2.7.7.2: FAD synthase

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For detailed information about FAD synthase, go to the full flat file.

Reaction

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

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5	Activating Compound
41746	AA Sequence
6	Application
1	CAS Registry Number
32	Cloned(Commentary)
13	Cofactor
10	Crystallization (Commentary)
300	Disease/ Diagnostics
13	General Information
3	General Stability
4	IC50 Value
41	Inhibitors
68	kcat/KM [mM/s]
30	Ki Value [mM]
124	KM Value [mM]
16	Localization
45	Metals/Ions
41	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
59	Organism
1	Oxidation Stability
9	Pathway
32	PDB ID
11	pH Optimum
1	pH Stability
3	pI Value
67	Protein Variants
31	Purification (Commentary)
2	Reaction
2	Reaction Type
54	Reference
30	Source Tissue
13	Specific Activity [micromol/min/mg]
6	Storage Stability
94	Substrates and Products (Substrate)
31	Subunits
61	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
3	Temperature Stability [°C]
60	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 2.7.7.2 - FAD synthase

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SYSTEMATIC NAME

IUBMB Comments

ATP:FMN adenylyltransferase

Requires Mg2+ and is highly specific for ATP as phosphate donor [5]. The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [3]. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].