Peptide deformylase 2

Details

Name
Peptide deformylase 2
Kind
protein
Synonyms
  • 3.5.1.88
  • PDF 2
  • Polypeptide deformylase 2
Gene Name
Not Available
UniProtKB Entry
O31410Swiss-Prot
Organism
Geobacillus stearothermophilus
NCBI Taxonomy ID
1422
Amino acid sequence
>lcl|BSEQ0016506|Peptide deformylase 2
MITMKDIIKEGHPTLRKVAEPVPLPPSEEDKRILQSLLDYVKMSQDPELAAKYGLRPGIG
LAAPQINVSKRMIAVHVTDENGTLYSYALFNPKIVSHSVQQCYLTTGEGCLSVDRDVPGY
VLRYARITVTGTTLDGEEVTLRLKGLPAIVFQHEIDHLNGIMFYDRINPADPFQVPDGAI
PIGR
Number of residues
184
Molecular Weight
20382.365
Theoretical pI
6.35
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|BSEQ0003262|555 bp
ATGATCACCATGAAAGATATCATTAAAGAAGGGCATCCGACGCTGCGGAAAGTGGCTGAG
CCCGTTCCGCTGCCGCCTTCAGAGGAAGACAAACGCATTTTGCAAAGCTTGCTTGACTAT
GTGAAAATGAGCCAAGATCCGGAACTGGCGGCCAAATACGGCCTGCGGCCNGGCATCGGC
CTCGCCGCTCCGCAAATCAACGTCTCCAAACGGATGATTGCCGTTCATGTCACTGATGAA
AACGGAACGCTGTACAGCTATGCCTTGTTCAATCCGAAAATCGTCAGCCACTCTGTGCAG
CAATGTTATTTGACGACGGGGGAAGGCTGCCTGTCGGTCGACCGTGATGTGCCCGGATAC
GTACTGCGCTATGCCCGCATCACGGTCACCGGCACGACGCTCGACGGCGAGGAAGTCACC
TTGCGCCTCAAAGGATTGCCGGCCATCGTCTTCCAGCATGAAATCGACCATTTAAACGGC
ATTATGTTTTATGACCGCATCAATCCGGCCGACCCGTTCCAAGTGCCAGACGGGGCGATC
CCGATCGGGCGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO31410
UniProtKB Entry NameDEF2_GEOSE
GenBank Protein ID2266414
GenBank Gene IDY10549
PDB ID(s)1LQY
General References
  1. Meinnel T, Lazennec C, Villoing S, Blanquet S: 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. J Mol Biol. 1997 Apr 4;267(3):749-61. [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