Reviewed,
UniProtKB/Swiss-Prot Q43209 (PIMT_WHEAT)
Last modified
June 16, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein-L-isoaspartate O-methyltransferase Short name=PIMT EC=2.1.1.77 Alternative name(s): Protein-beta-aspartate methyltransferase Protein L-isoaspartyl methyltransferase L-isoaspartyl protein carboxyl methyltransferase | ||
| Gene names |
| ||
| Organism | Triticum aestivum (Wheat) | ||
| Taxonomic identifier | 4565 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum |
Protein attributes
| Sequence length | 230 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues. |
| Catalytic activity | S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Tissue specificity | Highest contents in seeds. |
| Sequence similarities | Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | protein modification process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 230 | 230 | Protein-L-isoaspartate O-methyltransferase | PRO_0000111883 | |||||
Sites | |||||||||
| Active site | 65 | 1 | By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 18 | 1 | E → D | ||||||
| Natural variant | 41 | 1 | A → N | ||||||
| Natural variant | 52 | 1 | T → N | ||||||
| Natural variant | 54 | 1 | S → L | ||||||
| Natural variant | 122 | 1 | V → A | ||||||
| Natural variant | 143 | 1 | S → L | ||||||
| Natural variant | 147 | 1 | S → E | ||||||
| Natural variant | 156 | 1 | A → V | ||||||
| Natural variant | 203 | 1 | A → S | ||||||
| Natural variant | 208 | 1 | S → T | ||||||
| Natural variant | 210 | 1 | R → V | ||||||
| Natural variant | 214 | 1 | S → T | ||||||
Sequences
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References
| [1] | "Characterization of plant L-isoaspartyl methyltransferases that may be involved in seed survival: purification, cloning, and sequence analysis of the wheat germ enzyme." Mudgett M.B., Clarke S. Biochemistry 32:11100-11111(1993) [PubMed: 8198620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION. Strain: cv. Augusta. |
Cross-references
Sequence databases | |
|---|---|
| L07941 mRNA. Translation: AAA34297.1. | |
| PIR | T06519. |
| UniGene | Ta.162 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I1N based on UniProtKB P22061. |
| ModBase | Search... |
Organism-specific databases | |
| Gramene | Q43209. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.77. 253. |
Family and domain databases | |
| InterPro | IPR000682. PCMT. [Graphical view] |
| PANTHER | PTHR11579. PCMT. 1 hit. |
| Pfam | PF01135. PCMT. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00080. pimt. 1 hit. |
| PROSITE | PS01279. PCMT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PIMT_WHEAT | ||||||||
| Accession | Primary (citable) accession number: Q43209 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


