Q9LVQ0 · PME31_ARATH
- ProteinPectinesterase 31
- GenePME31
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids317 (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:18936961).
Acts in a blockwise manner, resulting in a cell wall rigidification
Acts in a blockwise manner, resulting in a cell wall rigidification
Miscellaneous
This is the only member of the pectinesterase family that do not contain a transmembrane or a signal peptide.
Catalytic activity
- [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H+ + n methanol
[(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:15378 + n CHEBI:17790
Activity regulation
Does not require salt for activity. Not inhibited by kiwi pectin methylesterase inhibitor (PMEI).
pH Dependence
Optimum pH is 8.0-8.5.
Temperature Dependence
Fully active at 0 or 30 degrees Celsius, inactive at 55 degrees Celsius.
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 | 91 | substrate | ||||
Sequence: T | ||||||
Binding site | 121 | substrate | ||||
Sequence: Q | ||||||
Site | 143 | Transition state stabilizer | ||||
Sequence: Q | ||||||
Active site | 144 | Proton donor | ||||
Sequence: D | ||||||
Active site | 165 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 222 | substrate | ||||
Sequence: R | ||||||
Binding site | 224 | substrate | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | pectinesterase activity | |
Biological Process | cell wall modification | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | pectin catabolic process | |
Biological Process | pectin metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePectinesterase 31
- EC number
- Short namesPE 31
- 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 accessionQ9LVQ0
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000371683 | 1-317 | Pectinesterase 31 | |||
Sequence: MATTRMVRVSQDGSGDYCSVQDAIDSVPLGNTCRTVIRLSPGIYRQPVYVPKRKNFITFAGISPEITVLTWNNTASKIEHHQASRVIGTGTFGCGSVIVEGEDFIAENITFENSAPEGSGQAVAIRVTADRCAFYNCRFLGWQDTLYLHHGKQYLKDCYIEGSVDFIFGNSTALLEHCHIHCKSQGFITAQSRKSSQESTGYVFLRCVITGNGQSGYMYLGRPWGPFGRVVLAYTYMDACIRNVGWHNWGNAENERSACFYEYRCFGPGSCSSERVPWSRELMDDEAGHFVHHSFVDPEQDRPWLCLRMGVKTPYSA |
Proteomic databases
Expression
Tissue specificity
Expressed in siliques.
Developmental stage
Expressed during late developmental phases of siliques.
Gene expression databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9LVQ0 | RFC4 Q93ZX1 | 4 | EBI-4466887, EBI-4470690 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length317
- Mass (Da)35,520
- Last updated2000-10-01 v1
- ChecksumBCD96098853B585B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018121 EMBL· GenBank· DDBJ | BAB01985.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE77534.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY070091 EMBL· GenBank· DDBJ | AAL49785.1 EMBL· GenBank· DDBJ | mRNA | ||
AY096561 EMBL· GenBank· DDBJ | AAM20211.1 EMBL· GenBank· DDBJ | mRNA | ||
AY084418 EMBL· GenBank· DDBJ | AAM60992.1 EMBL· GenBank· DDBJ | mRNA |