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
//