PIMT_SHELP
ID PIMT_SHELP Reviewed; 211 AA.
AC A3QC83;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
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=Shew_1211;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABO23081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000606; ABO23081.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041406509.1; NC_009092.1.
DR AlphaFoldDB; A3QC83; -.
DR SMR; A3QC83; -.
DR STRING; 323850.Shew_1211; -.
DR EnsemblBacteria; ABO23081; ABO23081; Shew_1211.
DR KEGG; slo:Shew_1211; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_6; -.
DR OrthoDB; 1948290at2; -.
DR Proteomes; UP000001558; 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..211
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000351935"
FT ACT_SITE 62
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 211 AA; 22854 MW; 635AB0B9780C8353 CRC64;
MNGVATTAAL NLARHLQGAG ITNAEVLAVV AKTPRELFLD AALGHKAYEN TALPIGQGQT
ISQPYIVARM TELLLESRPK RVLEIGTGSG YQAAILAQLV DELCTVERIK SLQIQARQRL
KRLDLHNVSF KYGDGWQGWA NKGPFDAIMV TAAASSVPQA LLQQLADGGV LVIPVGEETQ
QLMRVVRMGD QFHSQTIEMV KFVPLVNGEL A