ID BGLA_ASPFU Reviewed; 873 AA. AC Q4WJJ3; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 24-JAN-2024, entry version 99. DE RecName: Full=Probable beta-glucosidase A; DE EC=3.2.1.21; DE AltName: Full=Beta-D-glucoside glucohydrolase A; DE AltName: Full=Cellobiase A; DE AltName: Full=Gentiobiase A; DE Flags: Precursor; GN Name=bglA; Synonyms=bgl1; ORFNames=AFUA_1G05770; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes CC involved in the degradation of cellulosic biomass. Catalyzes the last CC step releasing glucose from the inhibitory cellobiose (By similarity). CC {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. 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; AAHF01000007; EAL88289.1; -; Genomic_DNA. DR RefSeq; XP_750327.1; XM_745234.1. DR PDB; 5FJI; X-ray; 1.95 A; A/B=30-873. DR PDBsum; 5FJI; -. DR AlphaFoldDB; Q4WJJ3; -. DR SMR; Q4WJJ3; -. DR STRING; 330879.Q4WJJ3; -. DR Allergome; 8995; Asp f Glucosidase. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR CLAE; BGL3A_ASPFU; -. DR GlyCosmos; Q4WJJ3; 12 sites, No reported glycans. DR EnsemblFungi; EAL88289; EAL88289; AFUA_1G05770. DR GeneID; 3507586; -. DR KEGG; afm:AFUA_1G05770; -. DR eggNOG; ENOG502QR4D; Eukaryota. DR HOGENOM; CLU_004542_2_0_1; -. DR InParanoid; Q4WJJ3; -. DR OMA; YYPSPWA; -. DR OrthoDB; 5486783at2759; -. DR UniPathway; UPA00696; -. DR Proteomes; UP000002530; Chromosome 1. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. 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; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..873 FT /note="Probable beta-glucosidase A" FT /id="PRO_0000394095" FT REGION 731..764 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 291 FT /evidence="ECO:0000250" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 222 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 263 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 326 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 333 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 365 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 453 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 534 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 553 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 575 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 679 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 725 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 51..61 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 66..73 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 80..87 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 120..126 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 129..145 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 176..192 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 233..238 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 242..249 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 253..257 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 259..262 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 271..274 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 275..281 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 286..290 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 299..304 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 308..315 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 325..332 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 338..354 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 357..360 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 372..378 FT /evidence="ECO:0007829|PDB:5FJI" FT TURN 379..382 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 383..388 FT /evidence="ECO:0007829|PDB:5FJI" FT TURN 397..399 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 400..409 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 412..418 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 427..433 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 434..436 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 447..449 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 460..463 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 473..483 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 487..491 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 497..506 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 508..516 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 528..531 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 541..549 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 553..563 FT /evidence="ECO:0007829|PDB:5FJI" FT TURN 568..572 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 576..581 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 586..588 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 589..597 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 613..615 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 616..618 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 634..636 FT /evidence="ECO:0007829|PDB:5FJI" FT TURN 638..641 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 645..650 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 668..677 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 704..707 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 724..727 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 729..733 FT /evidence="ECO:0007829|PDB:5FJI" FT TURN 736..739 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 742..744 FT /evidence="ECO:0007829|PDB:5FJI" FT TURN 748..751 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 769..772 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 774..784 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 786..788 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 790..792 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 795..799 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 809..813 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 816..818 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 823..831 FT /evidence="ECO:0007829|PDB:5FJI" FT HELIX 832..835 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 837..839 FT /evidence="ECO:0007829|PDB:5FJI" FT TURN 840..843 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 844..846 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 853..861 FT /evidence="ECO:0007829|PDB:5FJI" FT STRAND 865..868 FT /evidence="ECO:0007829|PDB:5FJI" SQ SEQUENCE 873 AA; 94753 MW; F942110284B04E9F CRC64; MRFGWLEVAA LTAASVANAQ VFDNSHGNNQ ELAFSPPFYP SPWADGQGEW ADAHRRAVEI VSQMTLAEKV NLTTGTGWEM DRCVGQTGSV PRLGINWGLC GQDSPLGIRF SDLNSAFPAG TNVAATWDKT LAYLRGKAMG EEFNDKGVDI LLGPAAGPLG KYPDGGRIWE GFSPDPALTG VLFAETIKGI QDAGVIATAK HYILNEQEHF RQVGEAQGYG YNITETISSN VDDKTMHELY LWPFADAVRA GVGAVMCSYN QINNSYGCQN SQTLNKLLKA ELGFQGFVMS DWSAHHSGVG AALAGLDMSM PGDISFDDGL SFWGTNLTVS VLNGTVPAWR VDDMAVRIMT AYYKVGRDRL RIPPNFSSWT RDEYGWEHSA VSEGAWTKVN DFVNVQRSHS QIIREIGAAS TVLLKNTGAL PLTGKEVKVG VLGEDAGSNP WGANGCPDRG CDNGTLAMAW GSGTANFPYL VTPEQAIQRE VISNGGNVFA VTDNGALSQM ADVASQSSVS LVFVNADSGE GFISVDGNEG DRKNLTLWKN GEAVIDTVVS HCNNTIVVIH SVGPVLIDRW YDNPNVTAII WAGLPGQESG NSLVDVLYGR VNPSAKTPFT WGKTRESYGA PLLTEPNNGN GAPQDDFNEG VFIDYRHFDK RNETPIYEFG HGLSYTTFGY SHLRVQALNS SSSAYVPTSG ETKPAPTYGE IGSAADYLYP EGLKRITKFI YPWLNSTDLE DSSDDPNYGW QDSEYIPEGA RDGSPQPLLK AGGAPGGNPT LYQDLVRVSA TITNTGNVAG YEVPQLYVSL GGPNEPRVVL RKFDRIFLAP GEQKVWTTTL NRRDLANWDV EAQDWVITKY PKKVHVGSSS RKLPLRAPLP RVY //