ID G7XEM4_ASPKW Unreviewed; 794 AA.
AC G7XEM4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AKAW_03681 {ECO:0000313|EMBL:GAA85567.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85567.1};
RN [1] {ECO:0000313|EMBL:GAA85567.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85567.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; DF126453; GAA85567.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XEM4; -.
DR STRING; 1033177.G7XEM4; -.
DR VEuPathDB; FungiDB:AKAW_03681; -.
DR eggNOG; ENOG502R4T1; Eukaryota.
DR InParanoid; G7XEM4; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
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:SF14; BETA-GLUCOSIDASE D-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 2.
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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAA85567.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..794
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003505545"
FT DOMAIN 710..779
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 186..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 84606 MW; FF6C1F9905A309DE CRC64;
MKVLSFIVAA ALLGLTGASS NSSQGLLKSD GVALGDWESA YQKASTFVAG LTIDQKLALI
TGSSVNSTNG SFSGLIFLDG DMGLQNFYYV SAFSLSSALA MTWDRDAIYA QGKAVGSEFY
NKGIQVVAGP TSQPLGRTPW SGRNVEGFGP DPYLNGLATG LTTKAYIDAG VIPGAKHFLL
YEQETNRTGG GGGGGGPGGG GMPSGGMGPG SSNTSSMGAK PTGSMGRRAA SSSSELDSGS
APYSSNVDDK TLHETYLWPF YDAVKHGLGA VMCAMTKVNG TLSCQNSGLL MKHLKTELGF
PGLVWPDTNG QSSALESALG GEDYGSSSIW STSTMETLLS NGSLSEARLD DMAIRNLMGY
YYVNLDNGLQ PEEQSEDAYV DVRRNHSKLI RENGAKSMAL LKNKNALPLK KPRVMSVFGA
HAGPVLGGPN TAMDIEGSGP TYQGHLATGT GSAQASLPYL VPPYVALTNR IIEDGTMMRW
VLNDTYTSSS TSGLITEGTD STAVDPSYAD YATNSDACLV FLNALSGEGA DRTELYNDDQ
DTMVNTVADN CNNTIVIINT VGPRLMDQWI EHDNVTAVLY GSLLGQESGN SIVDVLYGDV
NPSGRLIHTI AKNESDYNVK ICYTAQCNFT EGVYLDYRYF DAYNITPRYP FGHGLSYTTF
SYSDLNIEKP STLSKYPTGK QTVGGNSDLW DIVGSVSVKV ANTGSLDGAE VPQLYLGFPT
AAQQPVRQLR GFERVEIASG KQSEVTFKLR RRDISYWDVR AQQWLVASGD YKVYVGASSR
DLKLNGTFAV QISS
//
