ID A0A364KLD9_9EURO Unreviewed; 831 AA.
AC A0A364KLD9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=BHQ10_000377 {ECO:0000313|EMBL:RAO64365.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO64365.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO64365.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO64365.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO64365.1}.
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DR EMBL; MIKG01000001; RAO64365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364KLD9; -.
DR STRING; 1196081.A0A364KLD9; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
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; 2.
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; 2.
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:UP000249363};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..831
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016941468"
FT DOMAIN 748..816
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 696..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 88723 MW; B9C0727700162380 CRC64;
MRNSLLISLA AAALAEGKAY SPPAYPAPWA SGAGEWAQAH DRAVEFVSQL TLAEKINLTT
GVGWEGGQCV GNTGSIPRLG FRSLCMQDSP LGVRDTDYNT AFPAGVNVAA TWDLDLAYRR
GVAMAEEHRG KGVDVQLGPV AGPLGRAPEG GRNWEGFAPD PVLTGQMMAS TIEGMQDTGV
IACAKHYIGN EQEHFRQGSQ ENYTVADAIS SNIDDVTLHE LYLWPFADAV RAGVGSVMCS
YNQLNNSYSC GNSYSLNHIL KGELDFQGFV MTDWGAQHSG VGDALAGADM DMPGDVAFDS
GTAFWGTNLT IAVLNGTVPE WRIDDMAVRI MSAFYKVGRD RTQVPINFAS WTLDTYGNEY
YYAGEGYKEI NQHVDVRGDH AKVVREIGSA SIVLLKNVDG ALPLTGSERF VAVFGEDAGS
NPDGVNGCSD RNCDNGTLAM GWGSGTANFP YLVTPEQAIQ AEVLKNGGIF TAITDSGATN
TTATTVAAQA SACLVFANAD SGEGYITVDG NVGDLVLHTV GPVLVEDWVN HPNITAVLWA
GLPGEQSGNS LVDVLYGSVN PGGKTPFTWG KQRSDWGTDI IYEPNNGDGA PQQDFTEGIF
IDYRHFDKYN ITPTYEFGYG LSYSTFSFSN LQVTPLAASP YKPATGHSGP APVLGKVLNA
TAYLFPNYIK RIEAFIYPWL NSTDLRTSSG DPNYGWSTSK YVPDGAQDGS PQPVNPAGGA
PGGNPALYDP VAEIRVTVKN TGKVAGVEVP QLYVSLGGPS DAPKVLRGFG RLSLGAGEEA
QWTATLTRRD VSNWDTVSQN WVVSNYTKTV YVGNSSRNLP LQQTLALKIG H
//
