ID A0A328ALS9_9CAUL Unreviewed; 666 AA.
AC A0A328ALS9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DJ017_15950 {ECO:0000313|EMBL:RAK55892.1};
OS Phenylobacterium soli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=2170551 {ECO:0000313|EMBL:RAK55892.1, ECO:0000313|Proteomes:UP000249254};
RN [1] {ECO:0000313|Proteomes:UP000249254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LX32 {ECO:0000313|Proteomes:UP000249254};
RA Li X.;
RL Submitted (MAY-2018) 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: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:RAK55892.1}.
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DR EMBL; QFYQ01000001; RAK55892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328ALS9; -.
DR OrthoDB; 9810066at2; -.
DR Proteomes; UP000249254; 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; 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.
DR PROSITE; PS01279; PCMT; 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:RAK55892.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249254};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:RAK55892.1}.
FT REGION 212..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 62
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ SEQUENCE 666 AA; 74137 MW; FA64F3ED68B7AD2D CRC64;
MLDFAYARHR MVERQLAARG VGDRQVLDAM GEVPREAFVP DGMEEFAYED SPLPIESGQT
ISQPYIVGLM IQAAGIRPGE RVLEVGAGSG YAAAVMSRIA QAVYAIERHE PLTRLAQSRI
DRLGYDNIHL KTGDGTRGWA DAAPFDAILA AAGGPEVPAA LKAQLAIGGR LVMPVGEEPR
LQRLKKLTRI SQAEFREEDL GEVTFVPLIG EQGWGEDEQR RPPEPRSFRA PSPAASIPKL
IAHAAEPLPD LDDPAFGALF DRFAKAKVVL LGEASHGTSE FYRARAAITR RLIEHHGFKI
VAVEADWPDA AHFDRYVRHL PPPKHDEPPF RRFPTWMWRN AEVEGFIEGL REWNLARAPD
ARAGFYGLDL YNLSASIRAV LDYLDRVDPQ AGDIARQRYG CLTPWAKNPQ SYGRMALSAG
YRACEEGVVR TLTELLGNRP EYVKADGTAF LDAMGNARLV KNAEAYYRAM YYGSAESWNL
RDTHMFETLC SILDSQGPDA KAVVWAHNSH IGDASKTEMG TEREELNIGQ LCRERFGAEA
ALIGFGTHAG TVACASDWDE PMEVKPVNAS LPDSYERLAH EAGVGRFLLD LREGAHDELR
HRLLEPRLER FIGVIYRPET ERWSHYVACS LPQQFDAYVW FDETTAVKPL LTEARPGAEE
TYPFGL
//