ID   PIMT1_PELPD             Reviewed;         215 AA.
AC   A1ASL8;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein L-isoaspartyl methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein-beta-aspartate methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE            Short=PIMT 1 {ECO:0000255|HAMAP-Rule:MF_00090};
GN   Name=pcm1 {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=Ppro_2738;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000482; ABL00339.1; -; Genomic_DNA.
DR   RefSeq; WP_011736589.1; NC_008609.1.
DR   AlphaFoldDB; A1ASL8; -.
DR   SMR; A1ASL8; -.
DR   STRING; 338966.Ppro_2738; -.
DR   EnsemblBacteria; ABL00339; ABL00339; Ppro_2738.
DR   KEGG; ppd:Ppro_2738; -.
DR   eggNOG; COG2518; Bacteria.
DR   HOGENOM; CLU_055432_2_0_7; -.
DR   OMA; MVDTQVR; -.
DR   OrthoDB; 1948290at2; -.
DR   Proteomes; UP000006732; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..215
FT                   /note="Protein-L-isoaspartate O-methyltransferase 1"
FT                   /id="PRO_0000351896"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   215 AA;  23850 MW;  F3D11032C7DB8F8E CRC64;
     MNFDRARKKM VQEQIATRGI TDRRVLDAML KTPRHIFVQE AMAAQAYSDS SLPVGEKQTI
     SQPYTVALMT ELLELTGREK VLEIGTGSGY QTAILAALAD RVYTVERIRP LALRARKCLD
     SLRLFNVMLR INDSEGSPIG WDEEAPFDAI IVTAGAPAVP QVLTDQLAVD GRLVIPVGDE
     REQRLVKIVR KNDGTLETTT SIGCRFVPLI GRQGW