ID F9X1Q6_ZYMTI Unreviewed; 631 AA.
AC F9X1Q6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, 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 Name=BTG {ECO:0000313|EMBL:EGP91814.1};
GN ORFNames=MYCGRDRAFT_54587 {ECO:0000313|EMBL:EGP91814.1};
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:EGP91814.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP91814.1, 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; CM001196; EGP91814.1; -; Genomic_DNA.
DR RefSeq; XP_003856838.1; XM_003856790.1.
DR AlphaFoldDB; F9X1Q6; -.
DR STRING; 336722.F9X1Q6; -.
DR EnsemblFungi; Mycgr3T54587; Mycgr3P54587; Mycgr3G54587.
DR GeneID; 13398396; -.
DR KEGG; ztr:MYCGRDRAFT_54587; -.
DR VEuPathDB; FungiDB:ZTRI_1.2109; -.
DR eggNOG; ENOG502QTBT; Eukaryota.
DR HOGENOM; CLU_004542_8_2_1; -.
DR InParanoid; F9X1Q6; -.
DR OMA; STDQEHG; -.
DR OrthoDB; 2657687at2759; -.
DR Proteomes; UP000008062; Chromosome 1.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 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 PANTHER; PTHR30620:SF120; BETA-GLUCOSIDASE C; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..631
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003389943"
FT DOMAIN 67..414
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
SQ SEQUENCE 631 AA; 69100 MW; 5AE5C8E5698D3596 CRC64;
MSFYTGRKAF LATLLVTASF TGADSAVAPH LTSRQTNAAT GEVLPYRNAT LCIDERLDDL
LSRMTVAEKA GQLFHASITM GKNGTLAEAT SYRNSSAMEI GEKLMSHFNY GGDVENVREV
AEWHNLLQRT ALETRLGIPI SISSDPRHSF TENIGTGFAA KSLSQWPESL GLAALRDPAW
TLKFAEIARE EYMALGLRGA LHPQVDLSTE YRWARIANTM GEDANLTSQL VAAYIKGFQG
EELGRNSVTT VTKHFPGAGP MENGEDSHFT YGKNQTYPGH NFEHHLIPFK AAIAAGARQM
MPYYSRPIGT QYEEVAFSFN KGIITDLLRN ELGFEGIVVS DWGLITDTVI AGQDMPARAW
GVEQLSELDR AARVLGAGVD QFGGEQRTEL IVELVENDSV SEERIDVSVR RLLREKFILG
LFDNPFIDVD QAEQIVGNPY FVRLGAEAQR ASYTLLKNEN NLLPIKNPAG MKIYVDGFNT
TYLDGRDVTL VDTPEEAELA IVRLQAPFEP RPGGFESMYT AGSLEFNATE KARQAAIYSA
VPTVVDIKLG RPAAIPEIAE QAAALFGNYG ASPEALLNII FNVQGAKPLG KLPFDLPRSD
AAVEASKEDV PFDTVDPVFR FGDGLAYAED C
//
