ID BGL1_ASPAC Reviewed; 860 AA. AC P48825; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 22-FEB-2023, entry version 88. DE RecName: Full=Beta-glucosidase 1; DE EC=3.2.1.21; DE AltName: Full=Beta-D-glucoside glucohydrolase; DE AltName: Full=Cellobiase; DE AltName: Full=Gentiobiase; DE Flags: Precursor; OS Aspergillus aculeatus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5053; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=F-50; RX PubMed=8964516; DOI=10.1016/0378-1119(96)00179-5; RA Kawaguchi T., Enoki T., Tsurumaki S., Sumitani J., Ueda M., Ooi T., RA Arai M.; RT "Cloning and sequencing of the cDNA encoding beta-glucosidase 1 from RT Aspergillus aculeatus."; RL Gene 173:287-288(1996). 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 3 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; D64088; BAA10968.1; -; mRNA. DR PIR; JC4939; JC4939. DR PDB; 4IIB; X-ray; 1.80 A; A/B=20-860. DR PDB; 4IIC; X-ray; 1.90 A; A/B=20-860. DR PDB; 4IID; X-ray; 2.30 A; A/B=20-860. DR PDB; 4IIE; X-ray; 2.00 A; A/B=20-860. DR PDB; 4IIF; X-ray; 2.45 A; A/B=20-860. DR PDB; 4IIG; X-ray; 2.30 A; A/B=20-860. DR PDB; 4IIH; X-ray; 2.00 A; A/B=20-860. DR PDBsum; 4IIB; -. DR PDBsum; 4IIC; -. DR PDBsum; 4IID; -. DR PDBsum; 4IIE; -. DR PDBsum; 4IIF; -. DR PDBsum; 4IIG; -. DR PDBsum; 4IIH; -. DR AlphaFoldDB; P48825; -. DR SMR; P48825; -. DR BindingDB; P48825; -. DR ChEMBL; CHEMBL3493; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR CLAE; BGL3A_ASPAC; -. DR CLAE; BGL3A_ASPSA; -. DR VEuPathDB; FungiDB:ASPACDRAFT_50312; -. DR BRENDA; 3.2.1.21; 488. DR UniPathway; UPA00696; -. 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1. DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR026891; Fn3-like. DR InterPro; IPR019800; Glyco_hydro_3_AS. DR InterPro; IPR002772; Glyco_hydro_3_C. DR InterPro; IPR036881; Glyco_hydro_3_C_sf. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR036962; Glyco_hydro_3_N_sf. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1. DR PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-RELATED; 1. DR Pfam; PF14310; Fn3-like; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR Pfam; PF01915; Glyco_hydro_3_C; 1. DR PRINTS; PR00133; GLHYDRLASE3. DR SMART; SM01217; Fn3_like; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycoprotein; KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..860 FT /note="Beta-glucosidase 1" FT /id="PRO_0000011776" FT ACT_SITE 280 FT /evidence="ECO:0000250" FT CARBOHYD 61 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 211 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 252 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 315 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 322 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 354 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 387 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 442 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 523 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 542 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 564 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 658 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 668 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 690 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 712 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 41..51 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 56..63 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 109..115 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 118..134 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 165..181 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 185..192 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 202..207 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 222..227 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 231..238 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 260..263 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 264..270 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 288..293 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 297..304 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 314..321 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 327..343 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 362..367 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 368..371 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 372..377 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 386..388 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 389..398 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 401..407 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 416..422 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 423..425 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 449..452 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 462..472 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 476..480 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 486..495 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 497..505 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 517..520 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 530..540 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 542..552 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 557..561 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 565..570 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 578..586 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 602..604 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 605..607 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 623..625 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 627..630 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 634..639 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 657..666 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 691..694 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 711..714 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 716..720 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 723..726 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 729..732 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 735..738 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 750..754 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 756..759 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 761..771 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 773..775 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 777..779 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 782..786 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 796..800 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 803..805 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 810..818 FT /evidence="ECO:0007829|PDB:4IIB" FT HELIX 819..822 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 824..826 FT /evidence="ECO:0007829|PDB:4IIB" FT TURN 827..830 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 831..833 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 840..846 FT /evidence="ECO:0007829|PDB:4IIB" FT STRAND 852..855 FT /evidence="ECO:0007829|PDB:4IIB" SQ SEQUENCE 860 AA; 93053 MW; 4B484778B00FC694 CRC64; MKLSWLEAAA LTAASVVSAD ELAFSPPFYP SPWANGQGEW AEAYQRAVAI VSQMTLDEKV NLTTGTGWEL EKCVGQTGGV PRLNIGGMCL QDSPLGIRDS DYNSAFPAGV NVAATWDKNL AYLRGQAMGQ EFSDKGIDVQ LGPAAGPLGR SPDGGRNWEG FSPDPALTGV LFAETIKGIQ DAGVVATAKH YILNEQEHFR QVAEAAGYGF NISDTISSNV DDKTIHEMYL WPFADAVRAG VGAIMCSYNQ INNSYGCQNS YTLNKLLKAE LGFQGFVMSD WGAHHSGVGS ALAGLDMSMP GDITFDSATS FWGTNLTIAV LNGTVPQWRV DDMAVRIMAA YYKVGRDRLY QPPNFSSWTR DEYGFKYFYP QEGPYEKVNH FVNVQRNHSE VIRKLGADST VLLKNNNALP LTGKERKVAI LGEDAGSNSY GANGCSDRGC DNGTLAMAWG SGTAEFPYLV TPEQAIQAEV LKHKGSVYAI TDNWALSQVE TLAKQASVSL VFVNSDAGEG YISVDGNEGD RNNLTLWKNG DNLIKAAANN CNNTIVVIHS VGPVLVDEWY DHPNVTAILW AGLPGQESGN SLADVLYGRV NPGAKSPFTW GKTREAYGDY LVRELNNGNG APQDDFSEGV FIDYRGFDKR NETPIYEFGH GLSYTTFNYS GLHIQVLNAS SNAQVATETG AAPTFGQVGN ASDYVYPEGL TRISKFIYPW LNSTDLKASS GDPYYGVDTA EHVPEGATDG SPQPVLPAGG GSGGNPRLYD ELIRVSVTVK NTGRVAGDAV PQLYVSLGGP NEPKVVLRKF DRLTLKPSEE TVWTTTLTRR DLSNWDVAAQ DWVITSYPKK VHVGSSSRQL PLHAALPKVQ //