ID   PIMT_PYRAB              Reviewed;         216 AA.
AC   Q9UXX0; G8ZKS0;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   03-AUG-2022, entry version 121.
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; OrderedLocusNames=PYRAB17380; ORFNames=PAB1206;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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 (By similarity).
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB50643.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248288; CAB50643.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE71211.1; -; Genomic_DNA.
DR   PIR; E75025; E75025.
DR   RefSeq; WP_048147186.1; NC_000868.1.
DR   AlphaFoldDB; Q9UXX0; -.
DR   SMR; Q9UXX0; -.
DR   STRING; 272844.PAB1206; -.
DR   PRIDE; Q9UXX0; -.
DR   EnsemblBacteria; CAB50643; CAB50643; PAB1206.
DR   GeneID; 1496040; -.
DR   KEGG; pab:PAB1206; -.
DR   PATRIC; fig|272844.11.peg.1856; -.
DR   eggNOG; arCOG00976; Archaea.
DR   HOGENOM; CLU_055432_2_0_2; -.
DR   OrthoDB; 88476at2157; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..216
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_0000111921"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24321 MW;  A3BE8A6D727C2F78 CRC64;
     MDLYERWKRT VEMLEREGII RSLEVKEAFL KYPRYMFVED RYKSYAHIDE PLPIPAGQTV
     SAPHMVAIML EIAKLKEGMN VLEVGTGSGW NAALISYIVK TDVYSIERIP ELVEFAKRNL
     ERAGVKNVHV ILGDGSKGFP PKAPYDVIIV TAGAPKVPEP LVEQLKPGGR LIIPVGSYHL
     WQELLEVVKK KSGEIKVRNH GGVAFVPLIG EYGWRE