ID   A0A9X4NHR3_9LACT        Unreviewed;       477 AA.
AC   A0A9X4NHR3;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   24-JAN-2024, entry version 2.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:MDG4983253.1};
GN   ORFNames=OGZ51_03705 {ECO:0000313|EMBL:MDG4983253.1};
OS   Lactococcus lactis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1358 {ECO:0000313|EMBL:MDG4983253.1, ECO:0000313|Proteomes:UP001152614};
RN   [1] {ECO:0000313|EMBL:MDG4983253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3 {ECO:0000313|EMBL:MDG4983253.1};
RA   Turner M.S., Huang W.;
RL   Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MDG4983253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3 {ECO:0000313|EMBL:MDG4983253.1};
RX   PubMed=36906309;
RA   Huang W., Dong A., Pham H.T., Zhou C., Huo Z., Watjen A.P., Prakash S.,
RA   Bang-Berthelsen C.H., Turner M.S.;
RT   "Evaluation of the fermentation potential of lactic acid bacteria isolated
RT   from herbs, fruits and vegetables as starter cultures in nut-based milk
RT   alternatives.";
RL   Food Microbiol. 112:0-0(2023).
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:MDG4983253.1}.
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DR   EMBL; JAOWLY010000002; MDG4983253.1; -; Genomic_DNA.
DR   Proteomes; UP001152614; Unassembled WGS sequence.
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:SF296; 6-PHOSPHO-BETA-GLUCOSIDASE; 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        372
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   477 AA;  54753 MW;  7B8F428D52FB70BB CRC64;
     MPFSKDFLWG GATAANQCEG GYNQGGRGLA NVDLVPHGKD RFPIITGEMK HLEFDEDHFY
     PAKEAIDMYH HWKEDLALFA EMGFKTYRMS IAWTRIFPKG DEQEPNEEGL QFYEDIFREC
     QRLGIEPLVT ITHFDCPVHL IKEYGGWRNR KMVAFYENLA RAIFTRYKGL VHYWLTFNEI
     NMLLHAPFMG AGLVFEEGEN KEQAKYLAAH HELLASALAT KIGHEVDPEN KIGCMLAAGD
     YYPFDCNPEN VFEAQKQNHD NLFFIDVQSR GKYPNYLLKR LEREEITLPI EKGDLEILAE
     NTVDFISFSY YASRVAKVKD EDADKSAGNI FESVKNPYLE ASEWGWQIDP LGLRITMNSI
     YDRYQKPLFI VENGLGAVDK PDENGFVADD YRIDYMAAHI KEMKKAVELD GVELLGYTSW
     GCIDLVSAGT GEMSKRYGFI YVDRDDYGKG SLKRTPKKSF NWYKKVIASN GEDLTNE
//