ID A0A1E5RS86_9ASCO Unreviewed; 849 AA.
AC A0A1E5RS86;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AWRI3578_g1047 {ECO:0000313|EMBL:OEJ89678.1};
OS Hanseniaspora opuntiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=211096 {ECO:0000313|EMBL:OEJ89678.1, ECO:0000313|Proteomes:UP000095605};
RN [1] {ECO:0000313|Proteomes:UP000095605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3578 {ECO:0000313|Proteomes:UP000095605};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:OEJ89678.1}.
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DR EMBL; LPNL01000003; OEJ89678.1; -; Genomic_DNA.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000095605; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 410..572
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 849 AA; 94662 MW; B74BE7DFDBEF2E94 CRC64;
MTSFDPEQLI KQLTIDEKIQ LLTAKDYWHT VPIPRLNIPS IKVTDGPCGS RGSKSFNSTK
TAAFPCGTAL GSLFDKKRLF EVGQAMAIEA QHKSAKVILG PTTNIQRGPL GGRGFESISE
DPLLSGLAAA ELVNGIQSSG EVMATMKHFV CNDMEIXRFA YDXMVTDRAL REVYLEPFRL
AVKHSDPMFF MTAYNKVQGV HCSTSSKNIK DILHNEWNSR ALVMSDWYGS SHPMESIKAG
LDFDFPGPEK FRSVELIKHL LFSKAETRDG TIFTEHDIDL RVEKILNMIK YFVDVYGTTD
FTFDEDTSNN TPETSQFLRQ VAAESIVLLK NEDSVLPLKL SDADDLCIIG PNAKAKCHTG
GGSASLNAYY VVSPYEGILN VTEKXSLPYS KGCDAHKTLS NFIENCHTXD GQTGLSVKFY
QREDYKESGE SPFMVEVVDR SFNKMSDLRD PHIDVNEKLF YCDWEGFYTC QDGDGVYELG
CQVAGTALVY LDDKLIIDNK HGQVRGXFAY KAGTIEKXTC IEMKNGQTYK VRVAFGSIRT
SELEMVSGTT FGALQLGINK VIDAAEEIQY AVSLAKKHKN CIVVIGLNGE YETEGDDRPH
MHLPGLTDTL VSEVLKANPN AIVVNQSGTP VTVPWIDQCK VFLQAYYGGN ELGNAIADVI
FGNVNPGGKL SLSWPKKNED NPAFLNFTSH LGRVVYGEDI YVGYKYYDHA KRPTEFPFGF
GLSYTXFEFS DLKTSLXGND LLLEVTVKNT GSCAGSEVVQ IYTSRVDESL VPRVPKELKE
FEKVHLXXNE QTXVKFKLSV KDSFSYFNEI RXQWHLEKGK YXVSXGNSSS HLPLKEDVVI
NDDYHWSGL
//
