ID   PIMT_FERNB              Reviewed;         199 AA.
AC   A7HL14;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase {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 {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000255|HAMAP-Rule:MF_00090};
DE            Short=PIMT {ECO:0000255|HAMAP-Rule:MF_00090};
GN   Name=pcm {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=Fnod_0742;
OS   Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=381764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL   Submitted (JUL-2007) 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; CP000771; ABS60597.1; -; Genomic_DNA.
DR   RefSeq; WP_011993915.1; NC_009718.1.
DR   AlphaFoldDB; A7HL14; -.
DR   SMR; A7HL14; -.
DR   STRING; 381764.Fnod_0742; -.
DR   EnsemblBacteria; ABS60597; ABS60597; Fnod_0742.
DR   KEGG; fno:Fnod_0742; -.
DR   eggNOG; COG2518; Bacteria.
DR   HOGENOM; CLU_055432_2_0_0; -.
DR   OMA; TISAIHM; -.
DR   OrthoDB; 1948290at2; -.
DR   Proteomes; UP000002415; 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..199
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_0000351858"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   199 AA;  22484 MW;  DE7ADCEF61495CBD CRC64;
     MLFEHLQYYG VSRKIIEAMN KVDRKLFVPS ELQESAYLDI PLPIGYGQTI SAPHMVGMMC
     EYLELKDGDR VLEIGTGSGY NAAVMSLLVG ESGWIYTIER IPELVQEAQK RINLLGINNI
     TIIVGDGKEG LEEYAPFDKI TVTCYAKHIP KKLIEQLKDN GIMVIPVGNE YVQILKLIRK
     SGEKIIEEDL THVRFVPMQ