ID BGLB_PAEPO Reviewed; 448 AA. AC P22505; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=Beta-glucosidase B; DE EC=3.2.1.21; DE AltName: Full=Amygdalase; DE AltName: Full=Beta-D-glucoside glucohydrolase; DE AltName: Full=Cellobiase; DE AltName: Full=Gentiobiase; GN Name=bglB; OS Paenibacillus polymyxa (Bacillus polymyxa). OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=1406; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2123813; DOI=10.1016/0378-1119(90)90410-s; RA Gonzalez-Candelas L., Ramon D., Polaina J.; RT "Sequences and homology analysis of two genes encoding beta-glucosidases RT from Bacillus polymyxa."; RL Gene 95:31-38(1990). 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M60211; AAA22264.1; -; Genomic_DNA. DR PIR; JW0038; JW0038. DR PDB; 2JIE; X-ray; 2.30 A; A=2-448. DR PDB; 2O9P; X-ray; 2.10 A; A=2-448. DR PDB; 2O9R; X-ray; 2.30 A; A=4-448. DR PDB; 2O9T; X-ray; 2.15 A; A=2-448. DR PDB; 2Z1S; X-ray; 2.46 A; A=2-448. DR PDBsum; 2JIE; -. DR PDBsum; 2O9P; -. DR PDBsum; 2O9R; -. DR PDBsum; 2O9T; -. DR PDBsum; 2Z1S; -. DR AlphaFoldDB; P22505; -. DR SMR; P22505; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR eggNOG; COG2723; Bacteria. DR EvolutionaryTrace; P22505; -. DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001360; Glyco_hydro_1. DR InterPro; IPR018120; Glyco_hydro_1_AS. DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase. DR InterPro; IPR033132; Glyco_hydro_1_N_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR NCBIfam; TIGR03356; BGL; 1. DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1. DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 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 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; KW Hydrolase; Polysaccharide degradation. FT CHAIN 1..448 FT /note="Beta-glucosidase B" FT /id="PRO_0000063872" FT ACT_SITE 167 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 356 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 20..23 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 36..40 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 59..71 FT /evidence="ECO:0007829|PDB:2O9P" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 96..112 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 115..123 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 139..154 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 168..176 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 188..211 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 216..223 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 226..232 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 234..247 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 249..257 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 262..268 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 269..275 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 282..286 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 300..305 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 308..312 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 332..344 FT /evidence="ECO:0007829|PDB:2O9P" FT TURN 345..349 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 352..357 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 373..389 FT /evidence="ECO:0007829|PDB:2O9P" FT TURN 390..393 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 396..402 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 410..415 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 420..423 FT /evidence="ECO:0007829|PDB:2O9P" FT TURN 425..427 FT /evidence="ECO:0007829|PDB:2O9P" FT STRAND 430..432 FT /evidence="ECO:0007829|PDB:2O9P" FT HELIX 434..445 FT /evidence="ECO:0007829|PDB:2O9P" SQ SEQUENCE 448 AA; 51573 MW; 628F44507C21EF1F CRC64; MSENTFIFPA TFMWGTSTSS YQIEGGTDEG GRTPSIWDTF CQIPGKVIGG DCGDVACDHF HHFKEDVQLM KQLGFLHYRF SVAWPRIMPA AGIINEEGLL FYEHLLDEIE LAGLIPMLTL YHWDLPQWIE DEGGWTQRET IQHFKTYASV IMDRFGERIN WWNTINEPYC ASILGYGTGE HAPGHENWRE AFTAAHHILM CHGIASNLHK EKGLTGKIGI TLNMEHVDAA SERPEDVAAA IRRDGFINRW FAEPLFNGKY PEDMVEWYGT YLNGLDFVQP GDMELIQQPG DFLGINYYTR SIIRSTNDAS LLQVEQVHME EPVTDMGWEI HPESFYKLLT RIEKDFSKGL PILITENGAA MRDELVNGQI EDTGRHGYIE EHLKACHRFI EEGGQLKGYF VWSFLDNFEW AWGYSKRFGI VHINYETQER TPKQSALWFK QMMAKNGF //