PIMT2_POLSJ
ID PIMT2_POLSJ Reviewed; 211 AA.
AC Q123X2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE EC=2.1.1.77 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein L-isoaspartyl methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein-beta-aspartate methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE Short=PIMT 2 {ECO:0000255|HAMAP-Rule:MF_00090};
GN Name=pcm2 {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=Bpro_4278;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00090}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00090};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00090}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00090}.
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DR EMBL; CP000316; ABE46170.1; -; Genomic_DNA.
DR AlphaFoldDB; Q123X2; -.
DR SMR; Q123X2; -.
DR STRING; 296591.Bpro_4278; -.
DR EnsemblBacteria; ABE46170; ABE46170; Bpro_4278.
DR KEGG; pol:Bpro_4278; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_4; -.
DR OMA; TISAIHM; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00080; pimt; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..211
FT /note="Protein-L-isoaspartate O-methyltransferase 2"
FT /id="PRO_0000351902"
FT ACT_SITE 61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 211 AA; 23226 MW; A050B1BEC89513B0 CRC64;
MMEEITALVR ETRTETGKPA LDERVMAVMG KVPRHEFVPA DQLPRAYQNR PLPIGHGQTI
SQPYIVALMT DLARVEPGHK VLEVGTGSGY QAAVMAHLAR AVYTIEIIEP LGLQARQRLQ
KLGYDNVQVR LGDGYHGWEE HAPYDAILVT AAASHIPPPL IRQLKAGGRM VIPVGAAFMV
QQLMLVEKNR DGTVSTRQIL PVAFVPLTGQ R