Q43209 (PIMT_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein-L-isoaspartate O-methyltransferase
Short name=PIMT
EC=2.1.1.77

Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl methyltransferase
Protein-beta-aspartate methyltransferase

Gene names

Name:

PCM

Organism

Triticum aestivum (Wheat)

Taxonomic identifier

4565 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Protein existence	Evidence 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 methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 230	230	Protein-L-isoaspartate O-methyltransferase		PRO_0000111883
Sites
	Active site	65	1	By similarity
Natural variations
	Natural variant	18	1	E → D.
	Natural variant	41	1	A → N.
	Natural variant	52	1	T → N.
	Natural variant	54	1	S → L.
	Natural variant	122	1	V → A.
	Natural variant	143	1	S → L.
	Natural variant	147	1	S → E.
	Natural variant	156	1	A → V.
	Natural variant	203	1	A → S.
	Natural variant	208	1	S → T.
	Natural variant	210	1	R → V.
	Natural variant	214	1	S → T.

Sequences

	Sequence		Length	Mass (Da)
	Q43209 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7B600453B4B56C35	FASTA	230	24,708
	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

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07941 mRNA. Translation: AAA34297.1.
PIR	T06519.
UniGene	Ta.162.
3D structure databases
ProteinModelPortal	Q43209.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	Q43209.
Family and domain databases
InterPro	IPR000682. PCMT. [Graphical view]
PANTHER	PTHR11579. PCMT. 1 hit.
Pfam	PF01135. PCMT. 1 hit. [Graphical view]
TIGRFAMs	TIGR00080. Pimt. 1 hit.
PROSITE	PS01279. PCMT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PIMT_WHEAT

Accession

Primary (citable) accession number: Q43209

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program