O49006 · PME3_ARATH
- ProteinPectinesterase/pectinesterase inhibitor 3
- GenePME3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids592 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts in the modification of cell walls via demethylesterification of cell wall pectin (PubMed:21171891, PubMed:26183897).
Required for zinc Zn2+ homeostasis and to monitor Zn2+ influence on cell wall-controlled growth processes such as root cell elongation (PubMed:23826687).
Monitors seed germination and favors root hairs production (PubMed:28375469).
Prevents cruciferin seed storage proteins activity, but promotes the expression of genes involved in cell wall organization and remodeling as well as genes involved in lipid and protein metabolism, during post-germinative growth of seedlings (PubMed:28375469).
Confers sensitivity to Zn2+ when overexpressed (PubMed:23826687).
Acts as a susceptibility factor required for the initial colonization of the host tissue by virulent pathogens including Botrytis cinerea and Pectobacterium carotovorum, probably by facilitating cell wall pectine degradation by pathogen pectic enzymes after its demethylesterification (PubMed:21171891).
Required for zinc Zn2+ homeostasis and to monitor Zn2+ influence on cell wall-controlled growth processes such as root cell elongation (PubMed:23826687).
Monitors seed germination and favors root hairs production (PubMed:28375469).
Prevents cruciferin seed storage proteins activity, but promotes the expression of genes involved in cell wall organization and remodeling as well as genes involved in lipid and protein metabolism, during post-germinative growth of seedlings (PubMed:28375469).
Confers sensitivity to Zn2+ when overexpressed (PubMed:23826687).
Acts as a susceptibility factor required for the initial colonization of the host tissue by virulent pathogens including Botrytis cinerea and Pectobacterium carotovorum, probably by facilitating cell wall pectine degradation by pathogen pectic enzymes after its demethylesterification (PubMed:21171891).
Miscellaneous
The PMEI region may act as an autoinhibitory domain and prevent untimely PME activity during transport.
Catalytic activity
- [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n methanol + n H+This reaction proceeds in the forward direction.
[(1→4)-α-D-galacturonosyl methyl ester](n) RHEA-COMP:14573 + n CHEBI:15377 = [(1→4)-α-D-galacturonosyl](n) RHEA-COMP:14570 + n CHEBI:17790 + n CHEBI:15378
Activity regulation
Regulated negatively by pectinesterase inhibitors (e.g. PMEI3, PMEI4, PMEI7 and PMEI9) in a pH-dependent manner, mainly in slightly acidic conditions (pH 6.0 and 5.0), especially in dark-grown hypocotyls; this processus relies on changes in the protonation of amino acids involved in intermolecular and intramolecular interactions.
Biotechnology
Mutant pme3 facilitates efficiency of viable mesophyll protoplast isolation probably as a result of reduced methylesterified homogalacturonan (HGA) level.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
12 μM | HG96B82 | |||||
5 μM | HG96B69 | |||||
9 μM | HG96B20 | |||||
6 μM | HG97B77P63 | |||||
224 μM | HG96P64 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.07 μmol/min/ug | with HG96B82 as substrate | ||||
0.05 μmol/min/ug | with HG96B69 as substrate | ||||
0.1 μmol/min/ug | with HG96B20 as substrate | ||||
0.05 μmol/min/ug | with HG97B77P63 as substrate | ||||
0.02 μmol/min/ug | with HG96P64 as substrate |
pH Dependence
Optimum pH is 7.5 on homogalacturonan (HG) substrates with a degree of methylesterification between 60 and 80% and a random distribution of methyl esters.
Pathway
Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 356 | substrate; for pectinesterase activity | |||
Binding site | 386 | substrate; for pectinesterase activity | |||
Site | 408 | Transition state stabilizer | |||
Active site | 409 | Proton donor; for pectinesterase activity | |||
Active site | 430 | Nucleophile; for pectinesterase activity | |||
Binding site | 454 | substrate; for pectinesterase activity | |||
Binding site | 498 | substrate; for pectinesterase activity | |||
Binding site | 500 | substrate; for pectinesterase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apoplast | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | plant-type cell wall | |
Molecular Function | enzyme inhibitor activity | |
Molecular Function | mRNA binding | |
Molecular Function | pectinesterase activity | |
Biological Process | cell wall modification | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to fungus | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | negative regulation of seed germination | |
Biological Process | pectin catabolic process | |
Biological Process | regulation of gene expression | |
Biological Process | regulation of unidimensional cell growth | |
Biological Process | response to bacterium | |
Biological Process | response to fungus | |
Biological Process | response to nematode | |
Biological Process | response to zinc ion | |
Biological Process | root development | |
Biological Process | root hair cell development |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePectinesterase/pectinesterase inhibitor 3
- Alternative names
- Cleaved into 2 chains
Including 2 domains:
- Recommended namePectinesterase inhibitor 3
- Alternative names
- Recommended namePectinesterase 3
- EC number
- Short namesPE 3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO49006
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Present in hypocotyl cell walls.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Early germination and reduced root hair production associated with lower expression of several pectin-degrading enzymes, genes involved in cell wall organization and remodeling and genes involved in lipid and protein metabolism, thus leading to a global decrease in proteolytic activity, however, cruciferin genes accumulate abnormally (PubMed:28375469).
