PIMT_PYRAE
ID PIMT_PYRAE Reviewed; 205 AA.
AC Q8ZYN0;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=PAE0701;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL62963.1; -; Genomic_DNA.
DR PDB; 4O29; X-ray; 2.90 A; A=1-205.
DR PDBsum; 4O29; -.
DR AlphaFoldDB; Q8ZYN0; -.
DR SMR; Q8ZYN0; -.
DR STRING; 178306.PAE0701; -.
DR EnsemblBacteria; AAL62963; AAL62963; PAE0701.
DR KEGG; pai:PAE0701; -.
DR PATRIC; fig|178306.9.peg.508; -.
DR eggNOG; arCOG00976; Archaea.
DR HOGENOM; CLU_055432_2_0_2; -.
DR InParanoid; Q8ZYN0; -.
DR OMA; TISAIHM; -.
DR Proteomes; UP000002439; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..205
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000111922"
FT ACT_SITE 56
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:4O29"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:4O29"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:4O29"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:4O29"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4O29"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:4O29"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:4O29"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:4O29"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:4O29"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:4O29"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:4O29"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:4O29"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 163..175
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:4O29"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:4O29"
SQ SEQUENCE 205 AA; 22887 MW; C32FF6283BB8E7E8 CRC64;
MAKRLVEELE RDGIVKSERV KRALLTVPRE EFVLPEYRMM AYEDRPLPLF AGATISAPHM
VAMMCELIEP RPGMKILEVG TGSGYHAAVC AEAIEKKGRI YTIEIVKELA VFAAQNLERL
GYWGVVEVYH GDGKKGLEKH APFDAIIVTA AADVIPPALI RQLKDGGVMV IPVEERLGQV
LYKVVKRGDK IEKKAITYVM FVPLR
