O04886 (PME1_CITSI) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 69.
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 1 Short name=PE 1 EC=3.1.1.11 Alternative name(s): Pectin methylesterase | ||
| Gene names |
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| Organism | Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis) | ||
| Taxonomic identifier | 2711 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Sapindales › Rutaceae › Citrus |
Protein attributes
| Sequence length | 584 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 | |
| Tissue specificity | Expressed at high levels in flower buds, shoots and young leaves, and at lower levels in young fruit, young bark and juice vesicles. Not expressed at significant levels in leaf abscission zones following ethylene treatment or in mature leaves. In fruit abscission zones, expression was initially undetectable but increased markedly following ethylene treatment. Ref.1 |
| Induction | By ethylene. Ref.1 |
| 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 – 42 | 42 | Potential | ||||||||
| Chain | 43 – 584 | 542 | Pectinesterase 1 | PRO_0000023480 | |||||||
Sites | |||||||||||
| Active site | 401 | 1 | Proton donor By similarity | ||||||||
| Active site | 422 | 1 | Nucleophile By similarity | ||||||||
| Binding site | 348 | 1 | Substrate By similarity | ||||||||
| Binding site | 378 | 1 | Substrate By similarity | ||||||||
| Binding site | 490 | 1 | Substrate By similarity | ||||||||
| Binding site | 492 | 1 | Substrate By similarity | ||||||||
| Site | 400 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 108 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 129 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 226 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 415 ↔ 435 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 354 | 1 | A → V in AAB57670. Ref.1 | ||||||||
Sequences
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References
| [1] | "Genetics and expression of two pectinesterase genes in Valencia orange." Nairn C.J., Lewandowski D.J., Burns J.K. Physiol. Plantarum 102:226-235(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Valencia. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U82973 Genomic DNA. Translation: AAB57667.1. U82976 mRNA. Translation: AAB57670.1. |
| PIR | T10485. |
3D structure databases | |
| ProteinModelPortal | O04886. |
| SMR | O04886. Positions 266-584. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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 | PME1_CITSI | ||||||||
| Accession | Primary (citable) accession number: O04886 Secondary accession number(s): O04888 | ||||||||
| 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