ID A0A0U2WTX7_9BACL Unreviewed; 704 AA.
AC A0A0U2WTX7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=IJ21_33090 {ECO:0000313|EMBL:ALS28698.1};
OS Paenibacillus sp. 32O-W.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS28698.1, ECO:0000313|Proteomes:UP000059673};
RN [1] {ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS28698.1, ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|EMBL:ALS28698.1,
RC ECO:0000313|Proteomes:UP000059673};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
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};
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DR EMBL; CP013653; ALS28698.1; -; Genomic_DNA.
DR RefSeq; WP_062493760.1; NZ_CP013653.1.
DR AlphaFoldDB; A0A0U2WTX7; -.
DR STRING; 1695218.IJ21_33090; -.
DR KEGG; pow:IJ21_33090; -.
DR PATRIC; fig|1695218.3.peg.3551; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000059673; Chromosome.
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:SF121; PERIPLASMIC 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:ALS28698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059673}.
FT DOMAIN 617..686
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 704 AA; 77169 MW; 7004C72005C15E61 CRC64;
MSVEQQIDKL LSRMTLQEKI GQMIQTGTFE EADKEKIRMG RIGSVLGVTG ADLVNELQRI
AVEESRLGIP LLIAGDVIHG YRTTFPIPLA EACSWNMALI EETAAVAARE ASAAGIHWIL
APMVDIARDP RWGRVAEGAG EDVWLAAAIA RARVAGIQRN DWEDRPHMVA CPKHFAGYGL
AEAGRDYNTV DVSERRLRET YFPPFQAALE AGAGTMMCAF NELNGVPCTG NRWLLTDVLQ
QEWGFQGFVV SDWESIGELV QHGFAESREE AARIAIEAGV HMDMQARVYD EYLEQLVNRG
IVPESVIDEA VRRILRIKFR AGLFDQPYTP PEHAASLLLH PDHVRTARAM ARESIVLLKN
EHNVLPLTSR VRKLAVVGPL ADDRAAVLGC WAGQGRSEDA VSILQGIVAT AEPDVEIMFC
RGWREETAEP DIAQAVDIVR QCETAVVVLG ETADMSGENN SRTSIELPSG QLELLKAIHA
TGVPVVLVLV NGRPLALEWA DRHIPAIVEA WHLGTQAGMA VADILFGKHN PSGKLPITFP
RSTGQIPIYY SAKKTGRPGL KRYADSEVEP LYPFGYGLSY TRFEYDRFGI SSTEIKAGDT
ITVSARITNA GTMEGAETVQ LYICDEAASI TRPVKELKGF AKISLKPGES HLVEFRLSAE
QLGFFNADGR YVVEPGRFTV WIGPDSRGGL CGTFSVIPCI SDEA
//