ID A0A372K685_9BURK Unreviewed; 443 AA.
AC A0A372K685;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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=D0B32_09685 {ECO:0000313|EMBL:RFU47801.1};
OS Paraburkholderia sp. DHOC27.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2303330 {ECO:0000313|EMBL:RFU47801.1, ECO:0000313|Proteomes:UP000263097};
RN [1] {ECO:0000313|EMBL:RFU47801.1, ECO:0000313|Proteomes:UP000263097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOC27 {ECO:0000313|EMBL:RFU47801.1,
RC ECO:0000313|Proteomes:UP000263097};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOC27, isolated from subtropical forest soil.";
RL Submitted (AUG-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:RFU47801.1}.
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DR EMBL; QVQV01000002; RFU47801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372K685; -.
DR OrthoDB; 9810066at2; -.
DR Proteomes; UP000263097; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF0; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR Pfam; PF01135; PCMT; 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:RFU47801.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000263097};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:RFU47801.1}.
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 290
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ SEQUENCE 443 AA; 45651 MW; 2971D59C51C662E4 CRC64;
MTNGRAKRFP LGLEDLVREP RRPEGRPGEV RAANLAAAAE ARANAARAKS PGRGGEGGAG
RSVARDAGKA PSQNAAKTVG NVGVSSGLKP NVQSGGPAGG GKAAGVTAGS TSASKPAGTS
SVKPAAPSAV KPTVTSGAKS LATSPVKPAI ALATKPAAGA AARPSVTAPG HPKTQPKAQP
LGPTSNQQAN RPALTPVMTR PVASKSTERS ATLNVAPMMA PNVALNGAQA LTSERIRERM
VDRLRANGIT DQRVIHAMSV VPRHMFVDPG LATQAYEDAA LPIGHHQTIS KPSVVARMIE
LAAHGRPLAN VLEIGTGCGY QAAVLSQVAR DVYSIERIKP LYERAKTNLR PLRIPNIRLH
YGDGRIGLPA VAPFDAIVIA AAGLDVPQAL LEQLAIGGRL VAPVGAQDGQ TQVLTLVERT
GPAQWRESRL DRVFFVPLKS GVI
//
