UniProt Accession

 DEF_ECOLI; P0A6K3; P27251; Q2M6V1 

Genbank Protein ID

 X77800; X63666; X65946; X77091; U18997; U00096; AP009048 

Genbank Nucleotide ID

 CAA54826.1; CAA45206.1; CAA54367.1; AAA58084.1; AAC76312.1; BAE78005.1 

Protein Name

 Peptide deformylase 

Protein Synonyms/Alias

 PDF; Polypeptide deformylase 

Gene Name

 def 

Gene Synonyms/Alias

 fms; b3287; JW3248 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
81	INPELLEKSGETGIE	acetylation	[1]
151	MDYLSPLKQQRIRQK	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 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. 

Sequence Annotation

 ACT_SITE 134 134
 METAL 91 91 Iron.
 METAL 133 133 Iron.
 METAL 137 137 Iron.  

Keyword

 3D-structure; Complete proteome; Hydrolase; Iron; Metal-binding; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 169 AA 

Protein Sequence

Gene Ontology

 GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
 GO:0042586; F:peptide deformylase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0043686; P:co-translational protein modification; IPI:EcoCyc.
 GO:0031365; P:N-terminal protein amino acid modification; IDA:EcoCyc.
 GO:0006412; P:translation; IEA:HAMAP. 

Interpro

 IPR000181; Fmet_deformylase.
 IPR023635; Peptide_deformylase. 

Pfam

 PF01327; Pep_deformylase 

SMART

  

PROSITE

  

PRINTS

 PR01576; PDEFORMYLASE.