ID G2XGJ8_VERDV Unreviewed; 823 AA.
AC G2XGJ8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=VDAG_09280 {ECO:0000313|EMBL:EGY18946.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY18946.1};
RN [1] {ECO:0000313|EMBL:EGY18946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY18946.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) 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; DS572719; EGY18946.1; -; Genomic_DNA.
DR RefSeq; XP_009653877.1; XM_009655582.1.
DR AlphaFoldDB; G2XGJ8; -.
DR STRING; 498257.G2XGJ8; -.
DR EnsemblFungi; EGY18946; EGY18946; VDAG_09280.
DR GeneID; 20710743; -.
DR KEGG; vda:VDAG_09280; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR InParanoid; G2XGJ8; -.
DR OMA; CTDPMGS; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF3; BETA-GLUCOSIDASE B-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.
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 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}.
FT DOMAIN 392..542
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 823 AA; 89294 MW; F1FD6AAE59AD0932 CRC64;
MGRYISQLDV ETVLATLTID EKITLLAGKS FSESADIPLK GIPSIKSVDG PNGVRSAATD
ELIRSACFPA GCSLAATFDP LVARRTGRAL AAEARGKRAH VLLGPTVCIH RHPLGGRNFE
SFSEDPFLAG KMASQYILGL QECGVGATIK HFVANEQETK RTTVDETISE RALREIYLKP
FEIAVREAKP WAVMTAYNHV NGQHCDNHEW LLKTVLRGEW GWKGLVMSDW GGTNSVAAAL
NAGLDLEMPG PPRIRKLQAV KDAVAKGEGD RRRSESDPLE LGVSTDKPEL RSIIRESGAR
GMVLLKNDGV LPLKKEELKG KRVALIGFAK DALAHGGGSA AVNAYYKVTP WDGLRAALGD
DVEFAFAQGA HRERLLAPIN RNGSSGAVLG LDGQPGFTRL LFENGRSEPS KTSHGQTLSA
YSPLGSQESL WRALEIVADF TPLESGSHYI ACSGLGPTKV YVDDKLIWEQ TGNSSDPMGS
LFLAAPEEEF RHHFEGGRKH RLRIRSDPPR KIGLEILEGR SGVRVGFSLE SVHDADLQAE
AVEAAQAADL AVVFTGHDPQ WETEGRDQDS FNLPRGQNEL IAAVAAANRN TVVVNSTGVA
VAMPWLDQVR GLVQAWFPGQ ECGNSIADVL TGAVNPEGRL PMTFPQKIED APAHGNFPGE
YVDGQLKVTY EEGVFVGYRH FDRLTRDKVN FPFGHGLSYT SFEYGAMEVA KTPHDNDRYA
VRVDVKNIGS VEGATLVQVY AGSAQASTDT PIKVLAGFQK VRLQPGEVKR IEIFVSVKDF
ASFDEASKQW VIQGGEYAIS LGETAADILQ TTIVVLAAKQ WKP
//
