ID A0A0F0HZ06_ASPPU Unreviewed; 633 AA.
AC A0A0F0HZ06;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=P875_00053088 {ECO:0000313|EMBL:KJK60715.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK60715.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK60715.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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 -!- 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:KJK60715.1}.
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DR EMBL; JZEE01000732; KJK60715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0HZ06; -.
DR STRING; 1403190.A0A0F0HZ06; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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 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 PANTHER; PTHR30620:SF120; BETA-GLUCOSIDASE C; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..633
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002442886"
FT DOMAIN 61..410
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 481..622
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 69908 MW; EA43D27779E19622 CRC64;
MRIDCAVASL TALATGCQAL STRPYVPRGH SLLRRNDSAP IYKDASYCID ERVDDLLARM
TIEEKAGQLF HTRLSDGPLD DEGSGNNAHN STSNMIGEKY MTHFNLASDI TNATETAEFI
NRIQELALQT RLGIPVTVST DPRHSFTENV GTGFKAGVFS QWPESIGLAA LRDPHVVRKF
AEVAKEEYIA VGIRAALHPQ VDLSTEPRWA RISNTWGENS TLTSELLVEY IKGFQGDKLG
PQSVKTVTKH FPGGGPVENG EDSHFAYGKN QTYPGNNLEE HLKPFKAAIA AGATEIMPYY
SRPIGTEYDP VAFSFNKRIV TELLRNELGF EGIVLTDWGL ITDGYIAGQY MPARAWGVEN
LTELERAARI LDAGCDQFGG EERPELIVQL VQEGTVSEDR IDVSVRRLLR EKFGLGLFDN
PFVDPESAGR VVGNDYFVRL GREAQRRSYT LLSNNEDIVP LKKIEQSTKF YIEGFNASFI
ESWNYTVVDS PEEADYALLR YNAPYEPRPG GFEANMHAGS LAFNDTEKAR QAKIYSAVPT
IVDIVMDRPA VIPEIIEQAK AVFASYGSDS NAFLDVVFGV SAPEGKLPFD LPSSMEAVEA
QMEDVPFDTR NPVFKFGHGL SYANPCASSS KCS
//
