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Database: UniProt
Entry: Q5FMF4_LACAC
LinkDB: Q5FMF4_LACAC
Original site: Q5FMF4_LACAC 
ID   Q5FMF4_LACAC            Unreviewed;       475 AA.
AC   Q5FMF4;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=6-p-beta-glucosidase {ECO:0000313|EMBL:AAV42120.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:AAV42120.1};
GN   OrderedLocusNames=LBA0225 {ECO:0000313|EMBL:AAV42120.1};
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381};
RN   [1] {ECO:0000313|EMBL:AAV42120.1, ECO:0000313|Proteomes:UP000006381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC   {ECO:0000313|Proteomes:UP000006381};
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP000033; AAV42120.1; -; Genomic_DNA.
DR   RefSeq; WP_011254081.1; NC_006814.3.
DR   RefSeq; YP_193151.1; NC_006814.3.
DR   AlphaFoldDB; Q5FMF4; -.
DR   SMR; Q5FMF4; -.
DR   STRING; 272621.LBA0225; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GeneID; 56941830; -.
DR   KEGG; lac:LBA0225; -.
DR   PATRIC; fig|272621.13.peg.215; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_2_9; -.
DR   OrthoDB; 1688691at2; -.
DR   BioCyc; LACI272621:G1G49-219-MONOMER; -.
DR   Proteomes; UP000006381; 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: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:AAV42120.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006381}.
FT   ACT_SITE        373
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   475 AA;  55519 MW;  2D7EA520CA14761D CRC64;
     MTESIFPKKF LWGGAVAAHQ LEGGYNEDGK GISIADLMTL GSHEYPRELT ATIEEGKYYP
     NHKAIDFYHH YQEDIKLMAE MGFKAFRTSI AWTRIFPNGD ETQPNEEGLA FYDKVFDECL
     KYNIEPVVTL SHFEMPYHLV TKYGGWSNRK LIDFFTRLAH VCFEKYHTKV KYWMTFNEIN
     NQANYESDIS VYENSGIKFN EDDDKQKIMY QAAHYEMVAS AEAVQIGHAI DPSLRIGCML
     AFCPIYPASP KPEDILFAQR AMDSRLYFGD VQVNGEYPSW LKQYFKNNNY NLDITDNDLQ
     ILKQGTVDYI GFSYYMSFTT KYTDHLDYRE YQDLVENPFI KANDWGWPID PVGLRYALNW
     MSTRWHKPLF IVENGLGAYD KLTEDHEVHD QYRINYLHDH ILEIKKAITE DGIDVIGYLP
     WGCIDLVSAS TGEMKKRYGF IYVDEDDHGN GSMKRYKKDS FYWYQNVIKT NGQEL
//
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