ID M2SG29_9SPHN Unreviewed; 663 AA.
AC M2SG29;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE EC=2.1.1.77 {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE Short=PIMT {ECO:0000256|HAMAP-Rule:MF_00090};
GN Name=pcm {ECO:0000256|HAMAP-Rule:MF_00090};
GN ORFNames=C725_0245 {ECO:0000313|EMBL:EMD84315.1};
OS Pacificimonas flava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Pacificimonas.
OX NCBI_TaxID=1234595 {ECO:0000313|EMBL:EMD84315.1, ECO:0000313|Proteomes:UP000011717};
RN [1] {ECO:0000313|EMBL:EMD84315.1, ECO:0000313|Proteomes:UP000011717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2015 {ECO:0000313|EMBL:EMD84315.1,
RC ECO:0000313|Proteomes:UP000011717};
RX PubMed=23661488;
RA Tang K., Liu K., Li S., Jiao N.;
RT "Draft Genome Sequence of Strain JLT2015T, Belonging to the Family
RT Sphingomonadaceae of the Alphaproteobacteria.";
RL Genome Announc. 1:E00226-13(2013).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00090};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|HAMAP-Rule:MF_00090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMD84315.1}.
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DR EMBL; AMRV01000001; EMD84315.1; -; Genomic_DNA.
DR RefSeq; WP_008599636.1; NZ_JACHGC010000002.1.
DR AlphaFoldDB; M2SG29; -.
DR PATRIC; fig|1234595.3.peg.244; -.
DR OrthoDB; 9810066at2; -.
DR Proteomes; UP000011717; Unassembled WGS sequence.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd14728; Ere-like; 1.
DR Gene3D; 1.20.1440.30; Biosynthetic Protein domain; 1.
DR Gene3D; 3.40.1660.10; EreA-like (biosynthetic domain); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR007815; Emycin_Estase.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR31299; ESTERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05850)-RELATED; 1.
DR PANTHER; PTHR31299:SF0; PRIBOSYLTRAN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05139; Erythro_esteras; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF159501; EreA/ChaN-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090,
KW ECO:0000313|EMBL:EMD84315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011717};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:EMD84315.1}.
FT ACT_SITE 62
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ SEQUENCE 663 AA; 74319 MW; 5ACFC8BCDA158044 CRC64;
MTDYKARRQR MVEQQLQRRG ISDPSVLDAM RDVPREAFVS EDMAEFAYED SPLPIEEKQT
ISQPYIVARM VEAAEIRPGN RVLEVGAGSG YAAAVIGRIA GEVHAIERQE RLAELARQRL
HRLGYQQVHV HVGDGTKGRP EAAPFDAILV AAGGPKIPDS LRAQLAIGGR LVMPVGDRPQ
MLTKVTRTGQ DKFEEEDLGA VTFVPLIGEE GWVENGSRSA SNHKPTASGQ RSLSELVADA
AEPLPDFDDP AFGKMFDRWA DKRVVLLGEA SHGTHEFYAA RAAITRHLIE HHGFSIVAVE
ADWPDAAQID RYVRHRPPGP FDGPPFERFP SWMWRNTDIA DLTAWMRAHN AGLDSDRRAG
FYGLDMYNMR GSISAVLDYL DEVDQEAAAV ARERYGCLTP WQNDPAVYGR AVLTSQYRKC
EQAVVEQCRA ILQKQLDYEG QDGESFLDAA QNARLIASAE RYYRIMYYGG AESWNLRDTH
MFETLENLLA SKGPEAKAIV WAHNSHIGDA RATDMGNVRG EHNIGQLCRE QWGDEAALLG
FGTHTGTVAA ATDWDGEMET KAVRPSRPDS YERVCHDSGR SRFLLDLSEG RHEALRRRLN
EPRLERFIGV IYRPETERQS HYSRAILPQQ FDGYVWFDET AAITPLTPEH HPEGVPDTYP
FGL
//
