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Database: UniProt
Entry: A0A0A2UDR4_9BACL
LinkDB: A0A0A2UDR4_9BACL
Original site: A0A0A2UDR4_9BACL 
ID   A0A0A2UDR4_9BACL        Unreviewed;       781 AA.
AC   A0A0A2UDR4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=P364_0123425 {ECO:0000313|EMBL:KGP79760.1};
OS   Paenibacillus sp. MAEPY2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP79760.1, ECO:0000313|Proteomes:UP000030061};
RN   [1] {ECO:0000313|EMBL:KGP79760.1, ECO:0000313|Proteomes:UP000030061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP79760.1,
RC   ECO:0000313|Proteomes:UP000030061};
RX   PubMed=24526641;
RA   Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT   "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT   MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL   Genome Announc. 2:0-0(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
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:KGP79760.1}.
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DR   EMBL; AWUK01000032; KGP79760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2UDR4; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000030061; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KGP79760.1}.
FT   DOMAIN          699..768
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   781 AA;  84819 MW;  9CF431F4B57A457D CRC64;
     MIYKDKSKSV EERVEHLLSL MTTEEKAGQL IQPFGWQTYT NDEGNITLNE SFKQQVENGG
     VGSLYGALRA DPWTGVTLEN GLSAREGAEA VNLIQRHAIE HSRLGIPILI GEECSHGHMA
     IDGTVYPVPL LLGSTWNVDL YRDMCRAVAR ETRAQGGAVT YSPVLDVVRD PRWGRTEECF
     GEDPYLIGEL AVASVQGLQG ESLDQEDAVA ATLKHFVGYG SSEGGRNAGP VHMGWRELLE
     VDLYPFRKAV EAGAQSIMPA YNEIDGIPCT VNTELLEDVL RKGWGFDGLV ITDCGAINML
     ASGHDVAADG LEASIQAIQA GIDMEMSGEM FGQYLVQAIS EGKLEMHVLD QAVRRVLALK
     FKLGLFEKPY VDADRAAEVI GSAEHIQLAR QLAAEGVVLL KNEAAALPLS AATAGRIAVI
     GPNADQAYNQ LGDYTSPQPK SKVATVLDGI RSKFAVSKSG HAEEGSDGNS NGEVEVLYAP
     GCRIKGDSRE GFEHAIETAR QADTVIIVVG GSSARDFGEG TIDLKTGASN VSDNSWNDME
     CGEGIDRMTL GLAGVQLELI QEIHKLDKTL VIIYINGRPI TEPWVDEHAD AILEAWYPGQ
     EGGHAIADIL FGNVNPSGRL TISIPKHVGQ LPIYYNGKRS RGKRYLEEDL EPRYPFGYGL
     SYTTFDYSEL KLSTESMTAD ETVTVTVNVT NTGACRGAEV IQMYVSDVVS RVARPAKELK
     GFAKVNLEPG EMRTVIFHIG AEQLQYIGRD LTPVVEPGQF HIHIGRHVND TQFTELTVEG
     A
//
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