ID A0A022PVA7_ERYGU Unreviewed; 638 AA.
AC A0A022PVA7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=MIMGU_mgv1a002782mg {ECO:0000313|EMBL:EYU18175.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU18175.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU18175.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI632337; EYU18175.1; -; Genomic_DNA.
DR RefSeq; XP_012828672.1; XM_012973218.1.
DR AlphaFoldDB; A0A022PVA7; -.
DR STRING; 4155.A0A022PVA7; -.
DR GeneID; 105949914; -.
DR KEGG; egt:105949914; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR OMA; TTKVVYN; -.
DR OrthoDB; 1208905at2759; -.
DR PhylomeDB; A0A022PVA7; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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: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:UP000030748};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..638
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001506318"
FT DOMAIN 59..387
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 424..632
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 638 AA; 69389 MW; E86964B590091588 CRC64;
MQANSSPNYK MAKRQSFVVA LLVSCCLLAA ADAAEYKALY KDPKMPINRR IKDLLARMTL
EEKIGQMVQI ERTVASRDVI NKYYIGSVLG GGGSAPSPKA PPEKWVDMVN NFQNGALSTR
LGIPMIYGID AVHGHNGVYK ATVFPHNIGL GATRDPELVK KIGAATALEL RATGIPYTFA
PCVAVCRDPR WGRCYESYSE DTSVVRAMTE IIPGLQGDIP ANSTKGVPYI SGKEKVVACA
KHYVGDGGTT KGINQNDTVI SNRGLLSIHM PPYNDSIVKG VATIMISYSS FNGVKMHANR
DLITGYLKNT LRFRGFVISD FEGIDHITTP PHANYTYSIL AGVGAGIDMI MIPYNYTEFI
DGLTFLVKKK FIPMSRIDDA VIRILRVKFT MGLFENPLAD YSMTKYLGSQ EHRELAREAV
RKSLVLLKNG KSSDKPLIPL PKKASKVLVA GTHADDIGNQ CGGWTIQWQG QSGNITFGTT
ILNAVKNAVD PTMEVVFVEK PDIEYVKSNE FSYAIVVVGE SPYAEGYGDN LNLTLPESGY
STITNVCGSV KCVVVLITGR PIVIGPYLGQ IDGLVAAWLP GTEGQGVADV LFGDYGFSGK
LSRTWFKSVD QLPMNVGDPH YDPLFPFGFG LTTKGVKG
//
