ID A0A2N8LAW9_9STRE Unreviewed; 485 AA.
AC A0A2N8LAW9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:PND47309.1};
GN ORFNames=AT575_07235 {ECO:0000313|EMBL:PND47309.1};
OS Streptococcus penaeicida.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1765960 {ECO:0000313|EMBL:PND47309.1, ECO:0000313|Proteomes:UP000235963};
RN [1] {ECO:0000313|EMBL:PND47309.1, ECO:0000313|Proteomes:UP000235963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 1838 {ECO:0000313|EMBL:PND47309.1,
RC ECO:0000313|Proteomes:UP000235963};
RA Gomez-Gil B., Morales-Covarrubias M.;
RT "Streptococcus penaeicida sp. nov.";
RL Submitted (DEC-2015) 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:PND47309.1}.
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DR EMBL; LOCM01000028; PND47309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N8LAW9; -.
DR OrthoDB; 1637462at2; -.
DR Proteomes; UP000235963; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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:SF122; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLH; 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}.
FT ACT_SITE 383
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 485 AA; 54699 MW; 9465C6A06F39A98B CRC64;
MSILRDDFLW GGAIAANQVE GAWNLDGKGL SVADVAVFKP NLDVTDYAGH NTVTTAMIEE
AMATEDAKDY PKRRGIDFYH HYEEDIALFA EMGFKTLRLS IAWSRLFPTG EEEVANPQGL
AFYKKVFEEL KKHQIEPIVT LSHYEMPLAL SLKYNGWVDR AVIAHFTRFA ESCFEAFGDY
VTYWLTFNEI DSVGRHPFTT AGIIPDQCQA YSLEQAVYQA LHHQYLAAAI ATQKCHQMIP
GSQVGSMLTK LTTYPHTCHP EDVALALAQN LDNYSHSDIQ IFGKYPPLHL KRLQAMGVAP
QMEAGDEELL ANGRADYLAF SYYMSRTESA DPELEKTAGN TIMSVKNPYL ASTDWGWQID
PVGLRISLLE LYDRYQVPLI IVENGMGAKD TIEDDGSIHD PYRIAYLKAH IEEMKKAVEM
GVDLFGYTSW APIDLISVST SQMSKRYGYI YVDQDDLGNG SLKRSPKDSF YWYQKVIQSN
GDKLD
//
