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Showing Protein Peptide deformylase, mitochondrial (HMDBP01117)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP01117
Secondary Accession Numbers
  • 6410
Name Peptide deformylase, mitochondrial
Synonyms
  1. Polypeptide deformylase
Gene Name PDF
Protein Type Enzyme
Biological Properties
General Function Involved in iron ion binding
Specific Function Removes the formyl group from the N-terminal Met of newly synthesized proteins (By similarity).
Pathways Not Available
Reactions
Formyl-L-methionyl peptide + Water → Formic acid + methionyl peptide details
GO Classification
Biological Process
translation
positive regulation of cell proliferation
N-terminal protein amino acid modification
peptidyl-methionine modification
Cellular Component
mitochondrion
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
transition metal ion binding
iron ion binding
peptide deformylase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Molecular Function
iron ion binding
peptide deformylase activity
Process
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
biosynthetic process
Cellular Location
  1. Mitochondrion (Potential)
Gene Properties
Chromosome Location 16
Locus 16q22.1
SNPs PDF
Gene Sequence 
>732 bp
ATGGCCCGGCTGTGGGGCGCGCTGAGTCTTTGGCCACTGTGGGCGGCCGTGCCGTGGGGC
GGGGCGGCAGCCGTCGGTGTCCGGGCTTGCAGCTCCACGGCCGCCCCGGACGGCGTCGAG
GGCCCGGCGCTGCGGCGCTCCTATTGGCGCCACCTGAGGCGTCTGGTGCTGGGTCCTCCC
GAACCGCCGTTCTCGCACGTGTGCCAAGTCGGGGACCCGGTGCTGCGCGGCGTGGCGGCC
CCGGTGGAGCGGGCGCAGCTAGGCGGGCCCGAGCTGCAGCGGCTGACGCAACGGCTGGTC
CAGGTGATGCGGCGGCGGCGCTGCGTGGGCCTAAGCGCGCCGCAGCTGGGGGTGCCGCGG
CAGGTGCTGGCGCTGGAGCTCCCCGAGGCGCTGTGTCGGGAGTGCCCGCCCCGCCAGCGC
GCGCTCCGCCAAATGGAGCCCTTCCCCCTGCGCGTGTTCGTGAACCCCAGCCTGCGAGTG
CTTGACAGCCGCCTGGTCACCTTTCCCGAGGGCTGCGAGAGCGTCGCCGGCTTCCTGGCC
TGCGTGCCCCGCTTCCAGGCGGTGCAGATCTCAGGGCTGGACCCCAATGGAGAACAGGTG
GTGTGGCAGGCGAGCGGGTGGGCAGCCCGCATCATCCAGCACGAGATGGACCACCTGCAG
GGCTGCCTGTTTATTGACAAAATGGACAGCAGGACGTTCACAAACGTCTATTGGATGAAG
GTGAATGACTAA
Protein Properties
Number of Residues 243
Molecular Weight 27013.25
Theoretical pI 9.152
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Peptide deformylase, mitochondrial
MARLWGALSLWPLWAAVPWGGAAAVGVRACSSTAAPDGVEGPALRRSYWRHLRRLVLGPP
EPPFSHVCQVGDPVLRGVAAPVERAQLGGPELQRLTQRLVQVMRRRRCVGLSAPQLGVPR
QVLALELPEALCRECPPRQRALRQMEPFPLRVFVNPSLRVLDSRLVTFPEGCESVAGFLA
CVPRFQAVQISGLDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSRTFTNVYWMK
VND
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9HBH1
UniProtKB/Swiss-Prot Entry Name DEFM_HUMAN
PDB IDs
GenBank Gene ID AF239156
GeneCard ID PDF
GenAtlas ID PDF
HGNC ID HGNC:30012
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Giglione C, Serero A, Pierre M, Boisson B, Meinnel T: Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J. 2000 Nov 1;19(21):5916-29. [PubMed:11060042 ]
  3. Serero A, Giglione C, Sardini A, Martinez-Sanz J, Meinnel T: An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway. J Biol Chem. 2003 Dec 26;278(52):52953-63. Epub 2003 Oct 7. [PubMed:14532271 ]