ID A0A427YCM7_9TREE Unreviewed; 777 AA.
AC A0A427YCM7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 9.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=EHS25_003041 {ECO:0000313|EMBL:RSH88813.1};
OS Saitozyma podzolica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH88813.1, ECO:0000313|Proteomes:UP000279259};
RN [1] {ECO:0000313|EMBL:RSH88813.1, ECO:0000313|Proteomes:UP000279259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH88813.1,
RC ECO:0000313|Proteomes:UP000279259};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Saitozyma podzolica DSM 27192.";
RL Submitted (NOV-2018) 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|RuleBase:RU361161}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:RSH88813.1}.
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DR EMBL; RSCD01000016; RSH88813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427YCM7; -.
DR STRING; 1890683.A0A427YCM7; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000279259; 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; 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:SF19; BETA-GLUCOSIDASE G-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|RuleBase:RU361161};
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|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000279259};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..777
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019473822"
FT DOMAIN 692..762
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 777 AA; 85721 MW; C36DC847EF0F882C CRC64;
MWGLLQSALV YANALAPAWS GVSGVVPQKH HKAPHAPYAD GGAWADAFEL AKDAVLNMTV
EEKVNITSAI LGPCPSNTGG VPRLNITGMC FDDGPAGPRY TDFVTQFPSA FFAAASFDRD
LIYERAVRIG NEFRGKGINV ALAPVTGGPL GRSPYAGRNW EAFSPDPYLS ATMSGITVRG
MQSSGLITCA KHYVLYEQEP VCTGPLDWTG GRTDCRDVSS NVDDKTFKEL YLPSFVESVR
AGTGAVMCSY NLINGTFSCE NDYTMNTILK GELNFQGFIL SDYGATHSTI PSAMSGMDME
LPSVAYFGPH LLEAVKHGHV PVHRLDDMVR RILTPWYAFQ QHRSYPETNF QKWTLEDEIE
IDGRKFRNAH ADNRGDNPSF ARKIAAESTV LLKNTGVLPL RHIRRIGVFG SDADYPHTLS
GCGPDLFCMT ASKERYWNGT VTIGGGSGAA YADYVGIRVD HLLHDDPAHF VSMGFIASQS
EVCLVFVSVF LKENQDREPG LRLDKGGEDL IRAVEARCAG EVVVIIHAGG QVVVEDWVHL
PRIGGVIFAG YPGQETGNAL VDILWGDVNP SGKLPFTMGK ATSDWPTGNI LRETSRGWFG
SETNPRSVFS EGLAIDYKWF DKYDITPRYE FGFGLSYTTF EMASLKVEKT WIKATDTVQA
TNEKHEGGDG LYDTIYVARV NLTNTGSTAG AEVAQLYMSY PQSEVEQPPR HLKGFHKVYL
QPGQTQTVQM HLRKKDISVW DVKHQTWRIP KGRFVFYAGN SSRNLPLEFK LDVKDKK
//
