ID BGLA_NIACI Reviewed; 450 AA. AC Q03506; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 110. DE RecName: Full=Beta-glucosidase; 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=bglA; OS Niallia circulans (Bacillus circulans). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia. OX NCBI_TaxID=1397; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29. RC STRAIN=ATCC 21783 / subsp. Alkalophilus; RX PubMed=8481013; DOI=10.1128/aem.59.3.927-932.1993; RA Paavilainen S.K., Hellman J., Korpela T.; RT "Purification, characterization, gene cloning, and sequencing of a new RT beta-glucosidase from Bacillus circulans subsp. alkalophilus."; RL Appl. Environ. Microbiol. 59:927-932(1993). 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; M96979; AAA22266.1; -; Genomic_DNA. DR PIR; A48969; A48969. DR PDB; 1QOX; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-450. DR PDBsum; 1QOX; -. DR AlphaFoldDB; Q03506; -. DR SMR; Q03506; -. DR MINT; Q03506; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR EvolutionaryTrace; Q03506; -. 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; KW Direct protein sequencing; Glycosidase; Hydrolase; KW Polysaccharide degradation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8481013" FT CHAIN 2..450 FT /note="Beta-glucosidase" FT /id="PRO_0000063870" FT ACT_SITE 166 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 355 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 11..15 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 34..40 FT /evidence="ECO:0007829|PDB:1QOX" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:1QOX" FT TURN 51..55 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 61..71 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 95..110 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 114..122 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:1QOX" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 138..154 FT /evidence="ECO:0007829|PDB:1QOX" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 167..175 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 187..210 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 233..244 FT /evidence="ECO:0007829|PDB:1QOX" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 248..255 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 261..269 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 280..284 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 298..303 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:1QOX" FT TURN 310..313 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 333..345 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 351..355 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 373..391 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 396..402 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 410..412 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 420..424 FT /evidence="ECO:0007829|PDB:1QOX" FT TURN 425..428 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 429..432 FT /evidence="ECO:0007829|PDB:1QOX" FT HELIX 434..445 FT /evidence="ECO:0007829|PDB:1QOX" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:1QOX" SQ SEQUENCE 450 AA; 51303 MW; C52C1DB233B72790 CRC64; MSIHMFPSDF KWGVATAAYQ IEGAYNEDGR GMSIWDTFAH TPGKVKNGDN GNVACDSYHR VEEDVQLLKD LGVKVYRFSI SWPRVLPQGT GEVNRAGLDY YHRLVDELLA NGIEPFCTLY HWDLPQALQD QGGWGSRITI DAFAEYAELM FKELGGKIKQ WITFNEPWCM AFLSNYLGVH APGNKDLQLA IDVSHHLLVA HGRAVTLFRE LGISGEIGIA PNTSWAVPYR RTKEDMEACL RVNGWSGDWY LDPIYFGEYP KFMLDWYENL GYKPPIVDGD MELIHQPIDF IGINYYTSSM NRYNPGEAGG MLSSEAISMG APKTDIGWEI YAEGLYDLLR YTADKYGNPT LYITENGACY NDGLSLDGRI HDQRRIDYLA MHLIQASRAI EDGINLKGYM EWSLMDNFEW AEGYGMRFGL VHVDYDTLVR TPKDSFYWYK GVISRGWLDL //