PIMT2_GEOUR
ID PIMT2_GEOUR Reviewed; 217 AA.
AC A5G4S7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Gura_2618;
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
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 Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-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; CP000698; ABQ26795.1; -; Genomic_DNA.
DR AlphaFoldDB; A5G4S7; -.
DR SMR; A5G4S7; -.
DR STRING; 351605.Gura_2618; -.
DR EnsemblBacteria; ABQ26795; ABQ26795; Gura_2618.
DR KEGG; gur:Gura_2618; -.
DR HOGENOM; CLU_055432_2_0_7; -.
DR OMA; TISAIHM; -.
DR Proteomes; UP000006695; 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..217
FT /note="Protein-L-isoaspartate O-methyltransferase 2"
FT /id="PRO_0000351863"
FT ACT_SITE 62
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 217 AA; 23637 MW; 0C77D6C487B136E3 CRC64;
MINLDIARRR MVENQIVARG IKDRRVIDAM LKVPRHIFVE EAMSAQAYSD SSLPIGEKQT
ISQPYMVALM SGMLQLTGKE KVLELGTGSG YQAAILAELA DRVYTVERIR PLALRARKAL
DSLGYLNVNL KIGDGTDGWA SEAPFDAILV TAGAPDVPMH LIDQLAVGGK LVIPVGNQSE
QTLVRITKGE NGAVSREDSI GCRFVKLIGR YGWSGED