ID K2KQR6_9GAMM Unreviewed; 211 AA.
AC K2KQR6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=A10D4_04225 {ECO:0000313|EMBL:EKE84789.1};
OS Idiomarina xiamenensis 10-D-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE84789.1, ECO:0000313|Proteomes:UP000014115};
RN [1] {ECO:0000313|EMBL:EKE84789.1, ECO:0000313|Proteomes:UP000014115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-D-4 {ECO:0000313|EMBL:EKE84789.1,
RC ECO:0000313|Proteomes:UP000014115};
RX PubMed=23209204; DOI=10.1128/JB.01855-12;
RA Lai Q., Wang L., Wang W., Shao Z.;
RT "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4.";
RL J. Bacteriol. 194:6938-6938(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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKE84789.1}.
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DR EMBL; AMRG01000004; EKE84789.1; -; Genomic_DNA.
DR RefSeq; WP_008487943.1; NZ_AMRG01000004.1.
DR AlphaFoldDB; K2KQR6; -.
DR STRING; 740709.A10D4_04225; -.
DR PATRIC; fig|740709.3.peg.854; -.
DR eggNOG; COG2518; Bacteria.
DR OrthoDB; 9810066at2; -.
DR Proteomes; UP000014115; Unassembled WGS sequence.
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:EKE84789.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014115};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:EKE84789.1}.
FT ACT_SITE 62
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ SEQUENCE 211 AA; 23459 MW; 8A2354DC4EEAE868 CRC64;
MINNYWGMAK RLVQLLVAQG ISNQRVLDII ESTPRHQFMP ESLAHQAYEN TALPIGKGQT
ISQPLMVATM TQLLLQHDCQ KVLEIGTGSG YQTAVLAQLV ERVFSVERIA ALQYQAKRRL
KQLDLHNVAM RHGDGWEGWS SKAPFDGIIV TAAAARVPEA LLQQLADGGV MILPVGEQQQ
SLYVVRRFGD NFEQQRIGDV KFVPLVKGTL L
//
