PIMT1_NITOC
ID PIMT1_NITOC Reviewed; 213 AA.
AC Q3JCZ3;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Noc_0790;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA57303.1; -; Genomic_DNA.
DR RefSeq; WP_002808840.1; NC_007484.1.
DR AlphaFoldDB; Q3JCZ3; -.
DR SMR; Q3JCZ3; -.
DR STRING; 323261.Noc_0790; -.
DR EnsemblBacteria; ABA57303; ABA57303; Noc_0790.
DR KEGG; noc:Noc_0790; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_6; -.
DR OMA; TISAIHM; -.
DR OrthoDB; 1948290at2; -.
DR Proteomes; UP000006838; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..213
FT /note="Protein-L-isoaspartate O-methyltransferase 1"
FT /id="PRO_0000351885"
FT ACT_SITE 64
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ SEQUENCE 213 AA; 23298 MW; A18277E4615BAB7D CRC64;
MGMTSRRARE RERLIQRLHE EGIRDPAVLK VIQETPRHIF VDEALSSRAY EDTALPIGFR
QTISQPYIVA RMTEALLAGG SLQKVLEVGT GSGYQTAILA GLAGLVYTVE RIKPLLTQAQ
ARFKHLGISN IRAKCADGLW GWPAYGPYQG ILVAAAPREI PQTLLKQLAV GGRMVIPVGA
SSGTQSLMIV TRTADDFEMK TLERVSFVPL VGE