A0AAD8IH52 · A0AAD8IH52_9APIA
- Proteinpectinesterase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids852 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n methanol + n H+
[(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
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 | 687 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | pectinesterase activity | |
Molecular Function | pectinesterase inhibitor activity | |
Biological Process | cell wall modification |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namepectinesterase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Apiales > Apiaceae > Apioideae > apioid superclade > Tordylieae > Tordyliinae > Heracleum
Accessions
- Primary accessionA0AAD8IH52
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 7-28 | Helical | ||||
Sequence: VTVIGVSSIVLVAVAIAVAVTI |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-189 | Pectinesterase inhibitor | ||||
Sequence: TANKSVKIMCEATDYKDACAKSLSSANTDDPKELIKTSFKAAVTDINDVVGKSKTFEDASKDSRTKEAYQLCKDLLETSVNDLDRSGDKVGQFEAGKMEEYVADVRTWLTGAIDYQETCIDAFQNTSGDAGDKMKDLLKSSYELSSNSLAM | ||||||
Region | 213-535 | Disordered | ||||
Sequence: DYGPRGDPPPSEDPGGLGSGSHRRLFEYDYGPRGDPPPSEDPGGPGSGSHRRLFEYDYGPRGDPPPSEDPGGPGSGSHRKLFEYDYGPRGDPPPSEDPGVPGSGSHRRIFEYDYGPRGDPPPSEDPGVPGSGSHRRLFEYDYGPRGDPPPSEDPGGPGSGSHRRLFEYDYGPRGDPPPSEDPGGPGSGSHRRLFEYDYGPRGDPPPSEDPGGPGSKSHRRLFDAAYGPPSDHSVTEDPGQGVESTVRKVFDNDNEPPSDDGTSNQNAEHISKGARKATTPGDDGPSNQNAEHISKGARKAGSSSKEVPKWAGTHQRNLLQGNP | ||||||
Compositional bias | 468-484 | Polar residues | ||||
Sequence: PPSDDGTSNQNAEHISK |
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
- Length852
- Mass (Da)92,088
- Last updated2024-05-29 v1
- Checksum6096B2308D2CE698
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 468-484 | Polar residues | ||||
Sequence: PPSDDGTSNQNAEHISK |
Keywords
- Technical term