Peptide deformylase

Details

Name
Peptide deformylase
Synonyms
  • 3.5.1.88
  • PDF
  • Polypeptide deformylase
Gene Name
def
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051268|Peptide deformylase
MAVVPIRIVGDPVLHTATTPVTVAADGSLPADLAQLIATMYDTMDAANGVGLAANQIGCS
LRLFVYDCAADRAMTARRRGVVINPVLETSEIPETMPDPDTDDEGCLSVPGESFPTGRAK
WARVTGLDADGSPVSIEGTGLFARMLQHETGHLDGFLYLDRLIGRYARNAKRAVKSHGWG
VPGLSWLPGEDPDPFGH
Number of residues
197
Molecular Weight
20938.52
Theoretical pI
Not Available
GO Classification
Functions
metal ion binding / peptide deformylase activity
Processes
co-translational protein modification / growth / N-terminal protein amino acid modification / peptidyl-methionine modification / protein deacylation / 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 (By similarity).
Specific Function
Metal ion binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051269|Peptide deformylase (def)
ATGGCAGTCGTACCCATCCGCATCGTGGGCGATCCCGTCTTACACACTGCGACCACACCG
GTGACGGTCGCCGCCGACGGTTCACTCCCGGCGGATCTCGCCCAGTTGATCGCCACCATG
TACGACACCATGGACGCCGCCAACGGAGTCGGCCTGGCTGCCAACCAGATCGGCTGCAGC
CTGCGGCTCTTCGTCTACGATTGCGCCGCGGACCGCGCAATGACCGCCCGCCGACGCGGT
GTGGTCATCAATCCGGTGCTTGAGACCTCCGAAATACCTGAGACCATGCCCGACCCGGAC
ACCGACGACGAAGGCTGTCTGTCGGTTCCCGGCGAGTCATTTCCTACCGGACGCGCGAAG
TGGGCACGAGTCACCGGACTCGACGCCGATGGCAGTCCGGTCAGTATCGAGGGCACCGGC
CTGTTCGCGCGGATGCTGCAGCACGAAACCGGGCACCTTGATGGATTCCTGTACCTGGAC
CGCCTCATCGGCCGGTACGCCCGCAACGCCAAACGGGCCGTCAAGTCACATGGCTGGGGC
GTTCCCGGACTGTCGTGGCTGCCCGGCGAGGACCCCGACCCGTTCGGTCACTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WIJ3
UniProtKB Entry NameDEF_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Raman K, Yeturu K, Chandra N: targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis. BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109. [Article]
  3. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08310N-[(2R)-2-{[(2S)-2-(1,3-benzoxazol-2-yl)pyrrolidin-1-yl]carbonyl}hexyl]-N-hydroxyformamideexperimentalunknownDetails