Q5PEE9 (PIMT_SALPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 44.
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: Protein-L-isoaspartate O-methyltransferase EC=2.1.1.77 Alternative name(s): L-isoaspartyl protein carboxyl methyltransferase Protein L-isoaspartyl methyltransferase Protein-beta-aspartate methyltransferase Short name=PIMT | ||||
| Gene names |
| ||||
| Organism | Salmonella paratyphi A [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 54388 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 208 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 By similarity. HAMAP MF_00090 |
| Catalytic activity | S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. HAMAP MF_00090 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00090. |
| Sequence similarities | Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| 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 – 208 | 208 | Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090 | PRO_1000004824 | |||||
Sites | |||||||||
| Active site | 59 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. Wilson R.K.Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000026 Genomic DNA. Translation: AAV78637.1. |
| RefSeq | YP_151949.1. NC_006511.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JG1 based on UniProtKB Q8TZR3. |
| ProteinModelPortal | Q5PEE9. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3177142. |
| GenomeReviews | Gene locus SPA2782 in contig CP000026_GR. |
| KEGG | spt:SPA2782. |
| PATRIC | 32355118. VBISalEnt134188_2957. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG699907. |
| OMA | YMVARMS. |
| ProtClustDB | PRK00312. |
Enzyme and pathway databases | |
| BioCyc | SENT295319:SPA2782-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00090. PIMT. [Tree] |
| InterPro | IPR000682. PCMT. [Graphical view] |
| KO | K00573. |
| 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_SALPA | ||||||||
| Accession | Primary (citable) accession number: Q5PEE9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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