A0A178UB30 · A0A178UB30_ARATH
- ProteinPectinesterase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids538 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
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
Pathway
Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 374 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | enzyme inhibitor activity | |
Molecular Function | pectinesterase activity | |
Biological Process | cell wall modification | |
Biological Process | pectin catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePectinesterase
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionA0A178UB30
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MGVIDMVLFWVLLVNA | ||||||
Chain | PRO_5033788647 | 17-538 | Pectinesterase | |||
Sequence: LLIVDASSRNMPFAYQNEMQRHCSSTKYTSLCVQNLREFRHGSLDGLDFVSFLVNKTISDSNLLIPPLSSSMGSSKLVSLEDSTYTLPSPSVSDSCERLMKMSTRRLRQAMEALNGSSRKRHTKHDVQTWLSAAMTFQQACKDSILDSGGSSSASAISHISQKMDHLSRLVSNSLTLVDTIMKNPKPKTKSTALPRWVTAGERRLLVGRARAHVVVAKDGSGDYRTVMEAVTAAHGNGRFIIYVKRGVYKEKVIIHKHEITLIGEGKDLTVIVGDDSATGGTSVPDTATMTVTGDGFIARDIGIKNIAGPRGHQAIALSITSDQSVLYRCSISGYQDTLYAAALRQFYRECDIYGTIDFIFGNAAAVFQSCNIFLRRPHGVKAYNVILANGRTDQRQNTGFALHSCRIRTDSDLSPVKHKYSSYLGRPWRKYSRAIVMESYIDDAIAEEGWAGWLDSGDEVLKTLYFGEFKNYGPKARISKRVTWEGFHSIGFEEANYFSVGKFLDGVSWLPSTGVSFTSGI |
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-193 | Pectinesterase inhibitor | ||||
Sequence: AYQNEMQRHCSSTKYTSLCVQNLREFRHGSLDGLDFVSFLVNKTISDSNLLIPPLSSSMGSSKLVSLEDSTYTLPSPSVSDSCERLMKMSTRRLRQAMEALNGSSRKRHTKHDVQTWLSAAMTFQQACKDSILDSGGSSSASAISHISQKMDHLSRLVSNSLTL |
Sequence similarities
In the C-terminal section; belongs to the pectinesterase family.
In the N-terminal section; belongs to the PMEI family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length538
- Mass (Da)59,466
- Last updated2016-09-07 v1
- ChecksumABC777B49120A277