ID A0A225ASC2_9EURO Unreviewed; 886 AA.
AC A0A225ASC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=UA08_03394 {ECO:0000313|EMBL:OKL61254.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL61254.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL61254.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL61254.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00024983}.
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 Evidence={ECO:0000256|ARBA:ARBA00000448,
CC ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKL61254.1}.
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DR EMBL; LFMY01000004; OKL61254.1; -; Genomic_DNA.
DR RefSeq; XP_020121375.1; XM_020265690.1.
DR AlphaFoldDB; A0A225ASC2; -.
DR STRING; 1441469.A0A225ASC2; -.
DR GeneID; 31003149; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000214365; 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; 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:SF10; BETA-GLUCOSIDASE F-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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000214365};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..886
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012285063"
FT DOMAIN 792..867
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 29..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 95206 MW; 3F5A911744034EBF CRC64;
MAGGSHPFVL FILGLLLVHC AARGNDGGAS PTLHRHLTEQ EKSNKVKREG LPSNYSTPDY
YPTPHGGWVS SWTEAYAKAQ LVVSNMTLAE KVNITSGTGY FMGPCVGQTG SALRFGIPRL
CLQDSPLGIR DTENNTAFPA GVTTGATWDK ELIYARGVAI GEEARGKGVN VQMGPVVGPI
GRKPKSGRIW EGFGADPSLQ GLAAVQTIQG MQSVGVIATL KHFILNEQEM YRMTDPVQVG
YSSDIDDRTM HEIYLWPFAE GVRAGVGSVM AAYNHVNGSL CTQNSEILNG ILKDELGFQG
FVMSDWYAQD SGVPSALAGL DMAMPGDGAV PLIGVSWWNY ELSTAVLNGT VPLERLNDMV
TRVVAAWYQM GQDDDYPLPN FSSNTEDAVG PLYPGALFSP TGVVNQFVNV QGNHSIVARA
VARDAITLLK NVNETLPLSS SANLSVFGTD AGPNSKGLNS CTDMGCDNGI LTMGWGSGTS
RLPYVITPEE AIQNVSANTQ FYITDTFPSV TPNADEIAIV FINSDSGENY ITVDGNPGDR
LEAKLAAWHS GDELVVNAAA AFSTVIVVVH TVGPIIMEDW IDLPSVKGVL VAHLPGQEAG
NSLVDVLFGD YSPSGHLPYT IPHNESEYPA SVDLIDQVLG QIQDQYLERL YIDYRHFLQA
NITPRFPFGY GLSYTTFNFS DATIISGTTL TQYPPARASK GPTPTYATTI PPASEVAWPT
DISSIWRYLY PYLDDPEAAT STAPYPYPTG YSTTPHAAPR AGGSQGGNPA LWDTVFTISV
KVTNTGTRPG RAVAQLYVEL PADALGVDLP PRQLRQFEKT SILSPGDSET LTLPLTRKDL
SVWDVVMQDW LAPVDGEGVK FWIGQSVATE DLQIVCTVGQ GCESTS
//
