E7CIP7 · PME_SITOR
- ProteinPectinesterase
- GeneCE8-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids382 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Pectinesterase which probably plays an important role in the digestion of plant cell walls.
Miscellaneous
May originate from horizontal gene transfer of a bacterial enzyme to an ancentral weevil genome.
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 binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 193 | substrate | ||||
Sequence: Q | ||||||
Site | 215 | Transition state stabilizer | ||||
Sequence: Q | ||||||
Active site | 216 | Proton donor | ||||
Sequence: D | ||||||
Active site | 242 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 306 | substrate | ||||
Sequence: R | ||||||
Binding site | 308 | substrate | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | pectinesterase activity | |
Biological Process | cell wall modification | |
Biological Process | pectin catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePectinesterase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Coleoptera > Polyphaga > Cucujiformia > Curculionidae > Dryophthorinae > Sitophilus
Accessions
- Primary accessionE7CIP7
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MKIIVLLLLAVVLASA | ||||||
Chain | PRO_0000449247 | 17-382 | Pectinesterase | |||
Sequence: DQTAPGTASRPILTASESNYFTTATYLQGWSPPSISTSKADYTVGNGYNTIQAAVNAAINTGGTTRKYIKINAGTYQEVVYIPNTKVPLTIYGGGSSPSDTLITLNMPAQTTPSAYKSLVGSLFNSADPAYSMYNSCASKSGTIGTSCSTVFWVKAPAVQIVNLSIENSAKNTGDQQAVALQTNSDQIQIHNARLLGHQDTLYAGSGSSSVERSYYTNTYIEGDIDFVFGGGSAIFESCTFYVKADRRSDTAVVFAPDTDPHKMYGYFVYKSTITGDSAWSSSKKAYLGRAWDSGVSSSSAYVPGTSPNGQLIIKESTIDGIINTSGPWTTATSGRTYSGNNANSRDLNNDNYNRFWEYNNSGNGA | ||||||
Disulfide bond | 153↔164 | |||||
Sequence: CASKSGTIGTSC | ||||||
Glycosylation | 179 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 340 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 376 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed throughout the midgut with particularly strong expression in the ventriculus.
Structure
Family & Domains
Sequence similarities
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.
- Length382
- Mass (Da)40,697
- Last updated2011-03-08 v1
- ChecksumA6E2589668BD245C
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6J2X9X7 | A0A6J2X9X7_SITOR | LOC115876414 | 382 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 77 | in Ref. 1; AAW28928 | ||||
Sequence: T → A | ||||||
Sequence conflict | 153-159 | in Ref. 1; AAW28928 | ||||
Sequence: CASKSGT → WRSKSGA | ||||||
Sequence conflict | 170 | in Ref. 1; AAW28928 | ||||
Sequence: V → G | ||||||
Sequence conflict | 214 | in Ref. 1; AAW28928 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 268 | in Ref. 1; AAW28928 | ||||
Sequence: A → S | ||||||
Sequence conflict | 311 | in Ref. 1; AAW28928 | ||||
Sequence: G → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY841894 EMBL· GenBank· DDBJ | AAW28928.1 EMBL· GenBank· DDBJ | mRNA | ||
HM175754 EMBL· GenBank· DDBJ | ADU33259.1 EMBL· GenBank· DDBJ | mRNA |