PIMT_VIBC3
ID PIMT_VIBC3 Reviewed; 208 AA.
AC A5F9C1; C3LX58;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN OrderedLocusNames=VC0395_A0060, VC395_0549;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ21782.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP08568.1; -; Genomic_DNA.
DR RefSeq; WP_000002982.1; NZ_JAACZH010000029.1.
DR PDB; 4L7V; X-ray; 2.05 A; A=1-208.
DR PDBsum; 4L7V; -.
DR AlphaFoldDB; A5F9C1; -.
DR SMR; A5F9C1; -.
DR STRING; 345073.VC395_0549; -.
DR EnsemblBacteria; ABQ21782; ABQ21782; VC0395_A0060.
DR KEGG; vco:VC0395_A0060; -.
DR KEGG; vcr:VC395_0549; -.
DR PATRIC; fig|345073.21.peg.539; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_6; -.
DR OMA; TISAIHM; -.
DR BRENDA; 2.1.1.77; 15862.
DR Proteomes; UP000000249; Chromosome 2.
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; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..208
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_1000071256"
FT ACT_SITE 59
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:4L7V"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:4L7V"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:4L7V"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:4L7V"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4L7V"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4L7V"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:4L7V"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4L7V"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:4L7V"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4L7V"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:4L7V"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4L7V"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:4L7V"
FT STRAND 162..185
FT /evidence="ECO:0007829|PDB:4L7V"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:4L7V"
SQ SEQUENCE 208 AA; 22862 MW; 9D88EE538B5DA30E CRC64;
MANPKADRLI QFLTEQGITS PQVLAAIHAL PREFFVAPAM MHQAYDNNAL PIGQGQTISQ
PYIVAKMTEL LALTPETKVL EIGTGSGYQT AVLAKLVNHV FTVERIKTLQ WDAKRRLKQL
DIYNVSTKHG DGWQGWPARG PFDAILVTAA AAKVPQSLLD QLAEGGRMVI PVGEDEQYLY
KIVRQGGQFI SERVEAVRFV PLVAGDLA
