Reviewed, UniProtKB/Swiss-Prot Q2NVM1 (PIMT_SODGM)

Names and origin

Protein names

Recommended 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:	SG0529

Organism

Sodalis glossinidius (strain morsitans) [Complete proteome] [HAMAP]

Taxonomic identifier

343509 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Sodalis

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: HAMAP protein repair Inferred from electronic annotation. Source: HAMAP
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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 208	208	Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090		PRO_1000004829
Sites
	Active site	59	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2NVM1-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: 49639535825F18CD	FASTA	208	23,338
	10 20 30 40 50 60 MVDVRTQTLL AQLRQQGIRD ERLLQAMEAV PREHFIDEAF EHKAYDNTAL PIGLGQTISQ 70 80 90 100 110 120 PYIVARMTEL LALWPESRVL EIGTGSGYQT AILAHLVKHV CSVERIKKLQ WQAKRRLKLL 130 140 150 160 170 180 DLHNISTRHG DGWQGWLSRG PFDAIIVTAA PPEIPQALMA QLDEGGVMVL PVGDEQQHLT 190 200 RVRRKGGEFV VDTVEAVRFV PLVKGELA

References

[1]

"Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host." Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S. Genome Res. 16:149-156(2006) [PubMed: 16365377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP008232 Genomic DNA. Translation: BAE73804.1.
RefSeq	YP_454209.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3868230.
GenomeReviews	Gene locus SG0529 in contig AP008232_GR.
KEGG	sgl:SG0529.
NMPDR	fig|343509.6.peg.1189.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2NVM1.
OMA	Q2NVM1. YMVARMS.
Enzyme and pathway databases
BioCyc	SGLO343509:SG0529-MON.
Family and domain databases
HAMAP	MF_00090. [Tree]
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_SODGM

Accession

Primary (citable) accession number: Q2NVM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 7, 2006
Last modified:	June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)