ID A2RJA3_LACLM Unreviewed; 477 AA.
AC A2RJA3;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:CAL97355.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:CAL97355.1};
GN Name=ascB {ECO:0000313|EMBL:CAL97355.1};
GN OrderedLocusNames=llmg_0751 {ECO:0000313|EMBL:CAL97355.1};
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870 {ECO:0000313|EMBL:CAL97355.1, ECO:0000313|Proteomes:UP000000364};
RN [1] {ECO:0000313|EMBL:CAL97355.1, ECO:0000313|Proteomes:UP000000364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363 {ECO:0000313|EMBL:CAL97355.1,
RC ECO:0000313|Proteomes:UP000000364};
RX PubMed=17307855; DOI=10.1128/JB.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; AM406671; CAL97355.1; -; Genomic_DNA.
DR RefSeq; WP_011834737.1; NZ_WJVF01000008.1.
DR AlphaFoldDB; A2RJA3; -.
DR SMR; A2RJA3; -.
DR STRING; 416870.llmg_0751; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; llm:llmg_0751; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR OrthoDB; 1637462at2; -.
DR PhylomeDB; A2RJA3; -.
DR Proteomes; UP000000364; 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: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:CAL97355.1}.
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 477 AA; 54728 MW; 2D991C1B882E00DA CRC64;
MPFSKDFLWG GATAANQCEG GYNQGGRGLA NVDLVPHGKD RFPIITGEMK HLEFDEEHFY
PAKEAIDMYH HWKDDLALFA EMGFKTYRMS IAWTRIFPKG DEQEPNEEGL QFYEDIFKEC
KRLGIEPLVT ITHFDCPVHL IKEYGGWRNR KMVGFYEKLA RTIFTRFKGL VRYWLTFNEI
NMLLHAPFMG AGLVFEEGEN KEQAKYLAAH HELLASALAT KIAHEIDPEN KIGCMLAAGE
YYPFDCNPEN VLEAQKQNHD NLFFIDVQSR GKYPNYLLKR LEREDVQLPI ETGDLEILAE
NTVDFISFSY YSSRVAKIKD KDADKSAGNI FESVTNPYLK ASEWGWQIDP LGLRITMNSI
YDRYQKPLFV VENGLGALDK PDENGFVADD YRIDYMAAHI KEMKKAVELD GVELLGYTSW
GCIDLVSAGT GEMSKRYGFI YVDRDDFGKG TLKRTSKKSF DWYKKVIASN GEDLTNE
//
