Protein-L-isoaspartate O-methyltransferase

Details

Name
Protein-L-isoaspartate O-methyltransferase
年代ynonyms
  • 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
分子量
36399.64
Theoretical pI
5.31
GO Classification
Functions
protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Processes
protein repair
Components
cytoplasm
General Function
Protein-l-isoaspartate (d-aspartate) o-methyltransferase activity
年代pecific 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
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
  1. 年代wanson RV, Sanna MG, Simon MI: Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol. 1996 Jan;178(2):484-9. [Article]
  2. 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]
  3. 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]
  4. 年代kinner 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]

Drug Relations

Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details
DB01752 年代-adenosyl-L-homocysteine experimental unknown Details