ID   PME_PETIN               Reviewed;         374 AA.
AC   Q43043;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Pectinesterase;
DE            Short=PE;
DE            EC=3.1.1.11;
DE   AltName: Full=Pectin methylesterase;
DE   Flags: Precursor;
GN   Name=PPE1;
OS   Petunia integrifolia (Violet-flowered petunia) (Salpiglossis integrifolia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Pollen;
RX   PubMed=8049376; DOI=10.1007/bf00043881;
RA   Mu J.H., Stains J., Kao T.H.;
RT   "Characterization of a pollen-expressed gene encoding a putative pectin
RT   esterase of Petunia inflata.";
RL   Plant Mol. Biol. 25:539-544(1994).
CC   -!- FUNCTION: May play a role in pollen germination and/or tube growth.
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   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Pollen, and at much lower levels in pistils and
CC       petals.
CC   -!- DEVELOPMENTAL STAGE: Appears first in early bicellular pollen, peaking
CC       in mature pollen.
CC   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR   EMBL; L27101; AAA33714.1; -; Genomic_DNA.
DR   PIR; S78041; S78041.
DR   AlphaFoldDB; Q43043; -.
DR   SMR; Q43043; -.
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: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   InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00800; PECTINESTERASE_1; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW   Disulfide bond; Glycoprotein; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..374
FT                   /note="Pectinesterase"
FT                   /id="PRO_0000023495"
FT   ACT_SITE        186
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   ACT_SITE        207
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            185
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        200..220
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  41467 MW;  BC52DC4501B57490 CRC64;
     MVKLLNSTRE LSINALSMLN SFGDMVAQAT GLNRKLLTTD SSDATARRLL QISNAKPNAT
     VALDGSGQYK TIKEALDAVP KKNTEPFIIF IKAGVYKEYI DIPKSMTNVV LIGEGPTKTK
     ITGNKSVKDG PSTFHTTTVG VNGANFVAKN IGFENTAGPE KEQAVALRVS ADKAIIYNCQ
     IDGYQDTLYV HTYRQFYRDC TITGTVDFIF GNGEAVLQNC KVIVRKPAQN QSCMVTAQGR
     TEPIQKGAIV LQNCEIKPDT DYFSLSPPSK TYLGRPWKEY SRTIIMQSYI DKFIEPEGWA
     PWNITNFGRD TSYYAEYQNR GPGAALDKRI TWKGFQKGFT GEAAQKFTAG VYINNDENWL
     QKANVPYEAG MMKV