PMEU1_SOLLC
ID PMEU1_SOLLC Reviewed; 583 AA.
AC Q43143;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Pectinesterase/pectinesterase inhibitor U1;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor U1;
DE AltName: Full=Pectin methylesterase inhibitor U1;
DE Includes:
DE RecName: Full=Pectinesterase U1;
DE Short=PE U1;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase U1;
DE Flags: Precursor;
GN Name=PMEU1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Rio Grande; TISSUE=Leaf;
RA Gaffe J., Tiznado M.E., Handa A.K.;
RT "Cloning and nucleotide sequence of a pectin methylesterase cDNA homologue
RT from tomato leaves.";
RL (er) Plant Gene Register PGR96-017(1996).
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 -!- 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 -!- 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 EMBL; U49330; AAD09283.1; -; mRNA.
DR PIR; T07848; T07848.
DR RefSeq; NP_001233857.2; NM_001246928.2.
DR AlphaFoldDB; Q43143; -.
DR SMR; Q43143; -.
DR STRING; 4081.Solyc03g123630.2.1; -.
DR PaxDb; Q43143; -.
DR PRIDE; Q43143; -.
DR GeneID; 544016; -.
DR KEGG; sly:544016; -.
DR eggNOG; ENOG502QVK0; Eukaryota.
DR InParanoid; Q43143; -.
DR OrthoDB; 674407at2759; -.
DR BRENDA; 3.1.1.11; 3101.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q43143; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
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; 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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..583
FT /note="Pectinesterase/pectinesterase inhibitor U1"
FT /id="PRO_0000023493"
FT REGION 60..221
FT /note="Pectinesterase inhibitor U1"
FT REGION 272..570
FT /note="Pectinesterase U1"
FT ACT_SITE 400
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 421
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 347
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 399
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 414..434
FT /evidence="ECO:0000250"
SQ SEQUENCE 583 AA; 64103 MW; FA7434833CDA9EF2 CRC64;
MTRVEDFFSK QIDFCKRKKK IYLAIVASVL LVAAVIGVVA GVKSHSKNSD DHADIMAISS
SAHAIVKSAC SNTLHPELCY SAIVNVSDFS KKVTSQKDVI ELSLNITVKA VRRNYYAVKE
LIKTRKGLTP REKVALHDCL ETMDETLDEL HTAVEDLELY PNKKSLKEHV EDLKTLISSA
ITNQETCLDG FSHDEADKKV RKVLLKGQKH VEKMCSNALA MICNMTDTDI ANEMKLSAPA
NNRKLVEDNG EWPEWLSAGD RRLLQSSTVT PDVVVAADGS GDYKTVSEAV RKAPEKSSKR
YVIRIKAGVY RENVDVPKKK TNIMFMGDGK SNTIITASRN VQDGSTTFHS ATVVRVAGKV
LARDITFQNT AGASKHQAVA LCVGSDLSAF YRCDMLAYQD TLYVHSNRQF FVQCLVAGTV
DFIFGNGAAV FQDCDIHARR PGSGQKNMVT AQGRTDPNQN TGIVIQKCRI GATSDLRPVQ
KSFPTYLGRP WKEYSRTVIM QSSITDVIQP AGWHEWNGNF ALDTLFYGEY ANTGAGAPTS
GRVKWKGHKV ITSSTEAQAY TPGRFIAGGS WLSSTGFPFS LGL
