PIMT_DICTD
ID PIMT_DICTD Reviewed; 220 AA.
AC B8E0T1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {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 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000255|HAMAP-Rule:MF_00090};
DE Short=PIMT {ECO:0000255|HAMAP-Rule:MF_00090};
GN Name=pcm {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=Dtur_1394;
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=515635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310;
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK42668.1; -; Genomic_DNA.
DR RefSeq; WP_012583746.1; NC_011661.1.
DR RefSeq; YP_002353282.1; NC_011661.1.
DR AlphaFoldDB; B8E0T1; -.
DR SMR; B8E0T1; -.
DR STRING; 515635.Dtur_1394; -.
DR EnsemblBacteria; ACK42668; ACK42668; Dtur_1394.
DR KEGG; dtu:Dtur_1394; -.
DR PATRIC; fig|515635.4.peg.1441; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_0; -.
DR InParanoid; B8E0T1; -.
DR OMA; TISAIHM; -.
DR OrthoDB; 1948290at2; -.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IBA:GO_Central.
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..220
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_1000192389"
FT ACT_SITE 68
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 220 AA; 25096 MW; 600D2FBECAFA138C CRC64;
MSFKDFDAPK YKYKRKSLVE ILKNEGIKSQ KVLDAILKVP RHIFVPSEYL DLAYENEALP
IGYEQTISQP YIVALMTEAL DLKGDEKVLE IGTGSGYQTA ILAELAKEVY TIERIRELSE
EAKKRIKLLG YSNVYFKVGD GTLGWEEFSP YDRIIVTAAS YDIPNPLKEQ LKDGGVMVIP
IGGRDFQYLY KITKKNGNFY RENLGGVRFV PLKGEYGWKD
