ID A0A0G3LQC8_XANCT Unreviewed; 225 AA.
AC A0A0G3LQC8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=F0H32_11345 {ECO:0000313|EMBL:QEO26711.1}, FD63_10970
GN {ECO:0000313|EMBL:AKK67958.1};
OS Xanthomonas translucens pv. undulosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=487909 {ECO:0000313|EMBL:QEO26711.1, ECO:0000313|Proteomes:UP000324457};
RN [1] {ECO:0000313|Proteomes:UP000035194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xtu4699 {ECO:0000313|Proteomes:UP000035194};
RA Peng Z., Potnis N., Jones J., Liu Z., White F.F., Liu S.;
RT "A complete genome of Xanthomonas translucens and the full TAL effector
RT gene content using long read sequencing.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKK67958.1, ECO:0000313|Proteomes:UP000035194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xtu 4699 {ECO:0000313|EMBL:AKK67958.1}, and Xtu4699
RC {ECO:0000313|Proteomes:UP000035194};
RX PubMed=26729225; DOI=10.1186/s12864-015-2348-9;
RA Peng Z., Hu Y., Xie J., Potnis N., Akhunova A., Jones J., Liu Z.,
RA White F.F., Liu S.;
RT "Long read and single molecule DNA sequencing simplifies genome assembly
RT and TAL effector gene analysis of Xanthomonas translucens.";
RL BMC Genomics 17:21-21(2016).
RN [3] {ECO:0000313|EMBL:QEO26711.1, ECO:0000313|Proteomes:UP000324457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW16 {ECO:0000313|EMBL:QEO26711.1,
RC ECO:0000313|Proteomes:UP000324457};
RA Peng Z., Huguet-Tapia J.C., White F.;
RT "Xanthomonas translucens pv. undulosa LW16.";
RL Submitted (AUG-2019) 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: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; CP008714; AKK67958.1; -; Genomic_DNA.
DR EMBL; CP043540; QEO26711.1; -; Genomic_DNA.
DR RefSeq; WP_003474035.1; NZ_MADU01000115.1.
DR AlphaFoldDB; A0A0G3LQC8; -.
DR STRING; 487909.FD63_10970; -.
DR KEGG; xtn:FD63_10970; -.
DR Proteomes; UP000035194; Chromosome.
DR Proteomes; UP000324457; 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:QEO26711.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:QEO26711.1}.
FT ACT_SITE 75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ SEQUENCE 225 AA; 24334 MW; 9B84A91CBCEDA8C6 CRC64;
MTPRLRLQPE AIGIGMTSQR VRDRLVERLR ESGIRDEAVL NAVRTVPRHL FIDEALASRA
YEDTALPIGH GQTISQPWVV ARMTETVLAA APKKVLEVGT GSGYQAAILA ALGLEVYTVE
RIGDLLRQAR KRLRQLGMNV RSKHDDGRIG WAEHGPYDAI VVTAAAPALV DALVEQLAPG
GCLVAPVGGP SSQSLVRLRR DAEGRIEQDI LAPVSFVPLL SGMLD
//
