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Database: UniProt
Entry: W4D3L7_9BACL
LinkDB: W4D3L7_9BACL
Original site: W4D3L7_9BACL 
ID   W4D3L7_9BACL            Unreviewed;       469 AA.
AC   W4D3L7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Beta glucosidase {ECO:0000313|EMBL:ETT62614.1};
GN   ORFNames=C173_25981 {ECO:0000313|EMBL:ETT62614.1};
OS   Paenibacillus sp. FSL R7-277.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT62614.1, ECO:0000313|Proteomes:UP000019051};
RN   [1] {ECO:0000313|EMBL:ETT62614.1, ECO:0000313|Proteomes:UP000019051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT62614.1,
RC   ECO:0000313|Proteomes:UP000019051};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT62614.1}.
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DR   EMBL; ASPX01000085; ETT62614.1; -; Genomic_DNA.
DR   RefSeq; WP_036730499.1; NZ_ASPX01000085.1.
DR   AlphaFoldDB; W4D3L7; -.
DR   PATRIC; fig|1227352.4.peg.5211; -.
DR   eggNOG; COG2723; Bacteria.
DR   OrthoDB; 108629at2; -.
DR   Proteomes; UP000019051; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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:SF136; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLC; 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        369
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   469 AA;  53985 MW;  06C48A1A10811374 CRC64;
     MLHKQLHAFP ENFLWGGSTS AYQLEGAWDE DGKGPSVIDL ANHVEGVTDF KVASDHYHMY
     KEDVALMAEM GFKAYRFSIA WSRIYPQGDG AVNPKGLEFY SNLIDELLKY GIEPIVTMYH
     FDLPYGLEER GGWSNRATID AFEQYAKTLY ENYGDRVKWW LTINEQNMLI LHPGSIGTLN
     ENMTDPQKEL YQQNHHMLVA QAKAMVLCHQ MLPEAKIGPA PNIGVIYPAS SKPEDMLAAD
     NYAAIRNWLY LDMAVYGRYN HIAWSYLVEK GYEPKIEEED MDILRQGHPD FIAFNYYTSQ
     TVGESKNDGN DFSHTGDQHE IVGEPGAYRG SVNPNLQTTE FGWEIDPVGF RTTLRQIYSR
     YHLPLIVTEN GLGAFDKLEE DGTVNDAYRI EFFRKHIEQI QLALTDGVDV FGFCPWSAID
     LVSTHQGSSK RYGFIYVDRE EFDLKELRRI RKMSFYWYQK LIASRGEIR
//
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