPVRVSAT VFQNVDYQGA RAVLPLGSYT SSQLSAAGLA
PAAASSILVP DGYQVTGYSG DNFTGTAWTF TSNTPDLGVT GNNDVIRSLK VTFRPDKYFR
LNNVTNHWAL DSGGNVASGS NLKQWESIDH ANLQWQAIEL GNGYYRLVNR TNGMVADGWG
ATSNGDPARQ KAWDGSNTQQ WRITHRGQGQ YSIANRSTGL VLDGGGMVAA GAVAKQWTWQ
QHTNLLWTFG A
//
