PIMT_XANP2
ID PIMT_XANP2 Reviewed; 219 AA.
AC A7INP1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Xaut_4414;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
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; CP000781; ABS69635.1; -; Genomic_DNA.
DR RefSeq; WP_012116384.1; NC_009720.1.
DR AlphaFoldDB; A7INP1; -.
DR SMR; A7INP1; -.
DR STRING; 78245.Xaut_4414; -.
DR EnsemblBacteria; ABS69635; ABS69635; Xaut_4414.
DR KEGG; xau:Xaut_4414; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_5; -.
DR OMA; HYGDGML; -.
DR OrthoDB; 1948290at2; -.
DR PhylomeDB; A7INP1; -.
DR Proteomes; UP000002417; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..219
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000351950"
FT ACT_SITE 66
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 219 AA; 23549 MW; 506090C53073234D CRC64;
MSTGESEGEQ AERMAFILGL RQRGIRDVGV LRAMELVPRP LFVDPALRRH AYDDVALPIA
CGQTMSQPSL VAAMTEALSL TADHSVLEVG TGSGYHAAVL SHLAARVVTV DRYRSLVAEA
QARFEVLGLR NVTAYVGDGT LGMPARAPFD RILVTAAAPD IPFALIDQLK FGGVIVMPLG
APEEIQTLVR YVKEQSGRTR TELMKVRFVP LIPGAAATL