ID BGLH_NEOFI Reviewed; 829 AA. AC A1DPG0; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Probable beta-glucosidase H; DE EC=3.2.1.21; DE AltName: Full=Beta-D-glucoside glucohydrolase H; DE AltName: Full=Cellobiase H; DE AltName: Full=Gentiobiase H; GN Name=bglH; ORFNames=NFIA_060370; OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=331117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / RC NRRL 181 / WB 181; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). 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; DS027698; EAW16681.1; -; Genomic_DNA. DR RefSeq; XP_001258578.1; XM_001258577.1. DR AlphaFoldDB; A1DPG0; -. DR SMR; A1DPG0; -. DR STRING; 331117.A1DPG0; -. DR GlyCosmos; A1DPG0; 6 sites, No reported glycans. DR EnsemblFungi; EAW16681; EAW16681; NFIA_060370. DR GeneID; 4585094; -. DR KEGG; nfi:NFIA_060370; -. DR VEuPathDB; FungiDB:NFIA_060370; -. DR eggNOG; ENOG502SMPY; Eukaryota. DR HOGENOM; CLU_004542_4_0_1; -. DR OMA; DVKHNPA; -. DR OrthoDB; 5486783at2759; -. DR UniPathway; UPA00696; -. DR Proteomes; UP000006702; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; 2.60.120.260; Galactose-binding domain-like; 1. 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; 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 InterPro; IPR037524; PA14/GLEYA. DR InterPro; IPR011658; PA14_dom. DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1. DR PANTHER; PTHR42715:SF17; BETA-GLUCOSIDASE H-RELATED; 1. DR Pfam; PF14310; Fn3-like; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR Pfam; PF01915; Glyco_hydro_3_C; 1. DR Pfam; PF07691; PA14; 1. DR PRINTS; PR00133; GLHYDRLASE3. DR SMART; SM01217; Fn3_like; 1. DR SMART; SM00758; PA14; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF56988; Anthrax protective antigen; 1. DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1. DR PROSITE; PS51820; PA14; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted. FT CHAIN 1..829 FT /note="Probable beta-glucosidase H" FT /id="PRO_0000394882" FT DOMAIN 389..548 FT /note="PA14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164" FT ACT_SITE 225 FT /evidence="ECO:0000250" FT CARBOHYD 13 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 304 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 473 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 602 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 627 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 664 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 829 AA; 90819 MW; 76A219B2EEEF9D68 CRC64; MTAKFDVDYV LANITEDDKI ALLSGSDFWH THAIPKFNVP PIRTTDGPNG IRGTKFFAGV PAACLPCGTA LGATWDRDLL HQAGVLLGKE CLAKGAHCWL GPTINMQRSP LGGRGFESFA EDPHLSGIMA KSIILGCEST GVISTVKHYV GNDQEHERRA VDVLVTPRAL REIYLRPFQI VARDAHPGAL MTSYNKINGK HVVENPAMLD IVRKDWNWDP LIMSDWLGTY TTIDSMNAGL DLEMPGPTRY RGKYIESAMQ ARLIKQSTIN KRARKVLEFV QRASRAPVSA DETGRDFPED RALNRTLCAN SIVLLKNDGN LLPIPKTVKK IALIGSHVKT PAISGGGSAS LEPYYAVSLY DAVVEALPDA KILYEAGAYA HKMLPVIDRM LSNAVIHFYN EPPEKERTLL ATEPVVNTAF QLMDYNAPGL NRGLFWATLI GEFTPDVSGL WDFGLTVFGT ATLFVDDEMV IDNTTRQTRG TAFFGKGTVQ EVGQKQLTAG QTYKIRIEFG SANTSPMKAI GVVHFGGGAA HLGACLHMDP EQMVANAVKV AAEADYTIVC TGLNRDWESE GFDRPDMDLP PGIDALISSV LDLAADRTVI VNQSGTPVTL PWADRARGVV QAWYGGNETG HGIADVLFGD VNPCGKLPLS WPVDVKHNPA YLNNMSVGGR MLYGEDVYMG YRFYEKVGRE VLFPFGHGLS YTTFSVSPEA TVSPSVFSSD SPPTARVLVK NTGPVAGAQI LQLYIAAPNS ATPRPVKELH GFTKVFLQPG EERTVAIHID KYATSFWDEI EDMWKSEEGV YQVLIGTSSQ EIVSRGEFRV EQTRYWRGV //