PIMT1_SYNFM
ID PIMT1_SYNFM Reviewed; 214 AA.
AC A0LL58;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein L-isoaspartyl methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein-beta-aspartate methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00090};
DE Short=PIMT 1 {ECO:0000255|HAMAP-Rule:MF_00090};
GN Name=pcm1 {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=Sfum_2480;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK18160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LL58; -.
DR SMR; A0LL58; -.
DR STRING; 335543.Sfum_2480; -.
DR EnsemblBacteria; ABK18160; ABK18160; Sfum_2480.
DR KEGG; sfu:Sfum_2480; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_7; -.
DR OMA; DGNKGWE; -.
DR Proteomes; UP000001784; 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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..214
FT /note="Protein-L-isoaspartate O-methyltransferase 1"
FT /id="PRO_0000351944"
FT ACT_SITE 62
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 214 AA; 23699 MW; 64ED27E11530CAC9 CRC64;
MINFQKARDR MVETQLVSRG IHDRRVLEAM RKVPRHLFVD EALKEQAHSD HPLPIGDKQT
ISQPYIVALM TQSLELQGHE KILEIGTGSG YQAAVLAELA ERVFSIERNP NLAYRANQTL
QKLGYKNIIV RVADGTLGWP DEAPFDAILV TAGTPKIPQP LLDQLAEGGR LVVPVGDRLA
QELVLVESGP EGMKHTNLGG VRFVDLVGKW GWEG