ID A0A421JB92_9ASCO Unreviewed; 835 AA.
AC A0A421JB92;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=JA9_005047 {ECO:0000313|EMBL:RLV86115.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV86115.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV86115.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV86115.1,
RC ECO:0000313|Proteomes:UP000286412};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RLV86115.1}.
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DR EMBL; NSDU01000012; RLV86115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JB92; -.
DR STRING; 2028340.A0A421JB92; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000286412; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 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.
DR PROSITE; PS51820; PA14; 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:UP000286412}.
FT DOMAIN 398..559
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 835 AA; 92146 MW; C71F37D9D85970E7 CRC64;
MSNNFDVEET LQQLTLEEKI SLLAGRDFWH TVPVKRLKIP SLRTSDGPNG VRGTRFFNGV
KSACFPCGTA LASTFNKELL NESGKLMGEE ARHKGAHILL GPTTNMQRGP LGGRGFESFS
EDPYLAGIVS AAIVNGVQSK HVAATIKHYV GNDLEHERNA SDSIVTPRAM REIYLEPFRL
AVKHASPKAF MTGYNKVNGQ HVSQSKLYID EILRKEWNWD GLVMSDWFGT YTANTSIENG
LDLEMPGPTR FRTPAAVGHM IQTRELHIND LDARVRNVLE MIKYALNSGI PEDCPEDEEN
NTEQTAKHLR QVAGESIVLL KNEGILPLKK TEKIAVIGPN AKIAAYCGGG SASLRAYYTV
TPYEGITKKL GKEPLYTPGA HGHKTLPDMG RITKNPVTGG MGLNMKFFHE PPTEKKRTQF
DEVDIDTSQA FLADYYNKNL KGNLFFVDIE GEFEVEESGE YEFGLTVWGS AQLFVNNKLV
VDNTKDQVGG DAFFNLGTVE KKGTIKLEKG ATNKIRVEFG SAPTSTVKSE DSVDFGGGGA
VRFGFAQVID PQVQISRAVE LAKSVDKVVL SIGLTQEWES EGFDRPNMDL PGYTNDLVRA
VLEANPNTVV VNQSGTPVEF PWLSKAKALV HAWFGGNETG NAIADVLFGD VNPSGKLGLS
WPLRVQDNPT FLNFRTEKGR VLYGEDVFIG YRYYEKLQKQ VAFPFGYGLS YTKFGYSDLK
VSADDKEIKV SATIKNSGDV DGAEVVQVYI APKSSSIIRP IKELKEFTKL PIKSGKSATA
SFTLSLKDSI SYFDEYQNAW CAEKGDYEVH VGPSSDDIEL IGAFTVTETK YWHGL
//