Normal sensitivity to zinc Zn2+ (PubMed:23826687).
Increased resistance to Botrytis cinerea and Pectobacterium carotovorum associated with a reduced global pectin methylesterase (PME) activity, and correlating with an impaired ability of pathogens to grow on methylesterified pectin (PubMed:21171891).
Normal sensitivity to zinc Zn2+ (PubMed:23826687).
Increased resistance to Botrytis cinerea and Pectobacterium carotovorum associated with a reduced global pectin methylesterase (PME) activity, and correlating with an impaired ability of pathogens to grow on methylesterified pectin (PubMed:21171891).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 408 | Lost activity. Confers sensitivity to zinc Zn2+ when overexpressed. | |||
Mutagenesis | 409 | Lost activity. Confers sensitivity to zinc Zn2+ when overexpressed. | |||
Mutagenesis | 497 | In osz2; semi-dominant mutation with impaired proteolytic processing, and leading to an increased sensitivity to zinc Zn2+ characterized by Zn-triggered reduced root elongation due to a defect in cell elongation, but an increase number of root hairs; this phenotype is suppressed by calcium Ca2+ treatment. No obvious impact on pectin methylesterification. | |||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 24 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-35 | ||||
Propeptide | PRO_0000458966 | 36-238 | Removed in mature 42 kDa form | ||
Propeptide | PRO_0000458965 | 36-273 | Removed in mature 38 kDa form | ||
Chain | PRO_0000371662 | 36-592 | Pectinesterase/pectinesterase inhibitor 3 | ||
Glycosylation | 96 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 215 | N-linked (GlcNAc...) asparagine | |||
Chain | PRO_0000458967 | 239-592 | Pectinesterase 3 of 42 kDa | ||
Chain | PRO_0000458968 | 274-592 | Pectinesterase 3 of 38 kDa | ||
Disulfide bond | 423↔443 | ||||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, cotyledons, hypocotyls, seedlings, leaves, stems, flowers, dry seeds and siliques (PubMed:16622707, PubMed:28375469, PubMed:9767082).
Accumulates in etiolated hypocotyls (at protein level) (PubMed:26183897).
Accumulates in etiolated hypocotyls (at protein level) (PubMed:26183897).
Induction
Induced by necrotrophic pathogens such as Pectobacterium carotovorum and Botrytis cinerea.
Developmental stage
Expressed throughout silique development.
Gene expression databases
Interaction
Subunit
Interacts with BIIDXI and At5g11420 (PubMed:25442819).
Binds reversibly to PMEI4, PMEI7 and PMEI8 to be inhibited; the stability of the PME3-PMEIs complexes and the inhibition of the pectin methylesterase (PME) activity is pH-dependent, based on protonation status of amino-acids at the complex interface (PubMed:26183897, PubMed:28034952, PubMed:29109147).
Binds reversibly to PMEI4, PMEI7 and PMEI8 to be inhibited; the stability of the PME3-PMEIs complexes and the inhibition of the pectin methylesterase (PME) activity is pH-dependent, based on protonation status of amino-acids at the complex interface (PubMed:26183897, PubMed:28034952, PubMed:29109147).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 53-212 | Pectinesterase inhibitor 3 | |||
Region | 281-578 | Pectinesterase 3 | |||
Sequence similarities
In the N-terminal section; belongs to the PMEI family.
In the C-terminal section; belongs to the pectinesterase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length592
- Mass (Da)64,256
- Last updated2009-05-05 v2
- MD5 Checksum75D32BEF3D1B19C47C00B2821551AC9F
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 81-82 | in Ref. 1; AAC72288 | |||
Sequence conflict | 280 | in Ref. 1; AAC72288 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF033204 EMBL· GenBank· DDBJ | AAC72288.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB022220 EMBL· GenBank· DDBJ | BAB01037.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE75500.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY037184 EMBL· GenBank· DDBJ | AAK59769.1 EMBL· GenBank· DDBJ | mRNA | ||
AY052252 EMBL· GenBank· DDBJ | AAK97722.1 EMBL· GenBank· DDBJ | mRNA | ||
AY143950 EMBL· GenBank· DDBJ | AAN28889.1 EMBL· GenBank· DDBJ | mRNA | ||
AY058892 EMBL· GenBank· DDBJ | AAL24278.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK221816 EMBL· GenBank· DDBJ | BAD94011.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |