PIMT1_NITMU
ID PIMT1_NITMU Reviewed; 236 AA.
AC Q2YCR1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE EC=2.1.1.77 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein L-isoaspartyl methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein-beta-aspartate methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE Short=PIMT 1 {ECO:0000255|HAMAP-Rule:MF_00090};
GN Name=pcm1 {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=Nmul_A0151;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) 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:0000255|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:0000255|HAMAP-
CC Rule:MF_00090};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00090}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00090}.
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DR EMBL; CP000103; ABB73460.1; -; Genomic_DNA.
DR RefSeq; WP_011379515.1; NZ_FNVK01000030.1.
DR AlphaFoldDB; Q2YCR1; -.
DR SMR; Q2YCR1; -.
DR STRING; 323848.Nmul_A0151; -.
DR EnsemblBacteria; ABB73460; ABB73460; Nmul_A0151.
DR KEGG; nmu:Nmul_A0151; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_4; -.
DR OMA; DGNKGWE; -.
DR OrthoDB; 1948290at2; -.
DR Proteomes; UP000002718; 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:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00080; pimt; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..236
FT /note="Protein-L-isoaspartate O-methyltransferase 1"
FT /id="PRO_0000351889"
FT ACT_SITE 86
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 236 AA; 25648 MW; 314BB431C45A5DAD CRC64;
MNWQFATAFG ALMYFGCVIP LSAAEYEALR QKMVREVIAA SGNSPPGASV VAAMEKVERH
RFVPAWLSIF AYRNHPLPIG HGQTISQPLI VARMTELLKL KKDDKVLEIG TGSGYQAAVL
AEIAKTVYTI EIIEPLGNEA AGRLQSLGYD NVKTRIGDGY YGWPEAAPFD AILVTAAASH
VPPPLLKQLK PGGRMVVPLG APFMTQYLML VEKQPDGSVT THQIVPVRFV PLRGGH