ID PIMT_METJA Reviewed; 215 AA.
AC Q57636;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE EC=2.1.1.77;
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE AltName: Full=Protein L-isoaspartyl methyltransferase;
DE AltName: Full=Protein-beta-aspartate methyltransferase;
DE Short=PIMT;
GN Name=pcm; OrderedLocusNames=MJ0172;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 (By similarity).
CC {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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; L77117; AAB98157.1; -; Genomic_DNA.
DR PIR; E64321; E64321.
DR RefSeq; WP_010869667.1; NC_000909.1.
DR PDB; 2YXE; X-ray; 2.00 A; A/B=1-215.
DR PDBsum; 2YXE; -.
DR AlphaFoldDB; Q57636; -.
DR SMR; Q57636; -.
DR STRING; 243232.MJ_0172; -.
DR PaxDb; 243232-MJ_0172; -.
DR EnsemblBacteria; AAB98157; AAB98157; MJ_0172.
DR GeneID; 1451019; -.
DR KEGG; mja:MJ_0172; -.
DR eggNOG; arCOG00976; Archaea.
DR HOGENOM; CLU_055432_2_0_2; -.
DR InParanoid; Q57636; -.
DR OrthoDB; 33618at2157; -.
DR PhylomeDB; Q57636; -.
DR EvolutionaryTrace; Q57636; -.
DR Proteomes; UP000000805; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..215
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000111916"
FT ACT_SITE 61
FT /evidence="ECO:0000250"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:2YXE"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 167..190
FT /evidence="ECO:0007829|PDB:2YXE"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:2YXE"
SQ SEQUENCE 215 AA; 23761 MW; E5A8634F2E2BAE8B CRC64;
MDLEEQKKAV IEKLIREGYI KSKRVIDALL KVPREEFLPE HLKEYAYVDT PLEIGYGQTI
SAIHMVGMMC ELLDLKPGMK VLEIGTGCGY HAAVTAEIVG EDGLVVSIER IPELAEKAER
TLRKLGYDNV IVIVGDGTLG YEPLAPYDRI YTTAAGPKIP EPLIRQLKDG GKLLMPVGRY
LQRLVLAEKR GDEIIIKDCG PVAFVPLVGK EGFQG
//
