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Protein

Protein-L-isoaspartate O-methyltransferase

Gene

pcm

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei59By similarity1

GO - Molecular functioni

  • protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Source: EcoCyc

Keywordsi

Molecular functionMethyltransferase, Transferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:EG10689-MONOMER
MetaCyc:EG10689-MONOMER
BRENDAi2.1.1.77 2026

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:pcm
Ordered Locus Names:b2743, JW2713
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10689 pcm

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001118862 – 208Protein-L-isoaspartate O-methyltransferaseAdd BLAST207

Proteomic databases

PaxDbiP0A7A5
PRIDEiP0A7A5

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4263145, 14 interactors
IntActiP0A7A5, 2 interactors
STRINGi316385.ECDH10B_2911

Structurei

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 15Combined sources12
Helixi21 – 29Combined sources9
Helixi32 – 35Combined sources4
Helixi38 – 43Combined sources6
Beta strandi46 – 48Combined sources3
Helixi61 – 70Combined sources10
Beta strandi78 – 82Combined sources5
Helixi88 – 96Combined sources9
Beta strandi97 – 106Combined sources10
Helixi107 – 119Combined sources13
Beta strandi124 – 130Combined sources7
Helixi132 – 134Combined sources3
Helixi137 – 139Combined sources3
Beta strandi142 – 150Combined sources9
Helixi157 – 160Combined sources4
Beta strandi162 – 172Combined sources11
Beta strandi174 – 176Combined sources3
Beta strandi178 – 185Combined sources8
Beta strandi188 – 196Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LBFX-ray1.80A/B/C/D1-208[»]
ProteinModelPortaliP0A7A5
SMRiP0A7A5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7A5

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105E26 Bacteria
COG2518 LUCA
HOGENOMiHOG000257189
InParanoidiP0A7A5
KOiK00573
OMAiPYTVAFQ
PhylomeDBiP0A7A5

Family and domain databases

HAMAPiMF_00090 PIMT, 1 hit
InterProiView protein in InterPro
IPR000682 PCMT
IPR029063 SAM-dependent_MTases
PANTHERiPTHR11579 PTHR11579, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
TIGRFAMsiTIGR00080 pimt, 1 hit
PROSITEiView protein in PROSITE
PS01279 PCMT, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSRRVQALL DQLRAQGIQD EQVLNALAAV PREKFVDEAF EQKAWDNIAL
60 70 80 90 100
PIGQGQTISQ PYMVARMTEL LELTPQSRVL EIGTGSGYQT AILAHLVQHV
110 120 130 140 150
CSVERIKGLQ WQARRRLKNL DLHNVSTRHG DGWQGWQARA PFDAIIVTAA
160 170 180 190 200
PPEIPTALMT QLDEGGILVL PVGEEHQYLK RVRRRGGEFI IDTVEAVRFV

PLVKGELA
Length:208
Mass (Da):23,258
Last modified:January 23, 2007 - v2
Checksum:iBFA179567527A118
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63493 Genomic DNA Translation: AAA24302.1
U29579 Genomic DNA Translation: AAA69253.1
U00096 Genomic DNA Translation: AAC75785.1
AP009048 Genomic DNA Translation: BAE76820.1
L07942 Genomic DNA Translation: AAA79840.1
L07869 Unassigned DNA Translation: AAA17874.1
D17549 Genomic DNA Translation: BAA04486.1
PIRiJH0242
RefSeqiNP_417223.1, NC_000913.3
WP_000254708.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75785; AAC75785; b2743
BAE76820; BAE76820; BAE76820
GeneIDi944923
KEGGiecj:JW2713
eco:b2743
PATRICifig|1411691.4.peg.3997

Similar proteinsi

Entry informationi

Entry nameiPIMT_ECOLI
AccessioniPrimary (citable) accession number: P0A7A5
Secondary accession number(s): P24206, Q2MA86
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 95 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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