BGLC_OLEEU
ID BGLC_OLEEU Reviewed; 551 AA.
AC Q8GVD0; V5RMD5;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Oleuropein beta-glucosidase {ECO:0000305};
DE EC=3.2.1.206 {ECO:0000269|PubMed:25697790};
DE AltName: Full=Beta-glucosidase {ECO:0000303|PubMed:25697790};
DE Short=OeGLU {ECO:0000303|PubMed:25697790};
GN Name=GLU {ECO:0000303|PubMed:25697790}; Synonyms=BGLC {ECO:0000303|Ref.1};
OS Olea europaea (Common olive).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX NCBI_TaxID=4146;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Koroneiki;
RA Gazis F., Hatzopoulos P.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Ayvalik;
RA Deniz Sonmez G., Dundar E.;
RT "Full length nucleotide sequence of Olea europaea cv Ayvalik beta
RT glucosidase gene.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND SUBUNIT.
RX PubMed=25697790; DOI=10.1093/jxb/erv002;
RA Koudounas K., Banilas G., Michaelidis C., Demoliou C., Rigas S.,
RA Hatzopoulos P.;
RT "A defence-related Olea europaea beta-glucosidase hydrolyses and activates
RT oleuropein into a potent protein cross-linking agent.";
RL J. Exp. Bot. 66:2093-2106(2015).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP 543-LYS--THR-551, SUBUNIT, AND FUNCTION.
RX PubMed=28483880; DOI=10.1104/pp.17.00512;
RA Koudounas K., Thomopoulou M., Michaelidis C., Zevgiti E., Papakostas G.,
RA Tserou P., Daras G., Hatzopoulos P.;
RT "The C-domain of oleuropein beta-glucosidase assists in protein folding and
RT sequesters the enzyme in nucleus.";
RL Plant Physiol. 174:1371-1383(2017).
CC -!- FUNCTION: Major beta-glucosidase activating oleuropein into a potent
CC protein cross-linking agent (PubMed:25697790, PubMed:28483880). No
CC activity with rutin, luteolin or p-nitrophenyl-beta-glucopyranoside as
CC substrates (PubMed:25697790). {ECO:0000269|PubMed:25697790,
CC ECO:0000269|PubMed:28483880}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + oleuropein = D-glucose + oleuropein aglycone;
CC Xref=Rhea:RHEA:55740, ChEBI:CHEBI:4167, ChEBI:CHEBI:7747,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:139162; EC=3.2.1.206;
CC Evidence={ECO:0000269|PubMed:25697790};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.48 mM for oleuropein {ECO:0000269|PubMed:28483880};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:28483880};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:28483880};
CC -!- SUBUNIT: Homomultimer. Native form of the enzyme requires at least an
CC octamer conformation. {ECO:0000269|PubMed:28483880}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28483880}.
CC Note=Distinctive compartmentalization of the oleuropein/OeGLU dual
CC partner is a requisite to ensure a correct defense system response and
CC to prevent the autotoxicity. {ECO:0000269|PubMed:28483880}.
CC -!- TISSUE SPECIFICITY: Expressed in expanding leaves and in young drupes,
CC mostly in the developing seed coat tissues, the perisperm and the
CC mesocarp. Also detected in shoot and root meristems, flower buds,
CC developing ovaries and tapetal cells of the anther. Not detected in
CC embryos or endosperm, or in leaf trichomes.
CC {ECO:0000269|PubMed:25697790}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing mesocarp from 13 weeks
CC after flowering until veraison, when the color of drupes turned from
CC green to black. {ECO:0000269|PubMed:25697790}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000255|RuleBase:RU003690}.
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DR EMBL; AY083162; AAL93619.1; -; mRNA.
DR EMBL; KF623043; AHB37683.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GVD0; -.
DR SMR; Q8GVD0; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ag:AAL93619; -.
DR BRENDA; 3.2.1.206; 4398.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Nucleus; Plant defense.
FT CHAIN 1..551
FT /note="Oleuropein beta-glucosidase"
FT /id="PRO_0000433019"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..551
FT /note="Required for the homomultimerization"
FT /evidence="ECO:0000269|PubMed:28483880"
FT REGION 532..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 542..550
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:28483880"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT ACT_SITE 433
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GU20"
FT BINDING 201..205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 433
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 489..490
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT SITE 405
FT /note="Controls the gate shape and acceptance of
FT substrates"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT MUTAGEN 543..551
FT /note="Missing: Delocalization from the nucleus to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:28483880"
SQ SEQUENCE 551 AA; 62894 MW; 3274FF1162F71ABF CRC64;
MDIQSNVLTI TSGSTPTDTS SNGQAAKSTK ERIKRSDFPS DFVFGAATAS YQVEGAWNEG
GKGMSNWDYF TQSQPGGISD FSNGTIAIDH YNMFKDDVVV MKKLGLKAYR FSLSWPRILP
GGRLCHGVSK EGVQFYNDLI DALLAADIEP YITIFHWDIP QCLQLEYGGF LHERVVKDFI
EYSEICFWEF GDRVKYWITL NEPWSFTVQG YVAGAFPPNR GVTPKDTEET QKHARLHRGG
GKLLAAFKYG NPGTEPYKVA HNLILCHAHA VDIYRTKYQE SQGGKIGITN CISWNEPLTD
SQEDKDAATR GNDFMLGWFV EPVVTGEYPE SMIKYVGDRL PKFSEKEEKL VKGSYDFLGI
NYYTSTYTSD DPTKPTTDSY FTDSHTKTSH ERNKVPIGAQ AGSDWLYIVP WGIYRVMVDM
KKRYNDPVIY ITENGVDEVN DKSKTSTEAL KDDIRIHYHQ EHLYYLKLAM DQGVNVKGYF
IWSLFDNFEW AAGFSVRFGV MYVDYANGRY TRLPKRSAVW WRNFLTKPTA VPLKNEPEKS
EDRRKRLRGS T
