Hmdb loader
Identification
HMDB Protein ID HMDBP13033
Secondary Accession Numbers None
Name Triokinase/FMN cyclase
Synonyms
  1. Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
Gene Name TKFC
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate (PubMed:16289032). Represses IFIH1-mediated cellular antiviral response (By similarity).
Pathways
  • Carbon metabolism
  • Fructose and mannose metabolism
  • Glycerolipid metabolism
  • RIG-I-like receptor signaling pathway
Reactions Not Available
GO Classification
Biological Process
cellular carbohydrate metabolic process
negative regulation of MDA-5 signaling pathway
glycerol catabolic process
carbohydrate phosphorylation
regulation of innate immune response
Cellular Component
cytosol
Molecular Function
metal ion binding
ATP binding
FAD-AMP lyase (cyclizing) activity
glycerone kinase activity
triokinase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 578
Molecular Weight 59443.295
Theoretical pI 7.513
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q4KLZ6
UniProtKB/Swiss-Prot Entry Name TKFC_RAT
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
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. Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC: Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases. Biochem Biophys Res Commun. 2005 Dec 30;338(4):1682-9. Epub 2005 Nov 2. [PubMed:16289032 ]
  3. Lundby A, Secher A, Lage K, Nordsborg NB, Dmytriyev A, Lundby C, Olsen JV: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun. 2012 Jun 6;3:876. doi: 10.1038/ncomms1871. [PubMed:22673903 ]
  4. Cabezas A, Pinto RM, Fraiz F, Canales J, Gonzalez-Santiago S, Cameselle JC: Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion. Biochemistry. 2001 Nov 13;40(45):13710-22. doi: 10.1021/bi0157159. [PubMed:11695920 ]