Peptide deformylase

Details

Name

Peptide deformylase

Synonyms

• 3.5.1.88

Gene Name

Not Available

Organism

Plasmodium falciparum (isolate 3D7)

Amino acid sequence

>lcl|BSEQ0022036|Peptide deformylase
MLMYYSLFLFNLIICCNVTSIYGYIHNVRSLEPYIKNDQIKNYSSNIKQKRKGSLYLLKN
EKDEIKIVKYPDPILRRRSEEVTNFDDNLKRVVRKMFDIMYESKGIGLSAPQVNISKRII
VWNALYEKRKEENERIFINPSIVEQSLVKLKLIEGCLSFPGIEGKVERPSIVSISYYDIN
GYKHLKILKGIHSRIFQHEFDHLNGTLFIDKMTQVDKKKVRPKLNELIRDYKATHSEEPA
L

Number of residues

241

Molecular Weight

28393.87

Theoretical pI

9.88

GO Classification

Functions

ferrous iron binding / peptide deformylase activity

Processes

co-translational protein modification / N-terminal protein amino acid modification / translation

Components

apicoplast / integral component of membrane

General Function

Peptide deformylase activity

Specific Function

Removes the formyl group from the N-terminal Met of newly synthesized proteins.

Pfam Domain Function

• Pep_deformylase (PF01327)

Transmembrane Regions

6-25

Cellular Location

Cytoplasmic

Gene sequence

>lcl|BSEQ0022037|Peptide deformylase
ATGTTGATGTATTATTCACTTTTCCTTTTTAATTTAATAATATGTTGTAATGTTACAAGT
ATTTATGGATATATACACAATGTTAGATCACTTGAACCATATATAAAAAATGATCAGATA
AAAAATTATAGTAGTAATATAAAACAAAAGAGAAAAGGCTCTTTATATTTATTAAAAAAT
GAAAAGGATGAGATAAAAATCGTCAAGTACCCGGACCCTATATTAAGGCGACGAAGTGAA
GAAGTCACAAATTTTGATGATAATTTGAAGAGAGTTGTGAGAAAAATGTTTGATATTATG
TACGAGAGCAAAGGTATTGGTTTGTCTGCACCACAAGTAAATATAAGCAAACGAATTATT
GTATGGAATGCATTATATGAAAAAAGAAAAGAAGAAAATGAACGAATATTTATTAATCCG
TCCATAGTAGAACAGAGTCTAGTTAAATTAAAATTAATAGAAGGATGTTTATCATTTCCT
GGAATAGAAGGAAAAGTTGAACGACCTAGTATAGTATCTATATCATATTATGATATTAAT
GGATATAAACATTTAAAAATTTTGAAAGGTATACATTCTAGAATATTTCAACATGAATTT
GATCATCTTAATGGTACATTATTTATTGATAAAATGACACAAGTCGATAAAAAAAAAGTA
AGACCAAAACTTAACGAGCTAATTAGGGATTATAAGGCTACTCACTCAGAAGAACCAGCC
CTATAA

Chromosome Location

Not Available

Locus

Not Available

External Identifiers

Resource	Link
UniProtKB ID	Q8I372
UniProtKB Entry Name	Q8I372_PLAF7
GenBank Gene ID	AL929356

General References

1. Gardner MJ, Hall N, Fung E, White O, Berriman M, Hyman RW, Carlton JM, Pain A, Nelson KE, Bowman S, Paulsen IT, James K, Eisen JA, Rutherford K, Salzberg SL, Craig A, Kyes S, Chan MS, Nene V, Shallom SJ, Suh B, Peterson J, Angiuoli S, Pertea M, Allen J, Selengut J, Haft D, Mather MW, Vaidya AB, Martin DM, Fairlamb AH, Fraunholz MJ, Roos DS, Ralph SA, McFadden GI, Cummings LM, Subramanian GM, Mungall C, Venter JC, Carucci DJ, Hoffman SL, Newbold C, Davis RW, Fraser CM, Barrell B: Genome sequence of the human malaria parasite Plasmodium falciparum. Nature. 2002 Oct 3;419(6906):498-511. [Article]
2. Hall N, Pain A, Berriman M, Churcher C, Harris B, Harris D, Mungall K, Bowman S, Atkin R, Baker S, Barron A, Brooks K, Buckee CO, Burrows C, Cherevach I, Chillingworth C, Chillingworth T, Christodoulou Z, Clark L, Clark R, Corton C, Cronin A, Davies R, Davis P, Dear P, Dearden F, Doggett J, Feltwell T, Goble A, Goodhead I, Gwilliam R, Hamlin N, Hance Z, Harper D, Hauser H, Hornsby T, Holroyd S, Horrocks P, Humphray S, Jagels K, James KD, Johnson D, Kerhornou A, Knights A, Konfortov B, Kyes S, Larke N, Lawson D, Lennard N, Line A, Maddison M, McLean J, Mooney P, Moule S, Murphy L, Oliver K, Ormond D, Price C, Quail MA, Rabbinowitsch E, Rajandream MA, Rutter S, Rutherford KM, Sanders M, Simmonds M, Seeger K, Sharp S, Smith R, Squares R, Squares S, Stevens K, Taylor K, Tivey A, Unwin L, Whitehead S, Woodward J, Sulston JE, Craig A, Newbold C, Barrell BG: Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13. Nature. 2002 Oct 3;419(6906):527-31. [Article]
3. Kumar A, Nguyen KT, Srivathsan S, Ornstein B, Turley S, Hirsh I, Pei D, Hol WG: Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design. Structure. 2002 Mar;10(3):357-67. [Article]
4. Robien MA, Nguyen KT, Kumar A, Hirsh I, Turley S, Pei D, Hol WG: An improved crystal form of Plasmodium falciparum peptide deformylase. Protein Sci. 2004 Apr;13(4):1155-63. Epub 2004 Mar 9. [Article]

Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB02625	(2r)-2-{[Formyl(Hydroxy)Amino]Methyl}Hexanoic Acid	experimental	unknown		Details
DB03648	(2S,2'S)-2,2'-(1,2-Hydrazinediylbis{methylene[(2S)-1-oxo-2,1-hexanediyl]imino})bis(6-amino-N-phenylhexanamide)	experimental	unknown		Details