ID A0A072PH96_9EURO Unreviewed; 765 AA.
AC A0A072PH96;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=A1O9_04348 {ECO:0000313|EMBL:KEF59504.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF59504.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF59504.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF59504.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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:KEF59504.1}.
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DR EMBL; AMGV01000003; KEF59504.1; -; Genomic_DNA.
DR RefSeq; XP_013262094.1; XM_013406640.1.
DR AlphaFoldDB; A0A072PH96; -.
DR STRING; 1182545.A0A072PH96; -.
DR GeneID; 25279281; -.
DR VEuPathDB; FungiDB:A1O9_04348; -.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OrthoDB; 5485475at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000027920; 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: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 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:UP000027920};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..765
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001681612"
FT DOMAIN 685..753
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 765 AA; 83340 MW; 9B0B64939C068490 CRC64;
MAGRFLSLFA LNVSAALSAV LLPRQGSSAW EDKSLPAGER ADNLLPQLSW EEKIAQMGGI
RQLLQANASF NRTNWNNLYP LQHGILSYGS QLNQAQDVLP YANMVREEQL NSSKVPWITV
TDSVNSIYVP GGTIFPATLS LSTSWNLSMY EQVVAAIRDE NMALGTHWVL SPELDVAKEP
RNGRVGEMYG EDVYLIGEFA AQYVRTMQER DENGYIKVGT TVKHFLYGLG MGGINTASMD
GGVNHLYNDL AIPYIRVLKE NPTAIMISYS SIDRTPMSMN TALIQGMLRS EMGFQGLIMS
DAMGIMHLYT QSMVASSYKD AAIKALRAGL QLELAPGQPA CFPFLVSSSN DQEIVDLVDE
AVRQNLIIKF ETGMFDLPLP TLEQLNRTLR SNDHLEINRQ ASREAIVLLS NDGFLPQANL
SKVALIGPFG DILDPGSYAP STAATPLHGQ TLKDVLETRF SPANVQYVKG VDIRTTSSDD
EAGIEDAVIA ARNAGVAVLA LGSLSVYFLD PITGQRTDGE FFSHADLGLP GRQQQLLDAV
LDTGVPTILV LNGGQAFVLN NSTKRANAIL HQFLGGEFSA DALVEIITGQ VNPSGKLTIT
MPPAEGAFPI YYDYLPSDNV GGAAGYNGCA GDWSFPCLNR DDAPMAFGYG LSYTTFDISA
PQISNSSGVS ISCTVTNTGI VAGKEVVQVY FRQQYSEIEL PNKRLIRFEK IELQPGETRQ
VGFSIDRNDL GYYNNAKYQV DSGNYTFWVG SSSRMADLKN ATITL
//
