ID A0A395I2M7_ASPHC Unreviewed; 839 AA.
AC A0A395I2M7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=BO97DRAFT_387062 {ECO:0000313|EMBL:RAL14431.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL14431.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL14431.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL14431.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; KZ824275; RAL14431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395I2M7; -.
DR STRING; 1450537.A0A395I2M7; -.
DR VEuPathDB; FungiDB:BO97DRAFT_387062; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000248961; 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|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000248961}.
FT DOMAIN 395..555
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 839 AA; 92240 MW; F3071EDC86F947E6 CRC64;
MPRLDVEKTL EELTLGEKVA LTAGIDFWHT AAVPRLNIPS LRMSDGPNGV RGTRFFNGVP
AACFPCATAL GATWDTELLH QVGRLMGEES IAKGSHIILG PTINIQRSPL GGRGFESYAE
DGVLSGTLAG HYCRGVQEKG VAATLKHFVC NDQEHERLAV DTIITDRALR EIYLLPFQLA
MRICPTACVM TAYNKVNGTH VSENKEIITE ILRKEWGWDG LVMSDWFGTY STSDAINAGL
DLEMPGKTRW RGTALAHAVS SNKVAEFVMD ERVRNVLNLV NWVEPLGIPE QAEEKALNRP
EDQALLRRAA SESVVLMKNE DDILPLKKDK SILVIGPNAK FAAYCGGGSA SLDPYYTVSP
FEGVSAKSQG SVQFSQGVYS HKELPLLGPL LKTEDGQTGF KFRVYNEPAS EPNRTLVDEL
HLVRSSGFLM DYVNPKIKSF TFYVDMEGYF TPEEDGIYDF GVTVVGTGKL YIDDEVVVDN
TKNQRQGTAF FGNATVEERG SKALKAGQTY RILLEFGSAP TSDLDMRGVV IFGPGGFRFG
ACRQVTQEDL MSDAVSLASS AEQVVIFAGL TSEWETEGHD RDHMDLPPGS DEMISRVLDA
NPNAVVVIQS GTPVTMPWVH KTKGLLHAWF GGNECGNGIA DVLYGDVNPA AKLPVSFPVR
LQDNPSYLNF RSERGRVLYG EDVYVGYRYY EKVDLAPLFP FGHGLSYTTF SRSNLRLTSA
PEQPRLGLDG EPITATVSVT NTGARPGAEI LQLWVSPPAT GVNRPKRELK GFAKVHLQPG
ETKEVEIVVE KKLATSWWDE QRAKWASEKG VYEVQVTGTG DGVLKAEFTV EKTRFWLGL
//
