PME1_FICPW
ID PME1_FICPW Reviewed; 545 AA.
AC P83947;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Pectinesterase/pectinesterase inhibitor;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor;
DE AltName: Full=Pectin methylesterase inhibitor;
DE Includes:
DE RecName: Full=Pectinesterase;
DE Short=PE;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase;
DE Flags: Precursor;
OS Ficus pumila var. awkeotsang (Jelly fig) (Ficus awkeotsang).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Ficus.
OX NCBI_TaxID=204231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 229-239.
RC TISSUE=Pericarp;
RX PubMed=10898664; DOI=10.1021/jf000273d;
RA Ding J.L.C., Lee T.T.T., Wang M.M.C., Tai S.S.K., Tzen J.T.C.;
RT "Cloning and expression of an acidic pectin methylesterase from jelly fig
RT (Ficus awkeotsang).";
RL J. Agric. Food Chem. 48:3052-3057(2000).
RN [2]
RP PROTEIN SEQUENCE OF 229-256, AND CATALYTIC ACTIVITY.
RC TISSUE=Pericarp;
RX PubMed=16667199; DOI=10.1104/pp.91.4.1445;
RA Lin T.-P., Liu C.-C., Chen S.-W., Wang W.-Y.;
RT "Purification and characterization of pectinmethylesterase from Ficus
RT awkeotsang makino achenes.";
RL Plant Physiol. 91:1445-1453(1989).
RN [3]
RP CATALYTIC ACTIVITY, AND GLYCOSYLATION.
RC TISSUE=Pericarp;
RX PubMed=11982420; DOI=10.1021/jf010845+;
RA Ding J.L.C., Hsu J.S.F., Wang M.M.C., Tzen J.T.C.;
RT "Purification and glycosylation analysis of an acidic pectin methylesterase
RT in jelly fig (Ficus awkeotsang) achenes.";
RL J. Agric. Food Chem. 50:2920-2925(2002).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
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:11982420, ECO:0000269|PubMed:16667199};
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11982420}.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC prevent untimely PME activity during transport.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P83947; -.
DR SMR; P83947; -.
DR iPTMnet; P83947; -.
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:0004857; F:enzyme inhibitor activity; IEA:InterPro.
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; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
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; IPR006501; Pectinesterase_inhib_dom.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Secreted; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT PROPEP 38..228
FT /evidence="ECO:0000269|PubMed:10898664,
FT ECO:0000269|PubMed:16667199"
FT /id="PRO_0000023484"
FT CHAIN 229..545
FT /note="Pectinesterase/pectinesterase inhibitor"
FT /id="PRO_0000023485"
FT REGION 38..191
FT /note="Pectinesterase inhibitor"
FT REGION 232..530
FT /note="Pectinesterase"
FT ACT_SITE 360
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 381
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 307
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 359
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:11982420"
FT DISULFID 326..353
FT /evidence="ECO:0000250"
FT DISULFID 394..428
FT /evidence="ECO:0000250"
FT CONFLICT 249
FT /note="A -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 60602 MW; CF7B40DF36655D93 CRC64;
MEINQPNLLE ASKSCYSKIT FFLLVISFAA LVSTGFSSPE LSLHHKICDQ SVNKESCLAM
ISEVTGLNMA DHRNLLKSFL EKTTPRIQKA FETANDASRR INNPQERTAL LDCAELMDLS
KERVVDSISI LFHQNLTTRS HEDLHVWLSG VLTNHVTCLD GLEEGSTDYI KTLMESHLNE
LILRARTSLA IFVTLFPAKS NVIEPVTGNF PTWVTAGDRR LLQTLGKDIE PDIVVAKDGS
GDYETLNEAV AAIPDNSKKR VIVLVRTGIY EENVDFGYQK KNVMLVGEGM DYTIITGSRN
VVDGSTTFDS ATVAAVGDGF IAQDICFQNT AGPEKYQAVA LRIGADETVI NRCRIDAYQD
TLYPHNYRQF YRDRNITGTV DFIFGNAAVV FQNCNLIPRK QMKGQENTIT AQGRTDPNQN
TGTSIQNCEI FASADLEPVE DTFKSYLGRP WKEYSRTVVM ESYISDVIDP AGWLEWDRDF
ALKTLFYGEY RNGGPGSGTS ERVKWPGYHV ITSPEVAEQF TVAELIQGGS WLGSTGVDYT
AGLYA
