AC MF_00090; DC Protein; auto TR HAMAP; MF_00090; -; 1; level=0 XX Names: PIMT XX ID PIMT DE RecName: Full=Protein-L-isoaspartate O-methyltransferase; DE EC=2.1.1.77; DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase; DE AltName: Full=Protein L-isoaspartyl methyltransferase; DE AltName: Full=Protein-beta-aspartate methyltransferase; DE Short=PIMT; GN Name=pcm; XX CC -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues CC in peptides and proteins that result from spontaneous decomposition of CC normal L-aspartyl and L-asparaginyl residues. It plays a role in the CC repair and/or degradation of damaged proteins. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine = CC [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA- CC COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596, CC ChEBI:CHEBI:90598; EC=2.1.1.77; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L- CC isoaspartyl/D-aspartyl protein methyltransferase family. XX DR Pfam; PF01135; PCMT; 1; trigger=no DR NCBIfam; TIGR00080; Pimt; 1; trigger=no DR PROSITE; PS01279; PCMT; 1; trigger=no XX KW Cytoplasm KW Transferase KW Methyltransferase KW S-adenosyl-L-methionine XX GO GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity GO GO:0036211; P:protein modification process GO GO:0030091; P:protein repair GO GO:0005737; C:cytoplasm XX FT From: PIMT_ECOLI (P0A7A5) FT ACT_SITE 59 FT Condition: S XX Size: 198-327; Related: None; Template: Q56308; Q8TZR3; Scope: Bacteria Archaea Fusion: Nter: None Cter: Duplicate: in ANADF, ARCFU, GEOUR, MARN8, NITOC, NITMU, PELPD, POLSJ, CUPNH, RHOP2, SHESH, SYNFM Plasmid: None Comments: Possible wrong starts. Unknown C-terminal domain in THEMA. XX # Revision 1.32 2023/06/01 //