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Database: UniProt
Entry: D2T5K1_ERWP6
LinkDB: D2T5K1_ERWP6
Original site: D2T5K1_ERWP6 
ID   D2T5K1_ERWP6            Unreviewed;       218 AA.
AC   D2T5K1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE            EC=2.1.1.77 {ECO:0000256|HAMAP-Rule:MF_00090};
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE            Short=PIMT {ECO:0000256|HAMAP-Rule:MF_00090};
GN   Name=pcm {ECO:0000256|HAMAP-Rule:MF_00090,
GN   ECO:0000313|EMBL:CAY75432.1};
GN   OrderedLocusNames=EPYR_03052 {ECO:0000313|EMBL:CAY75432.1};
OS   Erwinia pyrifoliae (strain DSM 12163 / CIP 106111 / Ep16/96).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=644651 {ECO:0000313|EMBL:CAY75432.1, ECO:0000313|Proteomes:UP000008690};
RN   [1] {ECO:0000313|Proteomes:UP000008690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12163 / CIP 106111 / Ep16/96
RC   {ECO:0000313|Proteomes:UP000008690};
RX   PubMed=20047678; DOI=10.1186/1471-2164-11-2;
RA   Smits T.H., Jaenicke S., Rezzonico F., Kamber T., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia pyrifoliae
RT   DSM 12163T and comparative genomic insights into plant pathogenicity.";
RL   BMC Genomics 11:2-2(2010).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00090};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|HAMAP-Rule:MF_00090}.
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DR   EMBL; FN392235; CAY75432.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2T5K1; -.
DR   KEGG; epr:EPYR_03052; -.
DR   PATRIC; fig|644651.3.peg.2776; -.
DR   HOGENOM; CLU_055432_2_0_6; -.
DR   OMA; QWHARRR; -.
DR   Proteomes; UP000008690; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00090; PIMT; 1.
DR   InterPro; IPR000682; PCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00080; pimt; 1.
DR   PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11579:SF0; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01279; PCMT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090,
KW   ECO:0000313|EMBL:CAY75432.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:CAY75432.1}.
FT   ACT_SITE        69
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   218 AA;  23870 MW;  FA83868A88237EDC CRC64;
     MAGECRGRQG MVSGRIESLL VQLRLQGIDD ERLLLAIGDV PRARFIDEAF EHKAWENTAL
     PIGSGQTISQ PYMVAKMTSL LALTPASRVL EIGTGSGYQT AILAHLAGHV CSVERIKGLQ
     WQAKRRLKQL DLHNVSTRHG DGWLGWPSRG PFDAIIVTAA PPEIPDALMS QLVDGGIMVL
     PVGEENQVLK RIHRKGDEFI VDTIEPVRFV PLVKGDLA
//
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