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2.7.7.2: FAD synthase

This is an abbreviated version!
For detailed information about FAD synthase, go to the full flat file.

Word Map on EC 2.7.7.2

Reaction

ATP
+
FMN
=
diphosphate
 +
FAD

Synonyms

adenosine triphosphate-riboflavin mononucleotide transadenylase, adenosine triphosphate-riboflavine mononucleotide transadenylase, ATP-FMN adenylyltransferase, ATP:FMN adenylyl transferase, ATP:FMN adenylyltransferase, AtRibF1, AtRibF2, FAD pyrophosphorylase, FAD synthase, FAD synthetase, FAD synthetase isoform 1, FAD synthetase isoform 2, Fad1, FADS, FADS-6, FADS1, FADS2, FLAD1, flavin adenine dinucleotide synthetase, FMN adenylyltransferase, FMN pyrophosphorylase, FMN:ATP adenylyltransferase, FMNAT, lysZ, MJ1179, More, ribF, RibL, riboflavin adenine dinucleotide pyrophosphorylase, riboflavin mononucleotide adenylyltransferase, riboflavine adenine dinucleotide adenylyltransferase, SPAP_1083

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.2 FAD synthase

Crystallization

Crystallization on EC 2.7.7.2 - FAD synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3D structural model for based on the structure of Thermotoga maritima FADS
crystal structure predicts a dimer of trimers organization
hanging-drop vapor-diffusion method, 277 K
-
mutant enzyme E268D, hanging drop vapor diffusion method
-
purified recombinant DELTA(1-182)CaFADS module in binary complex with ADP-Ca2+ and in ternary complex with FMN-ADP-Mg2+, mixing of 0.002 ml of 7.5-10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM MgCl2, 1mM FMN and/or 1 mM ADP, with 0.002 ml of reservoir solution containing 10-14% PEG 8000, 20% glycerol, 0.1 M MES-NaOH pH 6.5, 200 mM CaCl2 for the binary complex, or with 0.002 ml of reservoir solution containing 26-30% PEG 4000, 200 mM Li2SO4, 100 mM sodium acetate, pH 5.0, as well as 0.002 ml of 1 M NaI solution, for the ternary complex, X-ray diffraction structure determination and analysis at 1.65-2.15 A resolution, modelling
purified recombinant enzyme mutant R66A and R66E, mixing of equal volumes of 10 mg/ml protein in 20mMTris/HCl, pH 8.0, and 1 mM DTT, with reservoir solution containing 1.5 M Li2SO4, 0.1 M HEPES/NaOH, pH 7.5, X-ray diffraction structure determination and analysis, molecular replacment and modelling using the native CaFADS structure, PDB ID 2X0K, as search model
homology modeling of structure
in complex with FAD, hanging drop vapor diffusion method