FAD (ECMDB01248) (M2MDB000308)
Record Information | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Version | 2.0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Creation Date | 2012-05-31 13:48:13 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Update Date | 2015-09-13 12:56:10 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary Accession Numbers |
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Identification | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Name: | FAD | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Description | Flavine Adenine Dinucleotide (FAD) is a condensation product of riboflavin and adenosine diphosphate. FAD is a redox cofactor involved in several important reactions in metabolism. It can exist in two different redox states, (FAD and FADH2) which it converts between by accepting or donating electrons. It is a coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Synonyms: |
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Chemical Formula: | C27H33N9O15P2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Weight: | Average: 785.5497 Monoisotopic: 785.157134455 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
InChI Key: | VWWQXMAJTJZDQX-UYBVJOGSSA-N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
InChI: | InChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
CAS number: | 146-14-5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
IUPAC Name: | {[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}[({[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-2H,3H,4H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy}(hydroxy)phosphoryl)oxy]phosphinic acid | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Traditional IUPAC Name: | flavine-adenine dinucleotide | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SMILES: | CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)CO[P@](O)(=O)O[P@@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC3=C1N=CN=C3N)C1=NC(=O)NC(=O)C1=N2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Chemical Taxonomy | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Description | belongs to the class of organic compounds known as flavin nucleotides. These are nucleotides containing a flavin moiety. Flavin is a compound that contains the tricyclic isoalloxazine ring system, which bears 2 oxo groups at the 2- and 4-positions. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Kingdom | Organic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Super Class | Nucleosides, nucleotides, and analogues | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Class | Flavin nucleotides | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sub Class | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Direct Parent | Flavin nucleotides | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Alternative Parents |
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Substituents |
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Molecular Framework | Aromatic heteropolycyclic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
External Descriptors |
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Physical Properties | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
State: | Solid | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Charge: | -3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Melting point: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental Properties: |
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Predicted Properties |
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Biological Properties | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Cellular Locations: | Cytoplasm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reactions: | FADH2 + 2 Hydrogen ion + SufBCD with two bound [2Fe-2S] clusters > FAD + SufBCD with bound [4Fe-4S] cluster FAD + Hydrogen ion + NADPH > FADH2 + NADP Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD scaffold complex + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with bound [2Fe-2S] cluster +2 SufSE sulfur acceptor complex Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD with bound [2Fe-2S] cluster + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with two bound [2Fe-2S] clusters +2 SufSE sulfur acceptor complex FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU scaffold protein > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with bound [2Fe-2S] cluster FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU with bound [2Fe-2S] cluster > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with two bound [2Fe-2S] clusters Adenosine triphosphate + Flavin Mononucleotide + Hydrogen ion > FAD + Pyrophosphate Butyryl-CoA + FAD <> Crotonoyl-CoA + FADH2 FAD + Octanoyl-CoA <> FADH2 + (2E)-Octenoyl-CoA FAD + Palmityl-CoA <> FADH2 + (2E)-Hexadecenoyl-CoA FAD + Tetradecanoyl-CoA <> FADH2 + (2E)-Tetradecenoyl-CoA FAD + Hexanoyl-CoA <> FADH2 + trans-2-Hexenoyl-CoA FAD + Stearoyl-CoA <> FADH2 + Trans-Octadec-2-enoyl-CoA Lauroyl-CoA + FAD <> (2E)-Dodecenoyl-CoA + FADH2 Decanoyl-CoA (N-C10:0CoA) + FAD <> (2E)-Decenoyl-CoA + FADH2 FAD + L-Proline > L-D-1-Pyrroline-5-carboxylic acid + FADH2 + Hydrogen ion D-Alanine + FAD + Water > FADH2 + Ammonium + Pyruvic acid FADH2 + 2 Hydrogen ion + IscU with two bound [2Fe-2S] clusters > FAD + IscU with bound [4Fe-4S] cluster FADH2 + 2 Fe3+ > FAD +2 Iron +2 Hydrogen ion FAD + Hydrogen ion + NADH > FADH2 + NAD FADH2 + 2 Ferroxamine > FAD +2 Iron +2 ferroxamine minus Fe(3) +2 Hydrogen ion Adenosine triphosphate + Flavin Mononucleotide <> Pyrophosphate + FAD Succinic acid + FAD <> FADH2 + Fumaric acid Glycerol 3-phosphate + FAD <> Dihydroxyacetone phosphate + FADH2 Butanoyl-CoA + FAD <> FADH2 + Crotonoyl-CoA L-Malic acid + FAD <> FADH2 + Oxalacetic acid More...An acyl-CoA + FAD > a dehydrogenated acyl-CoA + FADH(2) Adenosine triphosphate + Flavin Mononucleotide > Pyrophosphate + FAD FAD + [Protein]-L-threonine <> [Protein]-FMN-L-Threonine + Adenosine monophosphate Succinic acid + Ubiquinone-10 + FAD <> Fumaric acid + QH2 + FADH2 Flavin Mononucleotide + Hydrogen ion + Adenosine triphosphate > Pyrophosphate + FAD Succinic acid + FAD <> FADH2 + Fumaric acid FAD + Octanoyl-CoA <> FADH2 + (2E)-Octenoyl-CoA L-Malic acid + FAD <> FADH2 + Oxalacetic acid Glycerol 3-phosphate + FAD <> Dihydroxyacetone phosphate + FADH2 Succinic acid + FAD <> FADH2 + Fumaric acid Succinic acid + FAD <> FADH2 + Fumaric acid FAD + Octanoyl-CoA <> FADH2 + (2E)-Octenoyl-CoA L-Malic acid + FAD <> FADH2 + Oxalacetic acid | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SMPDB Pathways: |
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KEGG Pathways: | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
EcoCyc Pathways: |
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Concentrations | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Find out more about how we convert literature concentrations. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Spectra | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Spectra: | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
References | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
References: |
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Synthesis Reference: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Material Safety Data Sheet (MSDS) | Download (PDF) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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External Links: |
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Enzymes
- General function:
- Involved in electron carrier activity
- Specific function:
- Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
- Gene Name:
- frdA
- Uniprot ID:
- P00363
- Molecular weight:
- 65971
Reactions
Succinate + acceptor = fumarate + reduced acceptor. |
- General function:
- Involved in electron carrier activity
- Specific function:
- Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
- Gene Name:
- sdhB
- Uniprot ID:
- P07014
- Molecular weight:
- 26770
Reactions
Succinate + acceptor = fumarate + reduced acceptor. |
- General function:
- Involved in oxidoreductase activity
- Specific function:
- Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon
- Gene Name:
- putA
- Uniprot ID:
- P09546
- Molecular weight:
- 143814
Reactions
L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor. |
(S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2 H(2)O = L-glutamate + NAD(P)H. |
- General function:
- Involved in metabolic process
- Specific function:
- Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for NAD, biotin and Fe-S cluster synthesis. Transfers sulfur on 'Cys-456' of thiI in a transpersulfidation reaction. Transfers sulfur on 'Cys-19' of tusA in a transpersulfidation reaction. Functions also as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate
- Gene Name:
- iscS
- Uniprot ID:
- P0A6B7
- Molecular weight:
- 45089
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. |
- General function:
- Involved in D-amino-acid dehydrogenase activity
- Specific function:
- Oxidative deamination of D-amino acids
- Gene Name:
- dadA
- Uniprot ID:
- P0A6J5
- Molecular weight:
- 47607
Reactions
A D-amino acid + H(2)O + acceptor = a 2-oxo acid + NH(3) + reduced acceptor. |
- General function:
- Energy production and conversion
- Specific function:
- Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane
- Gene Name:
- frdC
- Uniprot ID:
- P0A8Q0
- Molecular weight:
- 15015
- General function:
- Involved in fumarate metabolic process
- Specific function:
- Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane
- Gene Name:
- frdD
- Uniprot ID:
- P0A8Q3
- Molecular weight:
- 13107
- General function:
- Involved in iron-sulfur cluster binding
- Specific function:
- Electron transfer protein; may also function as the membrane anchor for the glpAB dimer
- Gene Name:
- glpC
- Uniprot ID:
- P0A996
- Molecular weight:
- 44108
- General function:
- Involved in oxidoreductase activity
- Specific function:
- Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor
- Gene Name:
- glpA
- Uniprot ID:
- P0A9C0
- Molecular weight:
- 58958
Reactions
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. |
- General function:
- Involved in electron carrier activity
- Specific function:
- Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
- Gene Name:
- sdhA
- Uniprot ID:
- P0AC41
- Molecular weight:
- 64421
Reactions
Succinate + acceptor = fumarate + reduced acceptor. |
- General function:
- Involved in succinate dehydrogenase activity
- Specific function:
- Membrane-anchoring subunit of succinate dehydrogenase (SDH)
- Gene Name:
- sdhD
- Uniprot ID:
- P0AC44
- Molecular weight:
- 12867
- General function:
- Involved in electron carrier activity
- Specific function:
- Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
- Gene Name:
- frdB
- Uniprot ID:
- P0AC47
- Molecular weight:
- 27123
Reactions
Succinate + acceptor = fumarate + reduced acceptor. |
- General function:
- Involved in oxidoreductase activity
- Specific function:
- Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. Seems to reduces the complexed Fe(3+) iron of siderophores to Fe(2+), thus releasing it from the chelator
- Gene Name:
- fre
- Uniprot ID:
- P0AEN1
- Molecular weight:
- 26242
Reactions
Reduced riboflavin + NAD(P)(+) = riboflavin + NAD(P)H. |
2 cob(II)alamin + NAD(+) = 2 aquacob(III)alamin + NADH. |
- General function:
- Involved in FMN adenylyltransferase activity
- Specific function:
- ATP + riboflavin = ADP + FMN
- Gene Name:
- ribF
- Uniprot ID:
- P0AG40
- Molecular weight:
- 34734
Reactions
ATP + riboflavin = ADP + FMN. |
ATP + FMN = diphosphate + FAD. |
- General function:
- Involved in electron carrier activity
- Specific function:
- Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor
- Gene Name:
- glpB
- Uniprot ID:
- P13033
- Molecular weight:
- 45357
Reactions
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. |
- General function:
- Involved in oxidoreductase activity
- Specific function:
- Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor
- Gene Name:
- glpD
- Uniprot ID:
- P13035
- Molecular weight:
- 56750
Reactions
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. |
- General function:
- Involved in sulfite reductase (NADPH) activity
- Specific function:
- Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L- cysteine from sulfate
- Gene Name:
- cysI
- Uniprot ID:
- P17846
- Molecular weight:
- 63998
Reactions
H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. |
- General function:
- Involved in malate dehydrogenase (quinone) activity
- Specific function:
- (S)-malate + a quinone = oxaloacetate + reduced quinone
- Gene Name:
- mqo
- Uniprot ID:
- P33940
- Molecular weight:
- 60229
Reactions
(S)-malate + a quinone = oxaloacetate + reduced quinone. |
- General function:
- Involved in sulfite reductase (NADPH) activity
- Specific function:
- Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L- cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component
- Gene Name:
- cysJ
- Uniprot ID:
- P38038
- Molecular weight:
- 66269
Reactions
H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. |
- General function:
- Involved in 2 iron, 2 sulfur cluster binding
- Specific function:
- Involved in the reduction of ferric iron in cytoplasmic ferrioxamine B
- Gene Name:
- fhuF
- Uniprot ID:
- P39405
- Molecular weight:
- 30113
- General function:
- Involved in succinate dehydrogenase activity
- Specific function:
- Membrane-anchoring subunit of succinate dehydrogenase (SDH)
- Gene Name:
- sdhC
- Uniprot ID:
- P69054
- Molecular weight:
- 14299
- General function:
- Involved in metabolic process
- Specific function:
- Cysteine desulfurases mobilize the sulfur from L- cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo
- Gene Name:
- sufS
- Uniprot ID:
- P77444
- Molecular weight:
- 44433
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. |
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor. |
- General function:
- Involved in acyl-CoA dehydrogenase activity
- Specific function:
- Catalyzes the dehydrogenation of acyl-CoA
- Gene Name:
- fadE
- Uniprot ID:
- Q47146
- Molecular weight:
- 89224
Reactions
An acyl-CoA + FAD = a dehydrogenated acyl-CoA + FADH(2). |
- General function:
- Involved in nucleotide binding
- Specific function:
- Has low ATPase activity. The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation
- Gene Name:
- sufC
- Uniprot ID:
- P77499
- Molecular weight:
- 27582
- General function:
- Involved in iron-sulfur cluster assembly
- Specific function:
- The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation
- Gene Name:
- sufB
- Uniprot ID:
- P77522
- Molecular weight:
- 54745
- General function:
- Inorganic ion transport and metabolism
- Specific function:
- Specific function unknown
- Gene Name:
- cyaY
- Uniprot ID:
- P27838
- Molecular weight:
- 12231
- General function:
- Involved in iron ion binding
- Specific function:
- May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins (Potential)
- Gene Name:
- nifU
- Uniprot ID:
- P0ACD4
- Molecular weight:
- 13848
- General function:
- Not Available
- Specific function:
- Participates in cysteine desulfuration mediated by sufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for sufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of sufS, an intermediate product of cysteine desulfuration process. Together with the sufBCD complex, it thereby enhances up to 50- fold, the cysteine desulfurase activity of sufS. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Does not affect the selenocysteine lyase activity of sufS
- Gene Name:
- sufE
- Uniprot ID:
- P76194
- Molecular weight:
- 15800
- General function:
- Involved in iron-sulfur cluster assembly
- Specific function:
- The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein
- Gene Name:
- sufD
- Uniprot ID:
- P77689
- Molecular weight:
- 46822
Transporters
- General function:
- Involved in nucleotide binding
- Specific function:
- Has low ATPase activity. The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation
- Gene Name:
- sufC
- Uniprot ID:
- P77499
- Molecular weight:
- 27582