ID K0C5R2_CYCSP Unreviewed; 218 AA.
AC K0C5R2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 OrderedLocusNames=Q91_1038 {ECO:0000313|EMBL:AFT67076.1};
OS Cycloclasticus sp. (strain P1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT67076.1, ECO:0000313|Proteomes:UP000006282};
RN [1] {ECO:0000313|EMBL:AFT67076.1, ECO:0000313|Proteomes:UP000006282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:AFT67076.1,
RC ECO:0000313|Proteomes:UP000006282};
RX PubMed=23144416; DOI=10.1128/JB.01837-12;
RA Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT sp. strain P1.";
RL J. Bacteriol. 194:6677-6677(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003230; AFT67076.1; -; Genomic_DNA.
DR RefSeq; WP_015005848.1; NC_018697.1.
DR AlphaFoldDB; K0C5R2; -.
DR STRING; 385025.Q91_1038; -.
DR KEGG; cyq:Q91_1038; -.
DR PATRIC; fig|385025.3.peg.1057; -.
DR HOGENOM; CLU_055432_2_0_6; -.
DR Proteomes; UP000006282; 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.
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:AFT67076.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006282};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:AFT67076.1}.
FT ACT_SITE 68
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ SEQUENCE 218 AA; 24091 MW; 0D3D9E50C515B640 CRC64;
MKDLTGIGMT SQRTRDRLIA HLKELGIKDE RVLSVMRKVP RHLFMAEALS SRAYENTSLP
IGHGQTISQP YMVARMTELL IEDGLPENVL EVGTGSGYQS AILASLIPRV FSVERIRPLQ
EQAKRVLADI GVRNISFKHS DGGWGWKACG PYQAILAAAA PAEIPMNLLE QLTIGARLII
PVGKEGQQVL QRVTRTESAY EVETIEEVSF VPFLKGRA
//
