ID A9QSQ8_LACLK Unreviewed; 483 AA.
AC A9QSQ8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ABX75744.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:ABX75744.1};
GN Name=pbg {ECO:0000313|EMBL:ABX75744.1};
GN OrderedLocusNames=LLKF_0673 {ECO:0000313|EMBL:ABX75744.1};
OS Lactococcus lactis subsp. lactis (strain KF147).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=684738 {ECO:0000313|EMBL:ABX75744.1, ECO:0000313|Proteomes:UP000001886};
RN [1] {ECO:0000313|EMBL:ABX75744.1, ECO:0000313|Proteomes:UP000001886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF147 {ECO:0000313|EMBL:ABX75744.1,
RC ECO:0000313|Proteomes:UP000001886};
RX PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA van Hylckama Vlieg J.E.;
RT "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT isolates from plants identifies mechanisms of adaptation to the plant
RT niche.";
RL Appl. Environ. Microbiol. 74:424-436(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CP001834; ABX75744.1; -; Genomic_DNA.
DR RefSeq; WP_012897375.1; NC_013656.1.
DR AlphaFoldDB; A9QSQ8; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; llk:LLKF_0673; -.
DR HOGENOM; CLU_001859_0_1_9; -.
DR OMA; ICTINEP; -.
DR Proteomes; UP000001886; Chromosome.
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:SF122; 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:ABX75744.1}.
FT ACT_SITE 380
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 483 AA; 55659 MW; E5D13E27F6F6D83B CRC64;
MTFKPDFLWG GATAANQFEG AFLEDGRGWS TADTAKYYPH SDKTSMDSLM DPMTTSKIEF
AKKDLEGIYP KRYGIDFYHH FKEDIALFAE MGFKTFRMSI SWSRIFPNGD ELEPNETGLK
FYDQVFDELL KYHIEPLVTM SHYEFPLGLA LKQNGWESRE TVDHFEKYAR VILNRYKDKV
KYWLTFNEIN IIGITGYLSG GLLADKTQNM LQSQFQAAHH QFLASALAVK ACHEIIPEAK
IGCMLARMET YPETCNPLDV MATIDSDHAN LFYSDVQVRG YYPTYMKKVF KDHHLKIIKE
SGDDQLLKEG KVDFMSFSYY MSSISSSSEE GEVIGGNFTQ TKKNPYLKSS DWGWQIDPVG
LRITLHKLYD RYQVPLFVVE NGLGAHDTLE EDGTIHDNYR IDYLREHIKQ MGIAIDEGVD
LMGYTPWGCI DLVSASTSEM SKRYGFIYVD QDNEGEGSLK RFKKDSFYWY KSVIQSNGET
LYK
//