PIMT_PYRFU
ID PIMT_PYRFU Reviewed; 219 AA.
AC Q8TZR3;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=PF1922;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=11700066; DOI=10.1006/jmbi.2001.5095;
RA Griffith S.C., Sawaya M.R., Boutz D.R., Thapar N., Katz J.E., Clarke S.,
RA Yeates T.O.;
RT "Crystal structure of a protein repair methyltransferase from Pyrococcus
RT furiosus with its L-isoaspartyl peptide substrate.";
RL J. Mol. Biol. 313:1103-1116(2001).
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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=AAL82046.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009950; AAL82046.1; ALT_INIT; Genomic_DNA.
DR PDB; 1JG1; X-ray; 1.20 A; A=1-219.
DR PDB; 1JG2; X-ray; 1.50 A; A=1-219.
DR PDB; 1JG3; X-ray; 2.10 A; A/B=1-219.
DR PDB; 1JG4; X-ray; 1.50 A; A=1-219.
DR PDBsum; 1JG1; -.
DR PDBsum; 1JG2; -.
DR PDBsum; 1JG3; -.
DR PDBsum; 1JG4; -.
DR AlphaFoldDB; Q8TZR3; -.
DR SMR; Q8TZR3; -.
DR STRING; 186497.PF1922; -.
DR EnsemblBacteria; AAL82046; AAL82046; PF1922.
DR KEGG; pfu:PF1922; -.
DR PATRIC; fig|186497.12.peg.1993; -.
DR eggNOG; arCOG00976; Archaea.
DR HOGENOM; CLU_055432_2_0_2; -.
DR OMA; TISAIHM; -.
DR PhylomeDB; Q8TZR3; -.
DR BRENDA; 2.1.1.77; 5243.
DR EvolutionaryTrace; Q8TZR3; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..219
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000111923"
FT ACT_SITE 65
FT /evidence="ECO:0000250"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1JG3"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1JG4"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1JG3"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1JG1"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:1JG1"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:1JG1"
SQ SEQUENCE 219 AA; 24617 MW; A239F32E24C3445D CRC64;
MMDEKELYEK WMRTVEMLKA EGIIRSKEVE RAFLKYPRYL FVEDKYKKYA HIDEPLPIPA
GQTVSAPHMV AIMLEIANLK PGMNILEVGT GSGWNAALIS EIVKTDVYTI ERIPELVEFA
KRNLERAGVK NVHVILGDGS KGFPPKAPYD VIIVTAGAPK IPEPLIEQLK IGGKLIIPVG
SYHLWQELLE VRKTKDGIKI KNHGGVAFVP LIGEYGWKE
