ID K2QP39_MACPH Unreviewed; 634 AA.
AC K2QP39;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=MPH_11194 {ECO:0000313|EMBL:EKG11701.1};
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:EKG11701.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG11701.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG11701.1,
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 -!- 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:EKG11701.1}.
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DR EMBL; AHHD01000467; EKG11701.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QP39; -.
DR STRING; 1126212.K2QP39; -.
DR VEuPathDB; FungiDB:MPH_11194; -.
DR eggNOG; ENOG502QTBT; Eukaryota.
DR HOGENOM; CLU_004542_8_2_1; -.
DR InParanoid; K2QP39; -.
DR OrthoDB; 2657687at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
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 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 PANTHER; PTHR30620:SF120; BETA-GLUCOSIDASE C; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EKG11701.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..634
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003867164"
FT DOMAIN 68..417
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 493..630
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 634 AA; 69670 MW; 59C6D64728CB71A9 CRC64;
MRTPVLHTST TKPQGSWASI FVAALASISA VSARALPRGA AQNETVPAYR NPTLCIDERL
DDLIQRMTLE EKAGQLFIKQ IPMGTNGTID IETKTDNYTS ADLISQKLMS HFNLQSSGKA
SDIANWHNSI QELALQTRLG IPITIATDPR HSFAETAGSA VGVGSFSQWP ETLGLAALRS
PELVQRFAEI AREEYMAVGI RSALSPQIDV TTEPRWARSG QTYGEDANLT SSLVVGYLKG
FQGETLGRHS VTTVTKHFPG GGPGQNGNDS HFETGKNNVY PGGYFDYHLE PFRAAIAAGA
RQMMPSYARP IGTKYEEVAM GFNKGIVTDL LRDELGFDGI VVSDWGLVTN FTARGEEMEA
ISWGVENLSE IEKVEKILNA GVDQLGGEIR TELVIQLVNE GAISEERIDV SVRRLLREKF
VLGLFDNPFV DPDAADAIVG NDYFRRVGNE TQRRAYTLLK NDDDLLPLTL DADTKFYADG
FNASYLLERG LAVVDTPEEA DYAFLRLSTP YEARGGGFER NYHQGRLDFN ETEKARHAAI
TQTVPTIVDI YLDRPAVIPE LAEDSAALLG NYGASVDAFL DIVFGTEGWK PEGKLPFDLP
RSMEAVEANK EDVPFDTENP VFRYGHGLSY AEKC
//