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A7ZQI7 (PIMT_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:EcE24377A_3044
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length208 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.

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 – 208208Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090
PRO_1000057598

Sites

Active site591 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZQI7 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: BFA179567527A118

FASTA20823,258
        10         20         30         40         50         60 
MVSRRVQALL DQLRAQGIQD EQVLNALAAV PREKFVDEAF EQKAWDNIAL PIGQGQTISQ 

        70         80         90        100        110        120 
PYMVARMTEL LELTPQSRVL EIGTGSGYQT AILAHLVQHV CSVERIKGLQ WQARRRLKNL 

       130        140        150        160        170        180 
DLHNVSTRHG DGWQGWQARA PFDAIIVTAA PPEIPTALMT QLDEGGILVL PVGEEHQYLK 

       190        200 
RVRRRGGEFI IDTVEAVRFV PLVKGELA 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV20098.1.
RefSeqYP_001464066.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZQI7.
SMRA7ZQI7. Positions 2-208.
ModBaseSearch...

Protein-protein interaction databases

STRING331111.EcE24377A_3044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV20098; ABV20098; EcE24377A_3044.
GeneID5586309.
KEGGecw:EcE24377A_3044.
PATRIC18295394. VBIEscCol31211_3318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
HOGENOMHOG000257189.
KOK00573.
OMASLQWQAR.
ProtClustDBPRK00312.

Enzyme and pathway databases

BioCycECOL331111:GH7P-3080-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_ECO24
AccessionPrimary (citable) accession number: A7ZQI7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: May 1, 2013
This is version 39 of the entry and version 1 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