ID M1CLM2_SOLTU Unreviewed; 570 AA.
AC M1CLM2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=102583088 {ECO:0000313|EnsemblPlants:PGSC0003DMT400070041};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400070041, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400070041}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400070041};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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};
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DR AlphaFoldDB; M1CLM2; -.
DR EnsemblPlants; PGSC0003DMT400070041; PGSC0003DMT400070041; PGSC0003DMG400027240.
DR Gramene; PGSC0003DMT400070041; PGSC0003DMT400070041; PGSC0003DMG400027240.
DR HOGENOM; CLU_004542_9_3_1; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1CLM2; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 2.
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:SF91; BETA-GLUCOSIDASE; 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 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..570
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004013287"
FT DOMAIN 52..343
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 356..564
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 570 AA; 62486 MW; 5456214932CEC8B4 CRC64;
MQRRSKMGFL MRNFLVLFCW IILAVNAEEY ITYKDPNKPL NRRIKDLMKR MTLEEKIGQM
IQIDRTAATP KVMNKYYLGS VLSGGGSVPK KEASAEDWID MINGFQKGSL STRLGIPMIY
GIDAVHGNNN VYKATIFPHN VALGVIRDPQ LVKRIGSATA LEARATGIPY VFAPCLAVCR
DPRWGRCFES YSEDPNIVRS MSEMVPGLQG DVPSNGRLGV PFVANKQKVA ACAKHYVGDG
GTVKGINENN TIIDRHGLLS IHMAGYYSSI IKGVSTVMVS YSSWNGLRMH ENKEMVTGFL
KGTLRFRGFV ISDWAGIDKL TYPWHTNYTY SILEGVNSGI DMEHRELARE AVRRSLVLLK
NGANADEPVL PLPKKATNIL VAGAHANNMG YQCGGWTITW QGLSGNTTIG TTILSAIENT
VDPETKVVYK ENPDSEFVKS NNFSYAIVVV GETPYAEGSG DTLNLTIPAP GPDIMTTVCA
SVKCVVVLLT GRPVVIQPYL AQMDAVVAAW LPGTEGQGVA DVLFGDYGFT GKLARTWFKT
VDQLPMNVGD SHYDPLFPFG FGLTTEPVKA
//
