ID PIMT2_CUPNH Reviewed; 306 AA.
AC Q0K951;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=H16_A2375;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AM260479; CAJ93470.1; -; Genomic_DNA.
DR RefSeq; WP_011615630.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K951; -.
DR SMR; Q0K951; -.
DR STRING; 381666.H16_A2375; -.
DR GeneID; 57644505; -.
DR KEGG; reh:H16_A2375; -.
DR PATRIC; fig|381666.6.peg.2784; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_1_0_4; -.
DR OrthoDB; 9810066at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF0; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..306
FT /note="Protein-L-isoaspartate O-methyltransferase 2"
FT /id="PRO_0000351917"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 306 AA; 32108 MW; 2DD023CA233959CA CRC64;
MSTTPPRNKF PLPLDAVVER KPAPARTAGL PAVGTPRPAA PTPAPAKPAK PRLPRTAAPA
PAPVPASAVE QRASAATAGG GGMASARARA ALAARLRAAG IRDERVLSAI ATVPRHLFVE
PGLASQAYED AALPIGHQQT ISKPSVVARM IELLREGLAA DAPLERVLEI GTGCGYQAAV
LSQVAREVFS IERIRPLHEQ AKANLRPLRV PNLRLHYGDG MLGLPQAAPF SAIILAAAGM
EVPEALLEQL AIGGRLIAPV AVMPPAGVPG QTVTQQLLLI ERRNRHRFHR TALEAVFFVP
LKSGTI
//
