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P43522 (DEF_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:
Peptide deformylase

Short name=PDF
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:def
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions By similarity. HAMAP-Rule MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP-Rule MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082867

Sites

Active site1461 By similarity
Metal binding1021Iron By similarity
Metal binding1451Iron By similarity
Metal binding1491Iron By similarity

Secondary structure

............................. 192
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43522 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 665945183A251361

FASTA19222,092
        10         20         30         40         50         60 
MVYPIRLYGD PVLRRKARPV EDFSGIKRLA EDMLETMFEA KGVGLAAPQI GLSQRLFVAV 

        70         80         90        100        110        120 
EYADEPEGEE ERPLRELVRR VYVVANPVIT YREGLVEGTE GCLSLPGLYS EEVPRAERIR 

       130        140        150        160        170        180 
VEYQDEEGRG RVLELEGYMA RVFQHEIDHL DGILFFERLP KPKREAFLEA NRAELVRFQK 

       190 
EARALLKELS QG 

« Hide

References

[1]"Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase."
Meinnel T., Blanquet S.
J. Bacteriol. 176:7387-7390(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: VK1.
[2]"Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion."
Meinnel T., Lazennec C., Villoing S., Blanquet S.
J. Mol. Biol. 267:749-761(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79087 Genomic DNA. Translation: CAA55695.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V3YX-ray1.81A/B1-192[»]
ProteinModelPortalP43522.
SMRP43522. Positions 1-182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262724.TTC1662.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.45.10. 1 hit.
HAMAPMF_00163. Pep_deformylase.
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERPTHR10458. PTHR10458. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. SSF56420. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP43522.

Entry information

Entry nameDEF_THETH
AccessionPrimary (citable) accession number: P43522
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 75 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