Q43143 (PMEU1_SOLLC) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 76.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pectinesterase/pectinesterase inhibitor U1 Including the following 2 domains:
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| Gene names |
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| Organism | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | ||
| Taxonomic identifier | 4081 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon |
Protein attributes
| Sequence length | 583 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Acts in the modification of cell walls via demethylesterification of cell wall pectin By similarity. |
| Catalytic activity | Pectin + n H2O = n methanol + pectate. |
| Pathway | Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. |
| Subcellular location | |
| Miscellaneous | The PMEI region may act as an autoinhibitory domain and prevent untimely PME activity during transport. |
| Sequence similarities | In the N-terminal section; belongs to the PMEI family. In the C-terminal section; belongs to the pectinesterase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Cell wall Secreted |
| Domain | Signal |
| Molecular function | Aspartyl esterase Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | cell wall modification Inferred from electronic annotation. Source: InterPro cellular cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW enzyme inhibitor activityInferred from electronic annotation. Source: InterPro pectinesterase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 40 | 40 | Potential | ||||||||
| Chain | 41 – 583 | 543 | Pectinesterase/pectinesterase inhibitor U1 | PRO_0000023493 | |||||||
Regions | |||||||||||
| Region | 60 – 221 | 162 | Pectinesterase inhibitor U1 | ||||||||
| Region | 272 – 570 | 299 | Pectinesterase U1 | ||||||||
Sites | |||||||||||
| Active site | 400 | 1 | Proton donor; for pectinesterase activity By similarity | ||||||||
| Active site | 421 | 1 | Nucleophile; for pectinesterase activity By similarity | ||||||||
| Binding site | 347 | 1 | Substrate; for pectinesterase activity By similarity | ||||||||
| Binding site | 377 | 1 | Substrate; for pectinesterase activity By similarity | ||||||||
| Binding site | 489 | 1 | Substrate; for pectinesterase activity By similarity | ||||||||
| Binding site | 491 | 1 | Substrate; for pectinesterase activity By similarity | ||||||||
| Site | 399 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 85 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 105 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 224 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 414 ↔ 434 | By similarity | |||||||||
Sequences
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References
| [1] | "Cloning and nucleotide sequence of a pectin methylesterase cDNA homologue from tomato leaves." Gaffe J., Tiznado M.E., Handa A.K. Plant Gene Register PGR96-017 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Rio Grande. Tissue: Leaf. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U49330 mRNA. Translation: AAD09283.1. |
| PIR | T07848. |
| RefSeq | NP_001233857.1. NM_001246928.1. |
| UniGene | Les.67. |
3D structure databases | |
| ProteinModelPortal | Q43143. |
| SMR | Q43143. Positions 265-583. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 544016. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.11. 3101. |
Family and domain databases | |
| InterPro | IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. IPR006501. Pectinesterase_inhib. [Graphical view] |
| Gene3D | G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit. G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit. |
| Pfam | PF01095. Pectinesterase. 1 hit. PF04043. PMEI. 1 hit. [Graphical view] |
| SMART | SM00856. PMEI. 1 hit. [Graphical view] |
| SUPFAM | SSF51126. Pectin_lyas_like. 1 hit. SSF101148. Pectinesterase_inhib. 1 hit. |
| TIGRFAMs | TIGR01614. PME_inhib. 1 hit. |
| PROSITE | PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PMEU1_SOLLC | ||||||||
| Accession | Primary (citable) accession number: Q43143 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with