Tag | Content |
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CPLM ID | CPLM-002983 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein-L-isoaspartate O-methyltransferase |
Protein Synonyms/Alias | L-isoaspartyl protein carboxyl methyltransferase; Protein L-isoaspartyl methyltransferase; Protein-beta-aspartate methyltransferase; PIMT |
Gene Name | pcm |
Gene Synonyms/Alias | b2743; JW2713 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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34 | LAAVPREKFVDEAFE | acetylation | [1] | 118 | WQARRRLKNLDLHNV | acetylation | [1] | 204 | VRFVPLVKGELA*** | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | 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. |
Sequence Annotation | ACT_SITE 59 59 By similarity. |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Methyltransferase; Reference proteome; S-adenosyl-L-methionine; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 208 AA |
Protein Sequence | MVSRRVQALL DQLRAQGIQD EQVLNALAAV PREKFVDEAF EQKAWDNIAL PIGQGQTISQ 60 PYMVARMTEL LELTPQSRVL EIGTGSGYQT AILAHLVQHV CSVERIKGLQ WQARRRLKNL 120 DLHNVSTRHG DGWQGWQARA PFDAIIVTAA PPEIPTALMT QLDEGGILVL PVGEEHQYLK 180 RVRRRGGEFI IDTVEAVRFV PLVKGELA 208 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:EcoCyc. GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:EcoCyc. GO:0030091; P:protein repair; IEA:HAMAP. |
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