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Q88MF0 (PIMT_PSEPK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein-L-isoaspartate O-methyltransferase

EC=2.1.1.77
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl methyltransferase
Protein-beta-aspartate methyltransferase
Short name=PIMT
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.
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. HAMAP-Rule MF_00090

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence caution

The sequence AAN67242.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein 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-Rule MF_00090
PRO_0000111898

Sites

Active site601 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88MF0 [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

EMBL
GenBank
DDBJ
AE015451 Genomic DNA. Translation: AAN67242.1. Different initiation.
RefSeqNP_743778.1. NC_002947.3.

3D structure databases

ProteinModelPortalQ88MF0.
ModBaseSearch...

Protein-protein interaction databases

STRING160488.PP_1621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN67242; AAN67242; PP_1621.
GeneID1044857.
KEGGppu:PP_1621.
PATRIC19941468. VBIPsePut30601_1712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
HOGENOMHOG000257189.
KOK00573.
OMASLQWQAR.
ProtClustDBPRK00312.

Enzyme and pathway databases

BioCycPPUT160488:GIXO-1622-MONOMER.

Family and domain databases

HAMAPMF_00090. PIMT.
InterProIPR000682. PCMT.
[Graphical view]
PANTHERPTHR11579. PTHR11579. 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: May 1, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families