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 16-JUN-2009, entry version 66. DE RecName: Full=Beta-glucosidase A; DE EC=3.2.1.21; DE AltName: Full=Gentiobiase; DE AltName: Full=Cellobiase; DE AltName: Full=Beta-D-glucoside glucohydrolase; GN Name=bglA; OS Thermotoga maritima. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=2336; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX MEDLINE=94104595; PubMed=8277941; 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 RT family and other families of beta-1,4-glycosyl hydrolases."; RL Mol. Gen. Genet. 242:111-115(1994). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D- CC glucosyl residues with release of beta-D-glucose. CC -!- PATHWAY: Glycan metabolism; cellulose degradation. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. 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 CC another bacterial species. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X74163; CAA52276.1; -; Genomic_DNA. DR PIR; S41561; S34570. 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 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 CAZy; GH1; Glycoside Hydrolase Family 1. DR BRENDA; 3.2.1.21; 16699. DR GO; GO:0008422; F:beta-glucosidase activity; IEA:EC. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR InterPro; IPR001360; Glyco_hydro_1. DR InterPro; IPR018120; Glyco_hydro_1_AS. DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase. DR InterPro; IPR013781; Glyco_hydro_sg_catalytic. DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1. DR PANTHER; PTHR10353; Glyco_hydro_1; 1. DR Pfam; PF00232; Glyco_hydro_1; 1. DR PRINTS; PR00131; GLHYDRLASE1. DR TIGRFAMs; TIGR03356; BGL; 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 Glycosidase; Hydrolase; Polysaccharide degradation. FT CHAIN 1 446 Beta-glucosidase A. FT /FTId=PRO_0000063879. FT ACT_SITE 166 166 Proton donor (Potential). FT ACT_SITE 351 351 Nucleophile (By similarity). FT STRAND 11 15 FT HELIX 18 21 FT HELIX 27 29 FT HELIX 34 39 FT HELIX 46 48 FT STRAND 51 53 FT HELIX 57 70 FT STRAND 75 79 FT HELIX 82 85 FT STRAND 89 91 FT HELIX 95 110 FT STRAND 114 122 FT HELIX 126 129 FT TURN 130 132 FT HELIX 133 135 FT HELIX 139 154 FT TURN 155 157 FT STRAND 160 165 FT HELIX 167 175 FT HELIX 187 211 FT STRAND 216 229 FT HELIX 238 246 FT HELIX 249 257 FT HELIX 262 268 FT HELIX 269 271 FT HELIX 276 279 FT HELIX 280 283 FT STRAND 288 302 FT STRAND 310 313 FT HELIX 329 342 FT STRAND 347 352 FT HELIX 369 387 FT STRAND 392 398 FT HELIX 406 411 FT STRAND 416 419 FT TURN 421 423 FT STRAND 426 428 FT HELIX 430 440 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 //