ID A0A319CNI5_9EURO Unreviewed; 848 AA.
AC A0A319CNI5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=BO82DRAFT_399392 {ECO:0000313|EMBL:PYH84557.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH84557.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH84557.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH84557.1,
RC ECO:0000313|Proteomes:UP000248340};
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 (DEC-2016) 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; KZ821683; PYH84557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CNI5; -.
DR STRING; 1448315.A0A319CNI5; -.
DR VEuPathDB; FungiDB:BO82DRAFT_399392; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000248340; 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:UP000248340}.
FT DOMAIN 412..571
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 848 AA; 92693 MW; 774F162E5929CBD6 CRC64;
MPFVEPSPPE TDSAFAQIAS ADVEVLLKQL TLDEKVALLT GDDFWHTVAI PRLGIPSIRL
SDGPNGVRGT RFFGSVPAAC LPCGTALGAT FDRDLAEEVG GLLADEAKAK GAHVILGPTI
NIQRGPLGGR GFESYSEDPL LSGIMAGHYC KGLQQKNISA TLKHFVCNDQ EHERMAVNSI
VTDRAMREIY LLPFMLAIGV EKPDAIMTAY NKVNGIHASE SPALLQDILR GEWDWDGLLM
SDWFGTYSTS EAVQAGLDLE MPGPSRWRGS ALTHAITANK VSTATLDARV RAVLKLVQKA
SRSGIPEHAT EQQLNREQDR QLLRKIAAAT IVLLKNEDSI LPLDKHKKIA VIGPNSQIAT
YCGGGSAALN PYEAISPFEG ITRSAQADVE FAQGVYGHQM LPLLGKRLQT SDGQTGFTLK
IFNDPPTVLT RQPLEVRHET DAQVFFLDYS HPELQPVWYA EAEGDFIPEE SGLHDFGLCV
RGTGKLYVDG NLLVNNADVQ RPGPSFLGSG TLEETGTLDL VAGRSYRVQV QWGCAKTAKF
KIPGVVDFGH GGFRFGACKQ LSPQEGIEQG VKLAASVDQV ILVAGLSAEW ESEGEDRTGM
SLPPHTDELI SRVLEANPDT VVVVQSGTPV EMPWIDNAKA VLHAWYGGNE TGNGLADVIF
GDMNPSGKLP LTFPRRLKDN PTYFNFRSEG GRVLYGEDVY VGYRFYDEAE IEPLFPFGHG
LSYTTFGLSD LRLERNVDNN IQVRCKVRNT GTKAGAEVIQ VYVEPVQAPL KRPQKELKEF
RKIRLEPDAE EVVTIPLDLV RATSFWDEKA SAWCSHSGTY RILVGTSSRG HFLEASVDVE
ETTFWSGV
//
