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Reviewed, UniProtKB/Swiss-Prot Q88MF0 (PIMT_PSEPK)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-L-isoaspartate O-methyltransferase
    EC=2.1.1.77
Alternative name(s):
    Protein-beta-aspartate methyltransferase
      Short name=PIMT
    Protein L-isoaspartyl methyltransferase
    L-isoaspartyl protein carboxyl methyltransferase
Gene names
Name: pcm
Ordered Locus Names: PP_1621
OrganismPseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]
Taxonomic identifier160488 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins By similarity.

Catalytic activity

S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. HAMAP MF_00090

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein modification process

Inferred from electronic annotation. Source: HAMAP

protein repair

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090
PRO_0000111898

Sites

Active site601 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88MF0-1 [UniParc].

Last modified November 14, 2003. Version 2.
Checksum: F9E929C5BFDB3E4D

FASTA21223,469
        10         20         30         40         50         60 
MTSQRTRERL IQRLCEEGVS NTKVLDVIRR TPRHLFVDEA LAHRAYEDTA LPIGHNQTIS 

        70         80         90        100        110        120 
QPFMVAHMSE LLLEAGPLDK VLEIGTGSGY QTAILAQLVE RVFSVERIKV LQDRAKERLV 

       130        140        150        160        170        180 
ELNLRNVVFR WGDGCEGWPA LAPYNGIIVT AVAPEVPQAL LDQLAPGGRM VIPVGPAGEA 

       190        200        210 
QQLMLIVREE HGFSRRVLGA VRFVPLLNGP LA 

« Hide

Cross-references

Sequence databases

AE015451 Genomic DNA. Translation: AAN67242.1. Different initiation.
RefSeqNP_743778.1.

3D structure databases

HSSPHSSP built from PDB template 1KR5 based on UniProtKB P22061.
ModBaseSearch...

Genome annotation databases

GeneID1044857.
GenomeReviewsGene locus PP_1621 in contig AE015451_GR.
KEGGppu:PP_1621.
NMPDRfig|160488.1.peg.1608.
TIGRPP_1621.

Phylogenomic databases

HOGENOMQ88MF0.

Enzyme and pathway databases

BioCycPPUT160488:PP_1621-MON.

Family and domain databases

HAMAPMF_00090.
[Tree]
InterProIPR000682. PCMT.
[Graphical view]
PANTHERPTHR11579. PCMT. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
TIGRFAMsTIGR00080. pimt. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIMT_PSEPK
AccessionPrimary (citable) accession number: Q88MF0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: June 16, 2009
This is version 37 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents