ID F9X9Y9_ZYMTI Unreviewed; 774 AA.
AC F9X9Y9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=MgBGL1 {ECO:0000313|EMBL:EGP87784.1};
GN ORFNames=MYCGRDRAFT_85505 {ECO:0000313|EMBL:EGP87784.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87784.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP87784.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(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; CM001199; EGP87784.1; -; Genomic_DNA.
DR RefSeq; XP_003852808.1; XM_003852760.1.
DR AlphaFoldDB; F9X9Y9; -.
DR STRING; 336722.F9X9Y9; -.
DR EnsemblFungi; Mycgr3T85505; Mycgr3P85505; Mycgr3G85505.
DR GeneID; 13397129; -.
DR KEGG; ztr:MYCGRDRAFT_85505; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR InParanoid; F9X9Y9; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000008062; Chromosome 4.
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: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 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:UP000008062};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..774
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003395560"
FT DOMAIN 696..762
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 774 AA; 84329 MW; 16AF0CED82071F0A CRC64;
MKSPTLILLQ AGALLLQVPS VDAIAYTNVS EIPLCGQSPP VYPTPQGTGG PSSAWRNSYA
SALALVNQLT LEEKVNLTRG HVGTCVGNTP AVPRLGIRSL CFSDAPSGIR GQEFVSSFPA
QLTVGATFDK ELMLAYGEAL GEEYHGKGIN IALLPVAGPL GRTARGGRNW EGFGADHYLS
GVGMGLVTRG LQSKGVIAQM KHWLLNEQEW RRLPREDLGE SVSTNADDRT IWEGYVWPFM
DALREGCGSA MCSYQRINNS YGCQNSKLLN GILKTDLGFQ GFVTSDWNAQ HAGVASANAG
LDLVMPDGGY WGDNLTEAVT NGSVSSTRLD DMVTRILATW YHFNQDDVAA FPDPSVFNYD
TQHPIVDVRG DHAAVIREIA AAGTVLVKNV DKALPLKAPR FLNIYGYDAT IPTAPWNTSA
RFGGGYDVNF GWNTFDGTLI TAGGSGSNTP SGLVSPFEAI QRRVQADRGT TRWDFVNVQP
TVYASADASI VFINAYASES FDRTTLADEW SDQLVNNVAA KHNNTIVVIH SAGIRLVDRW
IEHPNVTAVV FALLPGEQSG NSIVDVLYGD VVPSGRLPFT VAKKEEDYGN LLNSSGTALP
DPFPQIDFTE GLHVDYKYFD QQNLDVRFEF GYGLSYTEFE YGSTVEVVAV GDGPKDEYPA
HLAPEDIPQG GSPKLWEVVY NVTFSIKNIG DVEAAEVPQL YLAVPNAPKW QLRGFEKTFL
RCGEEKQVTL GLTRRDLSIW DVVAQNWRMQ KGTYGLFVGA SSRDKRIEGH LVVE
//