CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010144
UniProt Accession
Genbank Protein ID
 U00089 
Genbank Nucleotide ID
Protein Name
 Peptide deformylase 
Protein Synonyms/Alias
 PDF; Polypeptide deformylase 
Gene Name
 def 
Gene Synonyms/Alias
 MPN_245; MP587 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
202LNPLFTNKEWKVINPacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819
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 (By similarity). 
Sequence Annotation
 ACT_SITE 179 179 By similarity.
 METAL 134 134 Iron (By similarity).
 METAL 178 178 Iron (By similarity).
 METAL 182 182 Iron (By similarity).  
Keyword
 Complete proteome; Hydrolase; Iron; Metal-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 216 AA 
Protein Sequence
MTKILPVSTI SIFRIILILP QINMELLPTK AWLVLDDVKE INEPTKPVQF PLDQASLDCI 60
AKMMAYVDAS YNGDAEKYGI IPGIGIAANQ IGYWKQMFYI HLMDGGVEHK CLLINPKIIN 120
LSANKSFLKS GEGCLSVPKM HQGYVIRHEW ITITGFDWLQ QKEITITATG LFGMCLQHEF 180
DHLQGRFYYH RINPLNPLFT NKEWKVINPA LPSDSE 216 
Gene Ontology
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0042586; F:peptide deformylase activity; IEA:HAMAP.
 GO:0006412; P:translation; IEA:HAMAP. 
Interpro
 IPR000181; Fmet_deformylase.
 IPR023635; Peptide_deformylase. 
Pfam
 PF01327; Pep_deformylase 
SMART
  
PROSITE
  
PRINTS
 PR01576; PDEFORMYLASE.