Peptide deformylase

Details

Name
Peptide deformylase
Kind
protein
Synonyms
  • 3.5.1.88
  • PDF
  • Polypeptide deformylase
Gene Name
def
UniProtKB Entry
Q82ZJ0Swiss-Prot
Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
NCBI Taxonomy ID
226185
Amino acid sequence
>lcl|BSEQ0012704|Peptide deformylase
MITMKDIIREGNPTLRAVAEEVPVPITEEDRQLGEDMLTFLKNSQDPVKAEELQLRGGVG
LAAPQLDISKRIIAVHVPSNDPENETPSLSTVMYNPKILSHSVQDVCLGEGEGCLSVDRD
VPGYVVRHNKITVSYFDMAGEKHKVRLKNYEAIVVQHEIDHINGIMFYDHINKENPFALK
EGVLVIE
Number of residues
187
Molecular Weight
20911.76
Theoretical pI
4.83
GO Classification
Functions
iron ion binding / peptide deformylase activity
Processes
translation
General 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.
Specific Function
metal ion binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0012705|Peptide deformylase (def)
ATGATTACAATGAAAGATATTATTCGTGAAGGGAATCCCACACTTCGTGCTGTGGCAGAA
GAAGTGCCTGTCCCTATCACTGAGGAAGACCGACAATTAGGTGAGGACATGTTGACTTTC
TTAAAAAATAGTCAAGATCCAGTCAAAGCCGAAGAATTACAATTACGTGGTGGCGTTGGT
TTAGCTGCACCACAATTAGATATTTCTAAACGAATTATTGCTGTCCATGTTCCTAGTAAC
GACCCAGAAAACGAAACGCCTTCATTAAGTACGGTGATGTACAACCCTAAAATTTTGAGC
CATTCTGTGCAAGATGTATGTTTAGGTGAAGGGGAAGGCTGTTTATCTGTCGATCGGGAT
GTACCTGGGTATGTCGTTCGCCATAACAAAATTACCGTCAGTTATTTTGACATGGCTGGC
GAAAAACACAAAGTTCGTTTAAAAAACTACGAAGCGATTGTGGTTCAACATGAAATTGAT
CATATTAATGGCATCATGTTCTACGATCATATTAACAAAGAAAATCCATTTGCTTTAAAA
GAGGGCGTTTTAGTCATCGAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ82ZJ0
UniProtKB Entry NameDEF_ENTFA
GenBank Protein ID29342120
GenBank Gene IDAE016830
PDB ID(s)2OS0, 2OS1
KEGG IDefa:EF3066
NCBI Gene ID1201912
General References
  1. Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM: Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 2003 Mar 28;299(5615):2071-4. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
2-[(Formyl-Hydroxy-Amino)-Methyl]-Heptanoic Acid [1-(2-Hydroxymethyl-Pyrrolidine-1-Carbonyl)-2-Methyl-Propyl]-AmideexperimentalunknowntargetDetails