Q0DIU9 · Q0DIU9_ORYSJ
- ProteinPectinesterase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids581 (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 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 | 410 | |||||
Sequence: D |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | enzyme inhibitor activity | |
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
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ0DIU9
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MAVRYEKKAMCALLLSLIMVALSVA | ||||||
Chain | PRO_5005142431 | 26-581 | Pectinesterase | |||
Sequence: AAGDGDAPPSTPVSPTTACNDTTDPSFCRTVLPPRGSSDLYTYGRFSVARSLDSARRFAGLVGRYLARHRGLSPAAVGALRDCQLMSELNVDFLSAAGATLRSAADALPDPQADDVHTLLSAILTNQQTCLDGLQAASSSWSERGGGGLAAPIANGTKLYSLSLSLFTRAWVPTAKGSKHHGGGKKPHQGHGKKQPPAAAASMRRGLFDAADGEMARRVAMEGPEATVAVNGVVTVDQGGGGNYTTVGDAVAAAPSNLDGSTGHYVIYVAGGVYEENVVVPKHKRYIMMVGDGVGQTVITGNRSVVDGWTTFNSATFAVVGQGFVAMNMTFRNTAGPSKHQAVALRSGADLSAFYGCSFEAYQDTLYAHSLRQFYRRCDVYGTVDYVFGNAAVVFQSCAFLSRLPRPRPVQHRHGAGPIRPQPEHRHLHPGLLPPRRPGPRRRRRRRPDAHLPRPAVEELLQDGGHGVLRRRPRRPGRVDAVVRRLRARHALLRRVQQLRPRRRHQPPRRLAGLPRPRRRRRRRQLHRHQHGARRQLAAPDRRPLHQRLPHFRSTY |
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-191 | Pectinesterase inhibitor | ||||
Sequence: STPVSPTTACNDTTDPSFCRTVLPPRGSSDLYTYGRFSVARSLDSARRFAGLVGRYLARHRGLSPAAVGALRDCQLMSELNVDFLSAAGATLRSAADALPDPQADDVHTLLSAILTNQQTCLDGLQAASSSWSERGGGGLAAPIANGTKLYSLSLSL | ||||||
Region | 200-226 | Disordered | ||||
Sequence: AKGSKHHGGGKKPHQGHGKKQPPAAAA | ||||||
Region | 432-501 | Disordered | ||||
Sequence: PRPVQHRHGAGPIRPQPEHRHLHPGLLPPRRPGPRRRRRRRPDAHLPRPAVEELLQDGGHGVLRRRPRRP | ||||||
Compositional bias | 461-475 | Basic residues | ||||
Sequence: RRPGPRRRRRRRPDA | ||||||
Compositional bias | 524-558 | Basic residues | ||||
Sequence: LRPRRRHQPPRRLAGLPRPRRRRRRRQLHRHQHGA | ||||||
Region | 524-581 | Disordered | ||||
Sequence: LRPRRRHQPPRRLAGLPRPRRRRRRRQLHRHQHGARRQLAAPDRRPLHQRLPHFRSTY | ||||||
Compositional bias | 559-573 | Basic and acidic residues | ||||
Sequence: RRQLAAPDRRPLHQR |
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
- Length581
- Mass (Da)63,417
- Last updated2006-10-17 v1
- Checksum10121C44BCFC89BC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 461-475 | Basic residues | ||||
Sequence: RRPGPRRRRRRRPDA | ||||||
Compositional bias | 524-558 | Basic residues | ||||
Sequence: LRPRRRHQPPRRLAGLPRPRRRRRRRQLHRHQHGA | ||||||
Compositional bias | 559-573 | Basic and acidic residues | ||||
Sequence: RRQLAAPDRRPLHQR |