ID   PME_ACTDE               Reviewed;         321 AA.
AC   P85076;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   02-SEP-2026, entry version 59.
DE   RecName: Full=Pectinesterase;
DE            Short=PE;
DE            EC=3.1.1.11;
DE   AltName: Full=Pectin methylesterase;
OS   Actinidia deliciosa (Kiwi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Actinidiaceae; Actinidia.
OX   NCBI_TaxID=3627;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, GLYCOSYLATION AT
RP   ASN-75; ASN-275; ASN-290 AND ASN-319, AND ACETYLATION AT THR-1.
RC   TISSUE=Fruit {ECO:0000269|PubMed:17932919};
RX   PubMed=17932919; DOI=10.1002/prot.21681;
RA   Ciardiello M.A., D'Avino R., Amoresano A., Tuppo L., Carpentieri A.,
RA   Carratore V., Tamburrini M., Giovane A., Pucci P., Camardella L.;
RT   "The peculiar structural features of kiwi fruit pectin methylesterase:
RT   Amino acid sequence, oligosaccharides structure, and modeling of the
RT   interaction with its natural proteinaceous inhibitor.";
RL   Proteins 71:195-206(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC         [(1->4)-alpha-D-galacturonosyl](n) + n methanol + n H(+);
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:17932919};
CC   -!- ACTIVITY REGULATION: Inhibited by PMEI. {ECO:0000269|PubMed:17932919}.
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5.
CC   -!- PTM: The N-glycans attached at Asn-75, Asn-275, Asn-290 and Asn-319 are
CC       complex oligosaccharides containing xylose, fucose, hexose and N-
CC       acetylglucosamine.
CC   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000255}.
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DR   AlphaFoldDB; P85076; -.
DR   SMR; P85076; -.
DR   Allergome; 3547; Act d 7.
DR   Allergome; 3976; Act d 7.0101.
DR   iPTMnet; P85076; -.
DR   BRENDA; 3.1.1.11; 121.
DR   UniPathway; UPA00545; UER00823.
DR   GO; GO:0030599; F:pectinesterase activity; EXP:UniProtKB.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   FunFam; 2.160.20.10:FF:000001; Pectinesterase; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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   PANTHER; PTHR31707; PECTINESTERASE; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aspartyl esterase; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase.
FT   CHAIN           1..321
FT                   /note="Pectinesterase"
FT                   /id="PRO_0000311723"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   ACT_SITE        158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            19
FT                   /note="Not glycosylated"
FT   SITE            136
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|PubMed:17932919"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17932919"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17932919"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17932919"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17932919"
FT   DISULFID        151..171
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  35368 MW;  26CEC95A8071C04D CRC64;
     TAVTDIVPDV VVAKDGSGNF TTVGAAVAAA KDSSTARFVI YIKEGAYFEY VDVDKKKTNL
     MFIGDGIGKT WIKGNRSVVD GWTTFRSSTV AVVGTGFIAR GISFENYAGP SKHQAVALRS
     GADFSAFYQC SFVGYQDTLY VHSLRQFYSE CDVYGTIDFI FGNAAAVLQK CNLYARKPNE
     NQKNIFTAQG RDDPNQNTGI SILNCKVAAA ADLIPVLSSF KTYLGRPWKE YSRTVFLLSQ
     MESLIDPAGW LEWSGDFALT TLYYREYKNT GPGSNTTARV TWPGYAVTTN ETEVIQFTVG
     NFIQGSQWLT SYNIPVYLNL T
//