ID   PME_CAPCH               Reviewed;          22 AA.
AC   P86085;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Pectinesterase {ECO:0000250|UniProtKB:P83218};
DE            Short=PE {ECO:0000250|UniProtKB:P83218};
DE            EC=3.1.1.11;
DE   AltName: Full=Pectin methylesterase {ECO:0000250|UniProtKB:P83218};
DE   Flags: Fragments;
OS   Capsicum chinense (Scotch bonnet) (Bonnet pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=80379;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Almagro L., Sabater Jara A.B., Pedreno M.A.;
RL   Submitted (JUL-2008) to UniProtKB.
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:0000250|UniProtKB:P83218};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P83218}.
CC   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000255}.
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DR   AlphaFoldDB; P86085; -.
DR   UniPathway; UPA00545; UER00823.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Hydrolase; Secreted.
FT   CHAIN           <1..>22
FT                   /note="Pectinesterase"
FT                   /id="PRO_0000362164"
FT   ACT_SITE        6
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P83218,
FT                   ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P83218"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P83218"
FT   SITE            5
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P83218"
FT   UNSURE          1
FT                   /note="I or L"
FT   UNSURE          4
FT                   /note="F or M"
FT   UNSURE          5
FT                   /note="Q or K"
FT   UNSURE          8
FT                   /note="L or I"
FT   UNSURE          13
FT                   /note="L or I"
FT   UNSURE          17
FT                   /note="L or I"
FT   UNSURE          22
FT                   /note="K or Q"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         22
SQ   SEQUENCE   22 AA;  2696 MW;  E7FC592B7685048D CRC64;
     IDAFQDTLYT HTLRTYLGRP WK