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
- Functionsiron ion binding / peptide deformylase activityProcessestranslation
- 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
- Pep_deformylase (PF01327)
- 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
Resource Link UniProtKB ID O31410 UniProtKB Entry Name DEF2_GEOSE GenBank Protein ID 2266414 GenBank Gene ID Y10549 PDB ID(s) 1LQY - General References
- 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
Drug Drug group Pharmacological action? Type Actions Details 2-[(Formyl-Hydroxy-Amino)-Methyl]-Heptanoic Acid [1-(2-Hydroxymethyl-Pyrrolidine-1-Carbonyl)-2-Methyl-Propyl]-Amide experimental unknown target Details