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Database: UniProt
Entry: A0A1H9K656_9PROT
LinkDB: A0A1H9K656_9PROT
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ID   A0A1H9K656_9PROT        Unreviewed;       254 AA.
AC   A0A1H9K656;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN05421690_100418 {ECO:0000313|EMBL:SEQ94413.1};
OS   Nitrosomonas sp. Nm51.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=133720 {ECO:0000313|EMBL:SEQ94413.1, ECO:0000313|Proteomes:UP000198732};
RN   [1] {ECO:0000313|EMBL:SEQ94413.1, ECO:0000313|Proteomes:UP000198732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm51 {ECO:0000313|EMBL:SEQ94413.1,
RC   ECO:0000313|Proteomes:UP000198732};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOGH01000004; SEQ94413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9K656; -.
DR   STRING; 133720.SAMN05421690_100418; -.
DR   Proteomes; UP000198732; 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:SEQ94413.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198732};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:SEQ94413.1}.
FT   ACT_SITE        104
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   254 AA;  28413 MW;  9702AE748A8E00CE CRC64;
     MKENLMNHFI FKQFFLLWIV LFNAFFISSA VRAEDFYAVK RAQMIKAIEA DVRTGYGNLA
     KKELDENVIK ALNTVPRHEF VPKKLQQSAY DNRPLPIGHG QTISQPYIVA IMTNLLGVGK
     NDRILEIGTG SGYQIAVLAE LVNKAYSIEI IEPLGKEAKA RLQRLGYDNI SLKIGDGYYG
     WEEHAPFDAI IVTAAASHIP PPLIQQLRPG GRMLIPVGSR FMVQELLLVE KTEEGKISTQ
     QLLPVAFVPL TGKH
//
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