PIMT_THEMA
ID PIMT_THEMA Reviewed; 317 AA.
AC Q56308;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
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=TM_0704;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8550470; DOI=10.1128/jb.178.2.484-489.1996;
RA Swanson R.V., Sanna M.G., Simon M.I.;
RT "Thermostable chemotaxis proteins from the hyperthermophilic bacterium
RT Thermotoga maritima.";
RL J. Bacteriol. 178:484-489(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9784234; DOI=10.1006/abbi.1998.0830;
RA Ichikawa J.K., Clarke S.;
RT "A highly active protein repair enzyme from an extreme thermophile: the L-
RT isoaspartyl methyltransferase from Thermotoga maritima.";
RL Arch. Biochem. Biophys. 358:222-231(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=11080641; DOI=10.1016/s0969-2126(00)00522-0;
RA Skinner M.M., Puvathingal J.M., Walter R.L., Friedman A.M.;
RT "Crystal structure of protein isoaspartyl methyltransferase. A catalyst for
RT protein repair.";
RL Structure 8:1189-1201(2000).
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.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=164 nmol/min/mg enzyme with KASA (isoD) LAKY as substrate at 85
CC degrees Celsius;
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius. Highly thermostable, with
CC no loss of activity after 60 min at 100 degrees Celsius. Enzyme
CC activity is observed at temperatures as high as 93 degrees Celsius.;
CC -!- SUBUNIT: Monomer.
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; U30501; AAA96385.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35786.1; -; Genomic_DNA.
DR PIR; G72342; G72342.
DR RefSeq; NP_228513.1; NC_000853.1.
DR RefSeq; WP_004081036.1; NZ_CP011107.1.
DR PDB; 1DL5; X-ray; 1.80 A; A/B=1-317.
DR PDBsum; 1DL5; -.
DR AlphaFoldDB; Q56308; -.
DR SMR; Q56308; -.
DR STRING; 243274.THEMA_01145; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR EnsemblBacteria; AAD35786; AAD35786; TM_0704.
DR KEGG; tma:TM0704; -.
DR eggNOG; COG2518; Bacteria.
DR InParanoid; Q56308; -.
DR OMA; ICHIEEN; -.
DR OrthoDB; 1409748at2; -.
DR EvolutionaryTrace; Q56308; -.
DR Proteomes; UP000008183; 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 Gene3D; 3.55.20.10; -; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR009107; PIM_MeTrfase_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF68930; SSF68930; 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..317
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000111905"
FT ACT_SITE 59
FT /evidence="ECO:0000250"
FT HELIX 2..11
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:1DL5"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1DL5"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:1DL5"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1DL5"
SQ SEQUENCE 317 AA; 36400 MW; 2FE6019571ADDF2C CRC64;
MREKLFWILK KYGVSDHIAK AFLEIPREEF LTKSYPLSYV YEDIVLVSYD DGEEYSTSSQ
PSLMALFMEW VGLDKGMRVL EIGGGTGYNA AVMSRVVGEK GLVVSVEYSR KICEIAKRNV
ERLGIENVIF VCGDGYYGVP EFSPYDVIFV TVGVDEVPET WFTQLKEGGR VIVPINLKLS
RRQPAFLFKK KDPYLVGNYK LETRFITAGG NLGNLLERNR KLLREFPFNR EILLVRSHIF
VELVDLLTRR LTEIDGTFYY AGPNGVVEFL DDRMRIYGDA PEIENLLTQW ESCGYRSFEY
LMLHVGYNAF SHISCSI
