ID BGLA_THEMA Reviewed; 446 AA. AC Q08638; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 133. 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; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=8277941; DOI=10.1007/bf00277355; RA Liebl W., Gabelsberger J., Schleifer K.H.; RT "Comparative amino acid sequence analysis of Thermotoga maritima beta- RT glucosidase (BglA) deduced from the nucleotide sequence of the gene RT indicates distant relationship between beta-glucosidases of the BGA family RT and other families of beta-1,4-glycosyl hydrolases."; RL Mol. Gen. Genet. 242:111-115(1994). 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 -!- CAUTION: As the DNA coding for this protein is not found in the CC complete genome of T.maritima. It could have originated from another CC bacterial species. {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; X74163; CAA52276.1; -; Genomic_DNA. DR PIR; S41561; S34570. DR RefSeq; WP_004082398.1; NZ_CP011107.1. DR PDB; 1OD0; X-ray; 2.11 A; A/B=2-446. DR PDB; 1OIF; X-ray; 2.12 A; A/B=2-446. DR PDB; 1OIM; X-ray; 2.15 A; A/B=2-446. DR PDB; 1OIN; X-ray; 2.15 A; A/B=2-446. DR PDB; 1UZ1; X-ray; 2.00 A; A/B=2-446. DR PDB; 1W3J; X-ray; 2.00 A; A/B=2-446. DR PDB; 2CBU; X-ray; 1.85 A; A/B=2-446. DR PDB; 2CBV; X-ray; 1.95 A; A/B=2-446. DR PDB; 2CES; X-ray; 2.15 A; A/B=2-446. DR PDB; 2CET; X-ray; 1.97 A; A/B=2-446. DR PDB; 2J75; X-ray; 1.85 A; A/B=2-446. DR PDB; 2J77; X-ray; 2.10 A; A/B=2-446. DR PDB; 2J78; X-ray; 1.65 A; A/B=2-446. DR PDB; 2J79; X-ray; 1.94 A; A/B=2-446. DR PDB; 2J7B; X-ray; 1.87 A; A/B=2-446. DR PDB; 2J7C; X-ray; 2.09 A; A/B=2-446. DR PDB; 2J7D; X-ray; 2.24 A; A/B=2-446. DR PDB; 2J7E; X-ray; 2.19 A; A/B=2-446. DR PDB; 2J7F; X-ray; 2.28 A; A/B=2-446. DR PDB; 2J7G; X-ray; 1.91 A; A/B=2-446. DR PDB; 2J7H; X-ray; 1.95 A; A/B=2-446. DR PDB; 2JAL; X-ray; 1.90 A; A/B=2-446. DR PDB; 2VRJ; X-ray; 1.90 A; A/B=2-446. DR PDB; 2WBG; X-ray; 1.85 A; A/B/C/D=2-446. DR PDB; 2WC3; X-ray; 2.00 A; A/B/C/D=2-446. DR PDB; 2WC4; X-ray; 1.70 A; A/B/C/D=2-446. DR PDB; 4GXP; X-ray; 3.00 A; A/B/C=1-160, A/B/C=204-217, A/B/C=352-380, A/B/C=395-446. DR PDB; 5N6S; X-ray; 2.10 A; A/B/C/D=2-446. DR PDB; 5N6T; X-ray; 2.10 A; A/B=2-446. DR PDB; 5OSS; X-ray; 1.70 A; A/B=2-446. DR PDBsum; 1OD0; -. DR PDBsum; 1OIF; -. DR PDBsum; 1OIM; -. DR PDBsum; 1OIN; -. DR PDBsum; 1UZ1; -. DR PDBsum; 1W3J; -. DR PDBsum; 2CBU; -. DR PDBsum; 2CBV; -. DR PDBsum; 2CES; -. DR PDBsum; 2CET; -. DR PDBsum; 2J75; -. DR PDBsum; 2J77; -. DR PDBsum; 2J78; -. DR PDBsum; 2J79; -. DR PDBsum; 2J7B; -. DR PDBsum; 2J7C; -. DR PDBsum; 2J7D; -. DR PDBsum; 2J7E; -. DR PDBsum; 2J7F; -. DR PDBsum; 2J7G; -. DR PDBsum; 2J7H; -. DR PDBsum; 2JAL; -. DR PDBsum; 2VRJ; -. DR PDBsum; 2WBG; -. DR PDBsum; 2WC3; -. DR PDBsum; 2WC4; -. DR PDBsum; 4GXP; -. DR PDBsum; 5N6S; -. DR PDBsum; 5N6T; -. DR PDBsum; 5OSS; -. DR AlphaFoldDB; Q08638; -. DR SMR; Q08638; -. DR DrugBank; DB08260; (1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamide. DR DrugBank; DB08090; (3Z,5S,6R,7S,8R,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol. DR DrugBank; DB07370; (3Z,5S,6R,7S,8R,8aS)-3-(octylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-5,6,7,8-tetrol. DR DrugBank; DB07367; (3Z,5S,6R,7S,8S,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol. DR DrugBank; DB04545; Afegostat. DR DrugBank; DB04658; Calystegine B2. DR DrugBank; DB03206; Duvoglustat. DR DrugBank; DB03862; Tetrahydrooxazine. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR PaxDb; 243274-THEMA_04935; -. DR KEGG; tmw:THMA_1897; -. DR PATRIC; fig|243274.18.peg.955; -. DR eggNOG; COG2723; Bacteria. DR UniPathway; UPA00696; -. DR EvolutionaryTrace; Q08638; -. 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. FT CHAIN 1..446 FT /note="Beta-glucosidase A" FT /id="PRO_0000063879" FT ACT_SITE 166 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 351 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055" FT STRAND 11..15 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 34..39 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 57..70 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 75..79 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 95..110 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 114..122 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:2J78" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 139..154 FT /evidence="ECO:0007829|PDB:2J78" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 167..175 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 187..211 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 216..231 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 233..246 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 249..257 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 262..268 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 288..302 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:5N6S" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:2WC4" FT STRAND 310..313 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 329..342 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 347..352 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 369..387 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 392..398 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 406..411 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 416..419 FT /evidence="ECO:0007829|PDB:2J78" FT TURN 421..423 FT /evidence="ECO:0007829|PDB:2J78" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:2J78" FT HELIX 430..441 FT /evidence="ECO:0007829|PDB:2J78" SQ SEQUENCE 446 AA; 51548 MW; 2E5B06E72BF84C01 CRC64; MNVKKFPEGF LWGVATASYQ IEGSPLADGA GMSIWHTFSH TPGNVKNGDT GDVACDHYNR WKEDIEIIEK LGVKAYRFSI SWPRILPEGT GRVNQKGLDF YNRIIDTLLE KGITPFVTIY HWDLPFALQL KGGWANREIA DWFAEYSRVL FENFGDRVKN WITLNEPWVV AIVGHLYGVH APGMRDIYVA FRAVHNLLRA HARAVKVFRE TVKDGKIGIV FNNGYFEPAS EKEEDIRAVR FMHQFNNYPL FLNPIYRGDY PELVLEFARE YLPENYKDDM SEIQEKIDFV GLNYYSGHLV KFDPDAPAKV SFVERDLPKT AMGWEIVPEG IYWILKKVKE EYNPPEVYIT ENGAAFDDVV SEDGRVHDQN RIDYLKAHIG QAWKAIQEGV PLKGYFVWSL LDNFEWAEGY SKRFGIVYVD YSTQKRIVKD SGYWYSNVVK NNGLED //