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Reviewed, UniProtKB/Swiss-Prot Q7N8K3 (PIMT_PHOLL)

Last modified June 16, 2009. Version 34. 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: plu0717
OrganismPhotorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]
Taxonomic identifier141679 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length208 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 – 208208Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090
PRO_0000111895

Sites

Active site591 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N8K3-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 5223D7B1A6FB66A4

FASTA20823,157
        10         20         30         40         50         60 
MLSRAMKNLL TQLRQQGIED ERLLAAISAV PRERFVDEAL AHKAYENTAL PIGYGQTISQ 

        70         80         90        100        110        120 
PYIVARMTEL LQLTPDAKIL EIGTGSGYQT AILAHLVKHV FSVERIKGLQ WQAKRRLKQL 

       130        140        150        160        170        180 
DLHNVSTRHG DGWQGWPSRG LFDAIIVTAA PPYIPQELML QLTDGGVMVL PVGEHTQILK 

       190        200 
SVKRHGNGFH SEVIEAVRFV PLVQGELA 

« Hide

Cross-references

Sequence databases

BX571861 Genomic DNA. Translation: CAE13012.1.
RefSeqNP_928062.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2800680.
GenomeReviewsGene locus plu0717 in contig BX470251_GR.
KEGGplu:plu0717.
NMPDRfig|243265.1.peg.686.

Organism-specific databases

PhotoListplu0717.
CMRSearch...

Phylogenomic databases

HOGENOMQ7N8K3.
OMAQ7N8K3. KELNYAN.

Enzyme and pathway databases

BioCycPLUM243265:PLU0717-MON.
BRENDA2.1.1.77. 308689.

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_PHOLL
AccessionPrimary (citable) accession number: Q7N8K3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: December 15, 2003
Last modified: June 16, 2009
This is version 34 of the entry and version 1 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