ID   PIMT2_SYNFM             Reviewed;         247 AA.
AC   A0LM89;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Sfum_2864;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
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., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
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; CP000478; ABK18541.1; -; Genomic_DNA.
DR   RefSeq; WP_011699706.1; NC_008554.1.
DR   AlphaFoldDB; A0LM89; -.
DR   SMR; A0LM89; -.
DR   STRING; 335543.Sfum_2864; -.
DR   EnsemblBacteria; ABK18541; ABK18541; Sfum_2864.
DR   KEGG; sfu:Sfum_2864; -.
DR   eggNOG; COG2518; Bacteria.
DR   HOGENOM; CLU_055432_2_0_7; -.
DR   OMA; MVDTQVR; -.
DR   OrthoDB; 1948290at2; -.
DR   Proteomes; UP000001784; 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..247
FT                   /note="Protein-L-isoaspartate O-methyltransferase 2"
FT                   /id="PRO_0000351945"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   247 AA;  26797 MW;  B4D30E32216DDF67 CRC64;
     MSRKSTGAFL VILLLSMAAG GAVGAADDPY GAARAKMVRE IEEDARRTSE RIGKTALDPR
     VMEIMARVPR HEFVPAAERA YAYENRPLPI GYGQTISQPY IVAVMTDLLK VGSESTVLEV
     GTGSGYQAAI LAEFVRSVYS IEIIEALAET AAERLKRLGY DNVRVRTGDG YHGWKEHAPF
     DGIVVTAAAG HIPPPLLDQL KPGGRMIIPV GGPFFVQQLM LVEKDEQGRT RTRQILPVAF
     VPLTGGH