Peptide deformylase
Details
- Name
- Peptide deformylase
- Synonyms
- 3.5.1.88
- Polypeptide deformylase
- Gene Name
- def
- Organism
- Thermus thermophilus
- Amino acid sequence
>lcl|BSEQ0017004|Peptide deformylase MVYPIRLYGDPVLRRKARPVEDFSGIKRLAEDMLETMFEAKGVGLAAPQIGLSQRLFVAV EYADEPEGEEERPLRELVRRVYVVANPVITYREGLVEGTEGCLSLPGLYSEEVPRAERIR VEYQDEEGRGRVLELEGYMARVFQHEIDHLDGILFFERLPKPKREAFLEANRAELVRFQK EARALLKELSQG
- Number of residues
- 192
- Molecular Weight
- 22092.115
- Theoretical pI
- 4.86
- GO Classification
- Functionsiron ion binding / peptide deformylase activityProcessestranslation
- General Function
- Peptide deformylase activity
- Specific 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 (By similarity).
- Pfam Domain Function
- Pep_deformylase (PF01327)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0006128|579 bp ATGGTCTACCCCATCCGGCTTTACGGAGACCCCGTCCTCCGCCGCAAGGCCCGGCCCGTG GAGGACTTCTCGGGGATTAAGCGCCTGGCGGAGGACATGCTGGAGACGATGTTTGAGGCC AAAGGGGTGGGGCTTGCCGCCCCCCAGATCGGCCTCTCCCAGCGCCTCTTCGTGGCGGTG GAGTACGCCGACGAGCCCGAGGGGGAGGAGGAGAGGCCCCTGAGGGAGCTCGTGCGCCGG GTCTACGTGGTGGCGAACCCGGTGATCACCTACCGGGAGGGACTGGTGGAGGGGACGGAG GGGTGCCTCTCCCTGCCCGGCCTCTACTCCGAGGAGGTGCCCCGGGCGGAGCGCATCCGG GTGGAGTACCAGGACGAGGAGGGCCGTGGGCGCGTGTTGGAGCTCGAGGGGTACATGGCC CGGGTCTTCCAGCATGAGATCGACCATCTGGACGGGATCCTCTTCTTTGAGCGCCTGCCC AAGCCCAAGCGGGAGGCCTTTCTGGAGGCCAACCGGGCGGAGCTCGTCCGCTTCCAGAAG GAGGCCCGGGCCTTGCTGAAGGAGCTTTCCCAGGGATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P43522 UniProtKB Entry Name DEF_THETH GenBank Gene ID X79087 - General References
- Meinnel T, Blanquet S: Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase. J Bacteriol. 1994 Dec;176(23):7387-90. [Article]
- 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]