ID A0A1F8AAD4_9EURO Unreviewed; 768 AA.
AC A0A1F8AAD4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Probable beta-glucosidase M {ECO:0000256|ARBA:ARBA00039571};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase M {ECO:0000256|ARBA:ARBA00041282};
DE AltName: Full=Cellobiase M {ECO:0000256|ARBA:ARBA00041589};
DE AltName: Full=Gentiobiase M {ECO:0000256|ARBA:ARBA00041805};
GN ORFNames=ABOM_001960 {ECO:0000313|EMBL:OGM48690.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM48690.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM48690.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
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}.
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:OGM48690.1}.
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DR EMBL; LYCR01000014; OGM48690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8AAD4; -.
DR STRING; 109264.A0A1F8AAD4; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
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:SF5; BETA-GLUCOSIDASE M-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.
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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..768
FT /note="Probable beta-glucosidase M"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009534652"
FT DOMAIN 691..757
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 768 AA; 82353 MW; CB350D2A144AA174 CRC64;
MHAIAGLAGL LAGVSLSYAA PTQENITSDA YFYGQSPAVY PSPEGTGSGA WASAYEKAKA
FVANLTPEEK VNLTAGVDAD NGCSGNIPAI PRLNFPGLCV SDAGNGLRST DHVNAWSSGV
HAGASWNKDL VHKRGLHMGS EYHKKGVHVL LGPVVGPIGR IAEGGRNWEG FSTDPYHSGL
LVSETIRGVQ AAGVGTSTKH YIANEQETNR NPETTDGLNI ASSSSNIDDK TMHELYLWPF
QDAVRAGSVS IMCSYQRINN SYGCQNSKTL NGLLKTELGF QGYVMTDWGA QHGGIAASNA
GLDMVMPYSS LWNSNLTDAI ANGTMEASRL DDMATRIIAS WYQVNQDAGF PSPGVGMPTD
VYAPHQAIIG KSSDSRKVLL QSAIEGHVLV KNTNNTLPLK SPEMISVFGY DAKGPDSLGF
KLEWFTYSPA IQPNHTLIVG GGSGGNSPAY VSAPLDALQN QVIEDGSAIL WNISAQDPEV
DPNTDACLVF INSYATEGYD RSGLVDEGSD ELVTNVASKC SNTIVTIHNA GIRLVNHWID
HENVTAVIFA HLPGQDSGRA LVELLYGRSN PSGKLPYTVA KKAEDYGALL HPAQPEGQYG
LFPQDDFSEG VYIDYRAFDQ QGIEPQFEFG FGLSYTTFDY SGLNIGPLSD NSTSQYPPSA
AIQEGGNPHL WDVILRVSVD ITNSGPVAGD EVAQLYLGIP NGPVRQLRGF EKVNIPVGET
VTVEFALGRR DLSTWDVVAQ EWLLQSGTYK VYVGRSSRDL PLQGEFTI
//
