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Database: UniProt
Entry: A0A2T0BIM3_9CLOT
LinkDB: A0A2T0BIM3_9CLOT
Original site: A0A2T0BIM3_9CLOT 
ID   A0A2T0BIM3_9CLOT        Unreviewed;       471 AA.
AC   A0A2T0BIM3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Aryl-phospho-beta-D-glucosidase BglA {ECO:0000313|EMBL:PRR83730.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:PRR83730.1};
GN   Name=bglA_1 {ECO:0000313|EMBL:PRR83730.1};
GN   ORFNames=CLVI_06770 {ECO:0000313|EMBL:PRR83730.1};
OS   Clostridium vincentii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR83730.1, ECO:0000313|Proteomes:UP000239471};
RN   [1] {ECO:0000313|EMBL:PRR83730.1, ECO:0000313|Proteomes:UP000239471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR83730.1,
RC   ECO:0000313|Proteomes:UP000239471};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium vincentii DSM 10228.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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:PRR83730.1}.
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DR   EMBL; PVXQ01000005; PRR83730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0BIM3; -.
DR   OrthoDB; 2339329at2; -.
DR   Proteomes; UP000239471; Unassembled WGS sequence.
DR   GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF348; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:PRR83730.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239471}.
FT   ACT_SITE        369
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   471 AA;  54129 MW;  62C84E273BE858FB CRC64;
     MNKLPDDFLW GGAVAANQFE GGWNKGGKGI SVSDVMTAGT HGVERVITDG IIEGMNYPNH
     KAIDFYSRYK KDIALFHEMG FKCFRTSIAW TRIFPNGDES EPNEEGLLFY DSVFDECLEY
     GIEPVVTISH FEMPYNLVVK YGGWRNPMLI DFFLNFCEVV YKRYKNKIKY WMPFNEINMI
     IRKPWKPGGI KFSEGENELL TKYQAAHYML VACAKAVILG KSINPDFIIG TMLLHTTTYA
     ATCNPDDVMA HIKKLHEAYF FTDVQVRGEY PSFQLKFMEK NNLDIKISEE DKKILREGTV
     DFIGFSYYSS SIEIANPTTE DASEGNEIKG YKNPLLPASE WGWQIDPVGL RITLNWLYDR
     YNIPLFIVEN GFGAVDKFEE DGSINDEYRI DYFKKHVEQM KKAVLEDGVE LLGYTTWGCI
     DLVSAGTGEM KKRYGFIHVD KDNDGKGTLN RTRKNSFYWY KKCIESNGEE L
//
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