PIMT_YERPB
ID PIMT_YERPB Reviewed; 208 AA.
AC B2K581;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=YPTS_0808;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) 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; CP001048; ACC87792.1; -; Genomic_DNA.
DR RefSeq; WP_002209395.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K581; -.
DR SMR; B2K581; -.
DR GeneID; 66842805; -.
DR KEGG; ypb:YPTS_0808; -.
DR PATRIC; fig|502801.10.peg.139; -.
DR OMA; TISAIHM; -.
DR BioCyc; YPSE502801:YPTS_RS04170-MON; -.
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..208
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000351963"
FT ACT_SITE 59
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 208 AA; 23432 MW; 962417DFAA32A225 CRC64;
MVNKRMQTLL MQLRQQGIHD ERLLQAIEAV PRERFVDEAL AHKAYENTAL PIGAGQTISQ
PYMVARMTEL LQLTPTSRVL EIGTGSGYQT AILAHLVDHV CSVERIKGLQ WQAKRRLKQL
DLHNVSTRHG DGWLGWQSRG PFDAIIVTAA PPEIPDALLE QLDEGGILVL PVGEQFQTLK
YVQRRNNEYH IETVEAVRFV PLVKGELA