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Database: UniProt
Entry: I9UNU2_HELPX
LinkDB: I9UNU2_HELPX
Original site: I9UNU2_HELPX 
ID   I9UNU2_HELPX            Unreviewed;       209 AA.
AC   I9UNU2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ECO:0000313|EMBL:EJB81824.1};
GN   ORFNames=HPHPH3_0560 {ECO:0000313|EMBL:EJB81824.1};
OS   Helicobacter pylori Hp H-3.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992059 {ECO:0000313|EMBL:EJB81824.1, ECO:0000313|Proteomes:UP000004029};
RN   [1] {ECO:0000313|EMBL:EJB81824.1, ECO:0000313|Proteomes:UP000004029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hp H-3 {ECO:0000313|EMBL:EJB81824.1,
RC   ECO:0000313|Proteomes:UP000004029};
RX   PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA   Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA   Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA   Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT   "Genome sequences of 65 Helicobacter pylori strains isolated from
RT   asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT   disease, or gastritis.";
RL   Pathog. Dis. 68:39-43(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:EJB81824.1}.
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DR   EMBL; AKOX01000003; EJB81824.1; -; Genomic_DNA.
DR   RefSeq; WP_001084552.1; NZ_AKOX01000003.1.
DR   AlphaFoldDB; I9UNU2; -.
DR   PATRIC; fig|992059.3.peg.540; -.
DR   Proteomes; UP000004029; 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:EJB81824.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:EJB81824.1}.
FT   ACT_SITE        59
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   209 AA;  23904 MW;  9E27247499C02227 CRC64;
     MNSIKNHLMC EEIHKRFNLH PKVRKAMESI EREVFVPAPF KHFAYTLNAL SMQAQQYISS
     PLTVAKMTQY LEIDHVDSVL EIGCGSGYQA AVLSQIFRRV FSIERIESLY IEARLRLKTL
     GLDNVHVKFA DGNKGWDQYA PYDRILFSAC AKNIPRALID QLEEGGILVA PIQENNEQVI
     KRFVKQNNAL RVQKVLEKCL FVPVVDGVQ
//
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