ID BGLS_HANAN Reviewed; 825 AA. AC P06835; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 04-NOV-2008, entry version 50. DE RecName: Full=Beta-glucosidase; DE EC=3.2.1.21; DE AltName: Full=Gentiobiase; DE AltName: Full=Cellobiase; DE AltName: Full=Beta-D-glucoside glucohydrolase; DE Flags: Precursor; OS Hansenula anomala (Yeast) (Candida pelliculosa). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4927; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Acetaetherius; RX MEDLINE=86016087; PubMed=2995925; DOI=10.1093/nar/13.17.6273; RA Kohchi C., Toh-e A.; RT "Nucleotide sequence of Candida pelliculosa beta-glucosidase gene."; RL Nucleic Acids Res. 13:6273-6282(1985). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D- CC glucose residues with release of beta-D-glucose. CC -!- PATHWAY: Glycan metabolism; cellulose degradation. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. 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; X02903; CAA26662.1; -; Genomic_DNA. DR PIR; B23783; GLHQ. DR GO; GO:0008422; F:beta-glucosidase activity; IEA:EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR InterPro; IPR002772; Glyco_hydro_3_C. DR InterPro; IPR001764; Glyco_hydro_3_N. DR Gene3D; G3DSA:3.20.20.300; Glyco_hydro_3_N; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR Pfam; PF01915; Glyco_hydro_3_C; 1. DR PRINTS; PR00133; GLHYDRLASE3. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 825 Beta-glucosidase. FT /FTId=PRO_0000011777. FT ACT_SITE 299 299 By similarity. FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT CARBOHYD 34 34 N-linked (GlcNAc...) (Potential). FT CARBOHYD 74 74 N-linked (GlcNAc...) (Potential). FT CARBOHYD 97 97 N-linked (GlcNAc...) (Potential). FT CARBOHYD 230 230 N-linked (GlcNAc...) (Potential). FT CARBOHYD 271 271 N-linked (GlcNAc...) (Potential). FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential). FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential). FT CARBOHYD 537 537 N-linked (GlcNAc...) (Potential). FT CARBOHYD 550 550 N-linked (GlcNAc...) (Potential). FT CARBOHYD 556 556 N-linked (GlcNAc...) (Potential). FT CARBOHYD 578 578 N-linked (GlcNAc...) (Potential). FT CARBOHYD 605 605 N-linked (GlcNAc...) (Potential). FT CARBOHYD 667 667 N-linked (GlcNAc...) (Potential). FT CARBOHYD 690 690 N-linked (GlcNAc...) (Potential). FT CARBOHYD 718 718 N-linked (GlcNAc...) (Potential). FT CARBOHYD 733 733 N-linked (GlcNAc...) (Potential). FT CARBOHYD 761 761 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 825 AA; 89561 MW; A43852FF3DE58B74 CRC64; MLLPLYGLAS FLVLSQAALV NTSAPQASND DPFNHSPSFY PTPQGGRIND GKWQAAFYRA RELVDQMSIA EKVNLTTGVG SASGPCSGNT GSVPRLNISS ICVQDGPLSV RAADLTDVFP CGMAASSSFN KQLIYDRAVA IGSEFKGKGA DAILGPVYGP MGVKAAGGRG WEGHGPDPYL EGVIAYLQTI GIQSQGVVST AKHLIGNEQE HFRFAKKDKH AGKIDPGMFN TSSSLSSEID DRAMHEIYLW PFAEAVRGGV SSIMCSYNKL NGSHACQNSY LLNYLLKEEL GFQGFVMTDW GALYSGIDAA NAGLDMDMPC EAQYFGGNLT TAVLNGTLPQ DRLDDMATRI LSALIYSGVH NPDGPNYNAQ TFLTEGHEYF KQQEGDIVVL NKHVDVRSDI NRAVALRSAV EGVVLLKNEH ETLPLGREKV KRISILGQAA GDDSKGTSCS LRGCGSGAIG TGYGSGAGTF SYFVTPADGI GARAQQEKIS YEFIGDSWNQ AAAMDSALYA DAAIEVANSV AGEEIGDVDG NYGDLNNLTL WHNAVPLIKN ISSINNNTIV IVTSGQQIDL EPFIDNENVT AVIYSSYLGQ DFGTVLAKVL FGDENPSGKL PFTIAKDVND YIPVIEKVDV PDPVDKFTES IYVDYRYFDK YNKPVRYEFG YGLSYSNFSL SDIEIQTLQP FSENAEPAAN YSETYQYKQS NMDPSEYTVP EGFKELANYT YPYIHDASSI KANSSYDYPE GYSTEQLDGP KSLAAGGLGG NHTCGMLVTL SLLKSQIKVL MLVGLHLNCM LDIQIMMNSQ HLQCNYVDLK RCFWIKIILK LFLLN //