ID A0A1B8AK28_FUSPO Unreviewed; 813 AA.
AC A0A1B8AK28;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=FPOA_07040 {ECO:0000313|EMBL:OBS20701.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS20701.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS20701.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS20701.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:OBS20701.1}.
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DR EMBL; LYXU01000003; OBS20701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8AK28; -.
DR STRING; 36050.A0A1B8AK28; -.
DR OMA; YERGYAM; -.
DR Proteomes; UP000091967; 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: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 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:SF19; BETA-GLUCOSIDASE G-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 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:UP000091967};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..813
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008602941"
FT DOMAIN 728..799
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 813 AA; 88451 MW; EB4FEBC3B194CF5A CRC64;
MASLRSVLVS GLLAASVNAQ DFGGNDRSEE AFSWVQPKNT TILGQYGHSP EFPSTYATGK
GWEQGFAKAK EFVSKLTLEE KADMVTGTPG PCVGNIIAIP RLGFNGLCLH DGPLAIRVAD
YASVFPAGVS AASSWDKELL YQRGLAMGQE FKAKGAHVLL GPVAGPLGRS AYSGRNWEGF
SPDPYLTGVA MEHTINGHQD AGVQATAKHF IGNEQEVMRN PTFKKDGYVG EVDEEALSSN
MDDRTMHELY LWPFANAAHA KAASFMCSYQ RLNGSYGCQN SKILNGILRD ELGFQGYVMS
DWGATHAGVA AINSGLDMDM PGGIGAYGMN WKAGSFFGGN LTNAVTNGTL EEARVDDMIM
RIMAPYFWLG QDSEEFPSVD ESSGDLNTFS PRKTWLKEFN FTGERSRDVR GDHGDLIRKH
GAETTVLLKN ENNALPLKKP KSIAVFGNDA GDITEGFLNQ KDYEFGTLVA GGGSGTGRLT
YLVSPLTAIN ARAKQDGTLV QQWLNNTLIA QSNVTDLWIP AVPDVCLVFL KTWAEEGGDR
GHLSVDWDGD DVVKSVAKSC NNTIVVTHSS GINTLPWADH PNVTAILAAH FPGQESGNSL
VDLLYGDVNP SGRLPYTIAL NGTDYNAPPT TAINTTGTDD WQSWFDEKLE IDYRYFDAKN
MSVRYEFGFG LSYSTFEISD ISAEPLADDI TAMPEALPVQ PGGNPALWET IYNVTVSVTN
SGKVDGATVP QLYVTFPESA PKGTPPKQLR GFEKVFLEAG ESKNVSFELM RRDLSYWDII
SQQWVIPEGE FTIRVGFSSR DLKEETKVTL VEA
//
