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
Functions
protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Processes
protein repair
Components
cytoplasm
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
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
ResourceLink
UniProtKB IDQ56308
UniProtKB Entry NamePIMT_THEMA
GenBank Gene IDU30501
General References
  1. Swanson RV, Sanna MG, Simon MI: Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol. 1996 Jan;178(2):484-9. [PubMed:8550470]
  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. [PubMed:10360571]
  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. [PubMed:9784234]
  4. 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. [PubMed:11080641]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01752S-adenosyl-L-homocysteineexperimentalunknownDetails