AL11A_OLEEU
ID AL11A_OLEEU Reviewed; 364 AA.
AC D8VPP5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Pectinesterase 1;
DE EC=3.1.1.11;
DE AltName: Full=Pollen allergen Ole e 11.0101;
DE Short=Ole e 11-1;
DE AltName: Allergen=Ole e 11.0101;
DE Flags: Precursor;
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], PROTEIN SEQUENCE OF 267-276 AND 354-359,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION
RP AT ASN-103, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pollen;
RX PubMed=20491902; DOI=10.1111/j.1742-4658.2010.07689.x;
RA Salamanca G., Rodriguez R., Quiralte J., Moreno C., Pascual C.Y.,
RA Barber D., Villalba M.;
RT "Pectin methylesterases of pollen tissue, a major allergen in olive tree.";
RL FEBS J. 277:2729-2739(2010).
RN [2]
RP 3D-STRUCTURE MODELING.
RX PubMed=22722698; DOI=10.1007/s00894-012-1492-2;
RA Jimenez-Lopez J.C., Kotchoni S.O., Rodriguez-Garcia M.I., Alche J.D.;
RT "Structure and functional features of olive pollen pectin methylesterase
RT using homology modeling and molecular docking methods.";
RL J. Mol. Model. 18:4965-4984(2012).
RN [3]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=22385802; DOI=10.1016/j.talanta.2012.01.016;
RA Esteve C., Montealegre C., Marina M.L., Garcia M.C.;
RT "Analysis of olive allergens.";
RL Talanta 92:1-14(2012).
CC -!- FUNCTION: Catalyzes the demethylesterification of homogalacturonan
CC components of pectin. May be involved in pollen tube development.
CC {ECO:0000269|PubMed:20491902}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC Evidence={ECO:0000269|PubMed:20491902};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:20491902};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20491902}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen. {ECO:0000269|PubMed:20491902}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:20491902}.
CC -!- POLYMORPHISM: Several isoforms of the allergen exist due to
CC polymorphism.
CC -!- ALLERGEN: Causes an allergic reaction in human. Allergen from olive
CC pollen. Important in Mediterranean countries and California. Its
CC prevalence is related to the geographic area.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; GU084173; ACZ57582.1; -; mRNA.
DR AlphaFoldDB; D8VPP5; -.
DR SMR; D8VPP5; -.
DR Allergome; 5966; Ole e 11.
DR Allergome; 8716; Ole e 11.0101.
DR iPTMnet; D8VPP5; -.
DR BRENDA; 3.1.1.11; 4398.
DR UniPathway; UPA00545; UER00823.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW Allergen; Aspartyl esterase; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..22
FT CHAIN 23..364
FT /note="Pectinesterase 1"
FT /id="PRO_0000421083"
FT ACT_SITE 220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20491902"
SQ SEQUENCE 364 AA; 39667 MW; EE0B77A896D62F12 CRC64;
MSCIAVEAVL LGILLYIPIV LSDDRAPIPS NSAQLNSWFD GIIQPVAVRK ATMDPALVTA
EGQTKVIKLK SDGSGDFKSI NEAIKSIPDD NTKRVILSLA PGNYSEKVKI GMYKHYITFY
GEDPNNMPIL VFGGTAAEYG TVDSATLIVE SNYFSAVNLK IVNSAPRPDG KRVGAQAAAL
RISGDKASFY NVKIYGFQDT LCDDKGKHFY KDCYIEGTVD FIFGSGKSIF LNTELHAVPG
DQPAIITAQA RKTDSEDTGY YFVNCRVTGG GAFLGRSWMP AAKVVFAYTE MVDAIHPEGW
ILVKPEHEST VRFSEYNNKG PGANMEKRAK FVKRLSDAEA KQSISLGSIE ASKWLLPPRV
VGLP
