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
//