Protein-L-isoaspartate O-methyltransferase
Details
- Name
- Protein-L-isoaspartate O-methyltransferase
- Synonyms
- 2.1.1.77
- L-isoaspartyl protein carboxyl methyltransferase
- PIMT
- Protein L-isoaspartyl methyltransferase
- Protein-beta-aspartate methyltransferase
- Gene Name
- pcm
- Organism
- Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
- Amino acid sequence
>lcl|BSEQ0021860|Protein-L-isoaspartate O-methyltransferase MREKLFWILKKYGVSDHIAKAFLEIPREEFLTKSYPLSYVYEDIVLVSYDDGEEYSTSSQ PSLMALFMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNV ERLGIENVIFVCGDGYYGVPEFSPYDVIFVTVGVDEVPETWFTQLKEGGRVIVPINLKLS RRQPAFLFKKKDPYLVGNYKLETRFITAGGNLGNLLERNRKLLREFPFNREILLVRSHIF VELVDLLTRRLTEIDGTFYYAGPNGVVEFLDDRMRIYGDAPEIENLLTQWESCGYRSFEY LMLHVGYNAFSHISCSI
- Number of residues
- 317
- Molecular Weight
- 36399.64
- Theoretical pI
- 5.31
- GO Classification
- Functionsprotein-L-isoaspartate (D-aspartate) O-methyltransferase activityProcessesprotein repairComponentscytoplasm
- General Function
- Protein-l-isoaspartate (d-aspartate) o-methyltransferase activity
- Specific 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.
- Pfam Domain Function
- PCMT (PF01135)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0021861|Protein-L-isoaspartate O-methyltransferase (pcm) ATGAGAGAAAAGCTCTTTTGGATTCTTAAAAAGTACGGTGTGAGCGATCACATCGCGAAG GCTTTTCTGGAAATACCCCGTGAGGAGTTCCTGACGAAGTCCTACCCACTCTCTTACGTT TACGAGGATATCGTTCTGGTTTCCTACGATGATGGAGAAGAATACAGCACTTCCAGTCAG CCCTCTTTGATGGCGCTGTTTATGGAGTGGGTGGGTCTGGACAAAGGAATGAGAGTCCTC GAAATAGGCGGAGGAACGGGTTACAACGCTGCCGTGATGAGCAGAGTTGTGGGTGAGAAA GGCCTTGTGGTCTCCGTGGAATATTCGAGGAAAATCTGCGAGATCGCGAAAAGGAACGTG GAACGCCTTGGAATAGAGAACGTTATTTTTGTCTGTGGCGATGGATACTACGGTGTTCCG GAGTTTTCCCCGTACGATGTTATCTTCGTAACAGTCGGTGTGGATGAGGTGCCGGAGACG TGGTTCACTCAACTCAAAGAAGGTGGGAGGGTGATAGTACCTATCAATTTGAAACTTTCA AGAAGACAGCCCGCTTTCCTGTTCAAAAAAAAGGATCCGTATCTTGTGGGAAACTACAAA CTGGAAACCAGGTTCATAACGGCAGGGGGCAATCTCGGAAATCTTCTCGAGAGGAACAGA AAGCTTTTGAGAGAATTTCCATTCAACAGAGAGATCTTACTCGTACGTTCTCATATCTTC GTGGAGCTGGTGGATCTCCTCACCAGGAGACTCACAGAGATTGATGGAACGTTCTACTAC GCTGGGCCAAACGGCGTGGTAGAGTTTCTCGATGACAGGATGAGAATCTACGGGGACGCT CCAGAGATAGAGAACCTTTTAACTCAGTGGGAAAGCTGCGGCTACAGGAGCTTCGAGTAT CTCATGCTTCATGTGGGTTACAACGCTTTTTCACATATATCCTGTTCTATTTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q56308 UniProtKB Entry Name PIMT_THEMA GenBank Gene ID U30501 - General References
- Swanson RV, Sanna MG, Simon MI: Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol. 1996 Jan;178(2):484-9. [Article]
- Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM: Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 1999 May 27;399(6734):323-9. [Article]
- Ichikawa JK, Clarke S: A highly active protein repair enzyme from an extreme thermophile: the L-isoaspartyl methyltransferase from Thermotoga maritima. Arch Biochem Biophys. 1998 Oct 15;358(2):222-31. [Article]
- Skinner MM, Puvathingal JM, Walter RL, Friedman AM: Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair. Structure. 2000 Nov 15;8(11):1189-201. [Article]