ID Q9UUQ3_ORPSP Unreviewed; 657 AA. AC Q9UUQ3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 13-SEP-2023, entry version 85. DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:AAD45834.1}; DE EC=3.2.1.21 {ECO:0000313|EMBL:AAD45834.1}; GN Name=bgl1 {ECO:0000313|EMBL:AAD45834.1}; OS Orpinomyces sp. (strain PC-2). OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota; OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales; OC Neocallimastigaceae; Orpinomyces. OX NCBI_TaxID=50059 {ECO:0000313|EMBL:AAD45834.1}; RN [1] {ECO:0000313|EMBL:AAD45834.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC-2 {ECO:0000313|EMBL:AAD45834.1}; RX PubMed=15054209; DOI=10.1385/ABAB:113:1-3:233; RA Li X.L., Ljungdahl L.G., Ximenes E.A., Chen H., Felix C.R., Cotta M.A., RA Dien B.S.; RT "Properties of a recombinant beta-glucosidase from polycentric anaerobic RT fungus Orpinomyces PC-2 and its application for cellulose hydrolysis."; RL Appl. Biochem. Biotechnol. 113-116:233-250(2004). RN [2] {ECO:0000313|EMBL:AAD45834.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC-2 {ECO:0000313|EMBL:AAD45834.1}; RX PubMed=17019643; DOI=10.1007/s00284-006-0098-2; RA Chen H., Hopper S.L., Li X.L., Ljungdahl L.G., Cerniglia C.E.; RT "Isolation of extremely AT-rich genomic DNA and analysis of genes encoding RT carbohydrate-degrading enzymes from Orpinomyces sp. strain PC-2."; RL Curr. Microbiol. 53:396-400(2006). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. CC {ECO:0000256|RuleBase:RU003690}. 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; AF016864; AAD45834.1; -; mRNA. DR AlphaFoldDB; Q9UUQ3; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR CLAE; BGL1A_ORPSP; -. 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:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001360; Glyco_hydro_1. DR InterPro; IPR033132; Glyco_hydro_1_N_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1. DR PANTHER; PTHR10353:SF36; LACTASE-LIKE PROTEIN; 1. DR Pfam; PF00232; Glyco_hydro_1; 3. DR PRINTS; PR00131; GLHYDRLASE1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1. PE 2: Evidence at transcript level; KW Glycosidase {ECO:0000313|EMBL:AAD45834.1}; KW Hydrolase {ECO:0000313|EMBL:AAD45834.1}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..657 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004338235" FT REGION 445..464 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 657 AA; 75228 MW; C228E706C037478B CRC64; MKTLTVFSAL LAVTAAKKCI VKSDAAVASE AEEVTAELTA PEDSGVESGE DDELLDLSTI DYGDDVDMST VKKLPADFKW GAATAAYQVE GAWDEEGRGE SVWDHFTHLY PKNVESGDRS KDFSTNGNIA CDSYHKFDED VKMLKLMNAK YYRFSISWPR LFPDGQARKV DGKWNVNEKG AEYYDMVINT LLKNDIVPFV TLYHWDLPYA LHEKYGGWLD YHSQDDFAKY AEFCFERFGD RVKNWITINE PWVNCVSGYR LGPGKAPYRC TGEAPRKLQN STDLDLEGGC SYEIGPTQYS KNSEPLPANR VPQKLEDVWC SHNILLGHAK AVKVYREKFQ KKQKGLIGIT VDGEAQIPWV EPGMTKKEYE NNLKYANLAA EFRIGWYSDP PMVGDYPKSV KERMGKDLPE FTEEEKKILK GSSSDFLGWN TYTAHWAAQA KNEDGSYIQP PTAEEANFDN SKKDMWDDNC KGRGDGWTCI PPTLGSQAGS SWNTKFAPTI RVGLNWFSKR YEGLIKNGIV ITENGCAQPN YKVARANDEV TKKYFESIGQ PKYADTYKEE DIEREDNLEG TLMHDTYRID WYDQYLKNLR LAYAVDNIDV RGYMAWSLLD NFEWENGYET RFGMTYIDFY NDKEMKRVPK DSLEHLGQWY LENVEQN //