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Reviewed, UniProtKB/Swiss-Prot Q43209 (PIMT_WHEAT)

Last modified June 16, 2009. Version 52. 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
      Short name=PIMT
    EC=2.1.1.77
Alternative name(s):
    Protein-beta-aspartate methyltransferase
    Protein L-isoaspartyl methyltransferase
    L-isoaspartyl protein carboxyl methyltransferase
Gene names
Name: PCM
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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. This enzyme does not act on D-aspartyl residues.

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Highest contents in seeds.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Protein-L-isoaspartate O-methyltransferase
PRO_0000111883

Sites

Active site651 By similarity

Natural variations

Natural variant181E → D
Natural variant411A → N
Natural variant521T → N
Natural variant541S → L
Natural variant1221V → A
Natural variant1431S → L
Natural variant1471S → E
Natural variant1561A → V
Natural variant2031A → S
Natural variant2081S → T
Natural variant2101R → V
Natural variant2141S → T

Sequences

Sequence LengthMass (Da)Tools
Q43209-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7B600453B4B56C35

FASTA23024,708
        10         20         30         40         50         60 
MAQFWAEGSL EKNNALVEYL KQYGVVRTDK VAEVMETIDR ALFVPEGFTP YTDSPMPIGY 

        70         80         90        100        110        120 
NATISAPHMH ATCLELLKDY LQPGMHALDV GSGSGYLTAC FAMMVGPEGR AVGIEHIPEL 

       130        140        150        160        170        180 
VVASTENVER SAAAALMKDG SLSFHVSDGR LGWPDAAPYD AIHVGAAAPE IPRPLLEQLK 

       190        200        210        220        230 
PGGRMVIPVG TYSQDLQVID KSADGSTSVR NDASVRYVPL TSRSAQLQDS 

« Hide

References

[1]"Characterization of plant L-isoaspartyl methyltransferases that may be involved in seed survival: purification, cloning, and sequence analysis of the wheat germ enzyme."
Mudgett M.B., Clarke S.
Biochemistry 32:11100-11111(1993) [PubMed: 8198620] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: cv. Augusta.

Cross-references

Sequence databases

L07941 mRNA. Translation: AAA34297.1.
PIRT06519.
UniGeneTa.162

3D structure databases

HSSPHSSP built from PDB template 1I1N based on UniProtKB P22061.
ModBaseSearch...

Organism-specific databases

GrameneQ43209.

Enzyme and pathway databases

BRENDA2.1.1.77. 253.

Family and domain databases

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_WHEAT
AccessionPrimary (citable) accession number: Q43209
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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