ID   A0A091CDU6_9ENTE        Unreviewed;       479 AA.
AC   A0A091CDU6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KFN92463.1};
DE            EC=3.2.1.- {ECO:0000313|EMBL:KFN92463.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:KFN92463.1};
GN   ORFNames=TMU3MR103_0458 {ECO:0000313|EMBL:KFN92463.1};
OS   Tetragenococcus muriaticus 3MR10-3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Tetragenococcus.
OX   NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN92463.1, ECO:0000313|Proteomes:UP000029381};
RN   [1] {ECO:0000313|EMBL:KFN92463.1, ECO:0000313|Proteomes:UP000029381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN92463.1,
RC   ECO:0000313|Proteomes:UP000029381};
RA   Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA   Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT   "Genome sequence of Tetragenococcus muriaticus.";
RL   Submitted (AUG-2014) 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:KFN92463.1}.
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DR   EMBL; JPVT01000048; KFN92463.1; -; Genomic_DNA.
DR   RefSeq; WP_028790171.1; NZ_JPVT01000048.1.
DR   AlphaFoldDB; A0A091CDU6; -.
DR   PATRIC; fig|1302648.3.peg.444; -.
DR   Proteomes; UP000029381; 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:SF85; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLA; 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:KFN92463.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029381}.
FT   ACT_SITE        376
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   479 AA;  55174 MW;  26B9277F4BAB9B99 CRC64;
     MSKLPKDFLW GGAVAAHQIE GGWDQDGKGP SVADVMTVGG PNKRREITDT IEKDKFYPNH
     EAIDFYHHYK EDIQLFAEMG LKAFRTSINW TRIFPNGDDA EPNEAGLQFY DNLFDECLKH
     GIEPVVTLTH FEMPLNLAKN YGGFRNRKVV DLFVRFAEVV FKRYKDKVKY WMTFNEINNM
     MDYTNPIFLW TNVGVQVKEG ENPKEVMYTA AHHTLIASAL AVAKGKEINP NFQIGAMVSH
     VPIYPLNSDP NNVMLAEESM HLRYFFPDVQ VRGKYPNYAL KEFKRDGLNI PILEGDADIL
     ANGKVDYLGF SYYMSNVVDI NTGENEDENI HGKIPYQVDN PYLSVSDWGW AIDPVGLRYT
     LNRFWDRYQV PLFIVENGFG AVDTVEEDGS IHDPERIDYL RQHIQEMIKA VDYDGVELMG
     YTPWGVIDLV SFTTGEMKKR YGMIYVDRDN ESNGTMERSK KDSFDWYKHV IETNGEELE
//