ID K2RU31_MACPH Unreviewed; 862 AA.
AC K2RU31;
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|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=MPH_04435 {ECO:0000313|EMBL:EKG18303.1};
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:EKG18303.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG18303.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG18303.1,
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 -!- 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:EKG18303.1}.
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DR EMBL; AHHD01000210; EKG18303.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RU31; -.
DR STRING; 1126212.K2RU31; -.
DR VEuPathDB; FungiDB:MPH_04435; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR InParanoid; K2RU31; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:SF10; BETA-GLUCOSIDASE F-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 Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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 765..839
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 862 AA; 91835 MW; 96B10A63DBAF0044 CRC64;
MSAAAADNQT TPSTRLAVPD GYVAAPAYPA PYGGWVEEWS ASYAKAAELV SQMTLAEKTN
ITTGTGYFMG RCVGNTGSAL RLGFPQLCLQ DSALGVKGTD NVTAFPPGIT VGATWNKDLM
YARGVAIGQE FRGKGVNIYL GPTVGPLGRK PRGGRNWEGF GADPVLQAVG GALTIQAVQE
QGVMATIKHF IGNEQESYRM YNPFQPGISS NIDDRTMHEL YLWPFAEGIR AGVTSVMTAY
NAVNGSACAQ NSYNINHLLK DELGFQGFTM SDWLSQISGA ASALAGLDMT MPGDPTVPLF
GDAWWAFHLT EAALNGSVPM DRIDDMTTRI VAAWYQMGQD QEYPDPNFST WTTDATGLLY
PGALFSPSGV VNEFVNVQAD HAAVARTVSM EAVTLLKNEN GTLPLSESTP LKVFGSAAEE
NPDGINSCSD KSCNKGTLGM GWGSGTANYP YIDSPIEALT RRAQNVTSYL TDSFPSNAVV
ADGDVALVFI TSDSGENYLS VEGNPGDRTA SGLNAWHNGD KLVQDAAAKY DTVVVIVQTV
GPILLEEWID LPSVKAVLFQ HLPGQEAGES LTSVLFGDES PSGHLPYSIP RAEDDLPASV
GIVGFELGQP QDTFSEGLYI DYRYLNAHNT TPRYPFGHGL SYTTFNYSAT ITPGIALTSS
PPARPPKGAT PAYNTTIPDP AEAVGPPAGF DKIWRYIYSW LSESDAEAAY AKRNTTTYPY
PEGYSETQTP GVPAGGAQGG NPALWDTAFN VTATITNTGV APGKAVAQAY VQFPSGIAWD
TPVIQLRDFA KTGTLQPGES AEVVLTITRK DLSVWDVVSQ NWVVPDVEGE YRIWVGESSG
TLELACSTTG LECESGLESP VA
//
