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Q56308 (PIMT_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:TM_0704
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
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. 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

Subunit structure

Monomer.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00090.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

Vmax=164 nmol/min/mg enzyme with KASA (isoD) LAKY as substrate at 85 degrees Celsius HAMAP-Rule MF_00090

Temperature dependence:

Optimum temperature is 85 degrees Celsius. Highly thermostable, with no loss of activity after 60 min at 100 degrees Celsius. Enzyme activity is observed at temperatures as high as 93 degrees Celsius.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein repair

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090
PRO_0000111905

Sites

Active site591 By similarity

Secondary structure

.................................................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56308 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2FE6019571ADDF2C

FASTA31736,400
        10         20         30         40         50         60 
MREKLFWILK KYGVSDHIAK AFLEIPREEF LTKSYPLSYV YEDIVLVSYD DGEEYSTSSQ 

        70         80         90        100        110        120 
PSLMALFMEW VGLDKGMRVL EIGGGTGYNA AVMSRVVGEK GLVVSVEYSR KICEIAKRNV 

       130        140        150        160        170        180 
ERLGIENVIF VCGDGYYGVP EFSPYDVIFV TVGVDEVPET WFTQLKEGGR VIVPINLKLS 

       190        200        210        220        230        240 
RRQPAFLFKK KDPYLVGNYK LETRFITAGG NLGNLLERNR KLLREFPFNR EILLVRSHIF 

       250        260        270        280        290        300 
VELVDLLTRR LTEIDGTFYY AGPNGVVEFL DDRMRIYGDA PEIENLLTQW ESCGYRSFEY 

       310 
LMLHVGYNAF SHISCSI 

« Hide

References

« Hide 'large scale' references
[1]"Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima."
Swanson R.V., Sanna M.G., Simon M.I.
J. Bacteriol. 178:484-489(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"A highly active protein repair enzyme from an extreme thermophile: the L-isoaspartyl methyltransferase from Thermotoga maritima."
Ichikawa J.K., Clarke S.
Arch. Biochem. Biophys. 358:222-231(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Crystal structure of protein isoaspartyl methyltransferase. A catalyst for protein repair."
Skinner M.M., Puvathingal J.M., Walter R.L., Friedman A.M.
Structure 8:1189-1201(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30501 Genomic DNA. Translation: AAA96385.1.
AE000512 Genomic DNA. Translation: AAD35786.1.
PIRG72342.
RefSeqNP_228513.1. NC_000853.1.
YP_007977054.1. NC_021214.1.
YP_008990327.1. NC_023151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DL5X-ray1.80A/B1-317[»]
ProteinModelPortalQ56308.
SMRQ56308. Positions 1-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35786; AAD35786; TM_0704.
GeneID15494307.
18092085.
898371.
KEGGtma:TM0704.
tmm:Tmari_0704.
PATRIC23936326. VBITheMar51294_0716.

Phylogenomic databases

eggNOGCOG2518.
KOK00573.
OMAPTQWRES.
OrthoDBEOG644ZP2.
ProtClustDBPRK13943.

Family and domain databases

Gene3D3.55.20.10. 1 hit.
HAMAPMF_00090. PIMT.
InterProIPR000682. PCMT.
IPR009107. PIM_MeTrfase_C.
[Graphical view]
PANTHERPTHR11579. PTHR11579. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
SUPFAMSSF68930. SSF68930. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ56308.

Entry information

Entry namePIMT_THEMA
AccessionPrimary (citable) accession number: Q56308
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 102 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references