ID BGLA_ACET2 Reviewed; 448 AA. AC P26208; A3DBX4; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=Beta-glucosidase A; DE EC=3.2.1.21; DE AltName: Full=Beta-D-glucoside glucohydrolase; DE AltName: Full=Cellobiase; DE AltName: Full=Gentiobiase; GN Name=bglA; OrderedLocusNames=Cthe_0212; OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=203119; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1909624; DOI=10.1111/j.1432-1033.1991.tb16186.x; RA Graebnitz F., Seiss M., Ruecknagel K.P., Staudenbauer W.L.; RT "Structure of the beta-glucosidase gene bglA of Clostridium thermocellum. RT Sequence analysis reveals a superfamily of cellulases and beta-glycosidases RT including human lactase/phlorizin hydrolase."; RL Eur. J. Biochem. 200:301-309(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., RA Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 3-448. RA Salama-Alber O., Bayer E.; RT "Crystal structure of Ruminiclostridium Thermocellum beta-Glucosidase A."; RL Submitted (JUL-2017) to the PDB data bank. 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 -!- PATHWAY: Glycan metabolism; cellulose degradation. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABN51453.1; Type=Erroneous initiation; Evidence={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; X60268; CAA42814.1; -; Genomic_DNA. DR EMBL; CP000568; ABN51453.1; ALT_INIT; Genomic_DNA. DR PIR; S17215; S17215. DR PDB; 5OGZ; X-ray; 1.60 A; A/B=3-448. DR PDBsum; 5OGZ; -. DR AlphaFoldDB; P26208; -. DR SMR; P26208; -. DR STRING; 203119.Cthe_0212; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR DNASU; 4808630; -. DR KEGG; cth:Cthe_0212; -. DR eggNOG; COG2723; Bacteria. DR HOGENOM; CLU_001859_1_3_9; -. DR BRENDA; 3.2.1.21; 1530. DR UniPathway; UPA00696; -. DR Proteomes; UP000002145; Chromosome. 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-UniPathway. 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; Reference proteome. FT CHAIN 1..448 FT /note="Beta-glucosidase A" FT /id="PRO_0000063876" 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:5OGZ" FT STRAND 11..15 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 34..39 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:5OGZ" FT TURN 51..55 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 57..71 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 95..110 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 114..122 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 126..130 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 138..154 FT /evidence="ECO:0007829|PDB:5OGZ" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 167..175 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 187..210 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 214..222 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 226..232 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 233..245 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 247..256 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 261..269 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 280..284 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 307..313 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 315..318 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 333..345 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 351..356 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 373..391 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 396..402 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 410..415 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 420..423 FT /evidence="ECO:0007829|PDB:5OGZ" FT TURN 425..427 FT /evidence="ECO:0007829|PDB:5OGZ" FT STRAND 430..432 FT /evidence="ECO:0007829|PDB:5OGZ" FT HELIX 434..445 FT /evidence="ECO:0007829|PDB:5OGZ" SQ SEQUENCE 448 AA; 51482 MW; D59B9EB7BEE67621 CRC64; MSKITFPKDF IWGSATAAYQ IEGAYNEDGK GESIWDRFSH TPGNIADGHT GDVACDHYHR YEEDIKIMKE IGIKSYRFSI SWPRIFPEGT GKLNQKGLDF YKRLTNLLLE NGIMPAITLY HWDLPQKLQD KGGWKNRDTT DYFTEYSEVI FKNLGDIVPI WFTHNEPGVV SLLGHFLGIH APGIKDLRTS LEVSHNLLLS HGKAVKLFRE MNIDAQIGIA LNLSYHYPAS EKAEDIEAAE LSFSLAGRWY LDPVLKGRYP ENALKLYKKK GIELSFPEDD LKLISQPIDF IAFNNYSSEF IKYDPSSESG FSPANSILEK FEKTDMGWII YPEGLYDLLM LLDRDYGKPN IVISENGAAF KDEIGSNGKI EDTKRIQYLK DYLTQAHRAI QDGVNLKAYY LWSLLDNFEW AYGYNKRFGI VHVNFDTLER KIKDSGYWYK EVIKNNGF //