ID K2QZD2_MACPH Unreviewed; 737 AA.
AC K2QZD2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=MPH_07402 {ECO:0000313|EMBL:EKG15351.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG15351.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG15351.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG15351.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:EKG15351.1}.
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DR EMBL; AHHD01000300; EKG15351.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QZD2; -.
DR STRING; 1126212.K2QZD2; -.
DR VEuPathDB; FungiDB:MPH_07402; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR InParanoid; K2QZD2; -.
DR OrthoDB; 2783936at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF29; BETA-GLUCOSIDASE L-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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 657..726
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 737 AA; 77685 MW; C760A5605E4B32D3 CRC64;
MRGPIAFAVA AAAVSNAQTS HTPTVDWTAA YDKATSALAQ INQTEKVGIV TGVGWGNGPC
VGNTYPVPKI GYPSLCLQDG PLGVRYASNV SAFPAGIQAA ATWDRELIYQ RGLALGKEAK
GLGVNVQLGP VSGALGKIPE AGRNWEGFSP DPYLAGICMF ETIVGMQEGG VQACAKHYLL
NEQELNRTTI SANADDRTTH ELYLWPFADA VKAGVTSFMC SYNKLNGTWA CENDKILNGL
LKDELDYKGF VMTDWGAHHT TVDSAIAGLD MSMPGTDYGK SPESLYWGAN LTAAVEAGDI
PQERLDDMVL RILAAWYALG QDDPAFPAVQ FDSWVDGEKG GYEAPQTQHN ELARAVARDG
IVLLKNENAT LPIKPTSGSL AIIGDDARVN PAGPNACSDR ACTNGTLAVG WGSGANEFPY
LIAPLDAIRE RASAAGTTII ASPTDDQAAG ASAAAAAETA IVFIVSNSGE EYLTVENNVG
DRINLDPWHD GNGLVAAVAE AAAGKPVVVV AHSVGPIILE SILSHENVVA LVWAGLGGQE
QGNALADVLF GDVSPSGKLP YTIAKAAEDY GTKLVGPDVD DEFEEGLYID YRHFDKAGIE
PRYEFGFGLS YTNFTYSDIA ITKTAASNAT AGSTDLYAPF ATVTATIANS GDVAGAEVAQ
LYLSLPAGID APPKQLRGFE KISLEAGASA SVEFVLRRKD ASYWNVERQQ WILPTGDFGI
AVAASSRDLR LEGTLTV
//
