ID A0A1Z5SM83_HORWE Unreviewed; 798 AA.
AC A0A1Z5SM83;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 28-JUN-2023, 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=BTJ68_15138 {ECO:0000313|EMBL:OTA21476.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA21476.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA21476.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA21476.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-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|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:OTA21476.1}.
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DR EMBL; MUNK01000423; OTA21476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5SM83; -.
DR STRING; 1157616.A0A1Z5SM83; -.
DR VEuPathDB; FungiDB:BTJ68_15138; -.
DR InParanoid; A0A1Z5SM83; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000194280; 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:SF5; BETA-GLUCOSIDASE M-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 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:UP000194280};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..798
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013097329"
FT DOMAIN 717..786
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 798 AA; 85773 MW; 9A9BA851500C67B2 CRC64;
MAAKSLLAAS LLFLSGSDAF PRRGHGDHNR PNWQESQITE GQFSDVKQRW DTAIARADEL
VQQMTLEEVA NVTLGQSDTM GCSGLTGSVS RLGFPGICLA DGPAGVRGTT FVNAYPAGIH
AAASFNRKLA YERGLYMGGE FRNKGVDTAL SVCVGPVGRV ATGGRNWEAF GADPYLQGQL
GSQMVSGMQL SVTADVKHFL GNEQELFRNP VTNKNNVTIP AFDSIITDHD IHELYMWPFQ
DAVHAGAGSV MGAYQQVNGE YSCESSDLLN DLLKDELNFP GFVVSDWGAQ YTGWPSAASG
LDVAMPNSRG KWDGGNLEMS VRNGTLPESR LRDMGRRIVA SWFYVNFDDV EGEPGFGLAD
DGYNFPHDTV EARDPAAKAS IYQAALEGHV LVKNDGALPL KTPKILNLYG YDATLPPVLM
PNPSGFNDWN FGTSALDLEE SDNELRGMLF QEIRYSQAAT LGNLWVGGGS GGNSPPYVST
PYSALAAKAE MDGTILEWNF NASETNPSVN AEADACLVFI NDYASEGNDR AGVADPASDE
LVTNVAANCS NTVVVIHNAG QRTLDFAGHP NITAIIMAHL PGQDSGRALV SLLFGETSPT
GRLPYTIPYK AEDFGSLLYP VVTPEAAPSA NLSDPSEFDY KYFQSNDIKP RYAFGYGLTY
SSFSYSDVSV SWKDGSAPAS APPSVEVKVP GGVASLFDTV ATVSATITNT GSVAAAEVAQ
LYVRRPNEPE GVTPLRGFEK TAYLQPGESE CVKMHLRRKD LSTWSSDDQQ WLMMAGDYEL
MVGASAEDIR LTGSLSLK
//
