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Identification
YMDB IDYMDB00085
NameFlavin Mononucleotide
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionFlavin Mononucleotide, also known as riboflavin-5-phosphate, 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. Flavin Mononucleotide is an extremely weak basic (essentially neutral) compound (based on its pKa). Flavin Mononucleotide exists in all living species, ranging from bacteria to humans.
Structure
Thumb
Synonyms
  • Flanin
  • Flavine mononucleotide
  • Flavol
  • FMN
  • Riboflavin
  • Riboflavin 5'-monophosphate
  • Riboflavin 5'-phosphate
  • Riboflavin Mononucleotide
  • Riboflavin monophosphate
  • Riboflavin phosphate
  • Riboflavin-5-phosphate
  • Riboflavin-5'-phosphate na
  • Riboflavine 5'-monophosphate
  • Riboflavine 5'-phosphate
  • Riboflavine dihydrogen phosphate
  • Riboflavine monophosphate
  • Riboflavine phosphate
  • Riboflavine-5'-phosphate
  • Vitamin B2 phosphate
  • Riboflavin 5'-(dihydrogen phosphate)
  • Riboflavin 5'-(dihydrogen phosphoric acid)
  • Riboflavin 5'-monophosphoric acid
  • Riboflavin 5'-phosphoric acid
  • Riboflavin monophosphoric acid
  • Riboflavin-5-phosphoric acid
  • Riboflavine dihydrogen phosphoric acid
  • 5'-Monophosphate, riboflavin
  • 5'-Phosphate, riboflavin
  • Flavin mononucleotide sodium salt
  • Mononucleotide, riboflavin
  • Flavin mononucleotide monosodium salt
  • Flavin mononucleotide monosodium salt, dihydrate
  • Phosphate, sodium riboflavin
  • Riboflavin 5' phosphate
  • Riboflavin phosphate, sodium
  • Mononucleotide, flavin
  • Riboflavin 5' monophosphate
  • Flavin mononucleotide disodium salt
  • Sodium riboflavin phosphate
  • a-CEHC
  • Α-cehc
  • 3-(6-Hydroxy-2,5,7,8-tetramethyl-3,4-dihydro-2H-1-benzopyran-2-yl)propanoate
  • Creatine phosphate
  • Creatine phosphic acid
  • N-(N-Phosphonoamido)sarcosine
  • N-(Phosphonoamidino)sarcosine
  • N-Phosphorylcreatine
  • N(Omega)-phosphonocreatine
  • Phosphorylcreatine
  • {[imino(phosphonoamino)methyl](methyl)amino}acetic acid
  • N-Phosphocreatine
  • Creatine phosphoric acid
  • {[imino(phosphonoamino)methyl](methyl)amino}acetate
  • Creatine-p
  • Creatine-phosphate
  • Creatinephosphoric acid
  • N-(Phosphonoamidino)-sarcosine
  • N-Phosphorocreatine
  • N-[Imino(phosphonoamino)methyl]-N-methyl-glycine
  • Neo-ton
  • p-Creatine
  • 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
  • 5'-Phospho-ribosyl-5-amino-4-imidazole carboxamide
  • 5'-Phosphoribosyl-5-amino-4-imidazolecarboxamide
  • 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
  • 5-Aminoimidazole-4-carboxamide ribotide
  • 5-Phosphoribosyl-4-carbamoyl-5-aminoimidazole
  • Acadesine 5'-monophosphate
  • AICA-Ribonucleotide
  • 5-Amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
  • Acadesine 5'-monophosphoric acid
  • 5-Amino-1-(5-phospho-b-D-ribosyl)imidazole-4-carboxamide
  • 5-Amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide
  • 5'-p-Ribosyl-5-amino-4-imidazole carboxamide
  • 5'-Phosphoribosyl-5-amino-4-imidazole carboxamide
  • 5-Amino-4-imidazolecarboxamide ribotide
  • AICA Ribonucleotide
  • Aminoimidazole carboxamide ribonucleotide
  • Z-Nucleotide
  • 4-Carboxy-5-aminoimidazole ribotide
  • 5-Amino-1-beta-D-ribofuranosylimidazole-4-carboxamide monophosphate
  • 5-Amino-4-imidazolecarboxamide ribofuranoside 5'-monophosphate
  • AICA Ribonucleotide, (D-ribofuranosyl)-isomer
  • AICAriboside 5'-monophosphate
  • CAIR
  • ZMP
CAS number146-17-8
WeightAverage: 456.3438
Monoisotopic: 456.104614802
InChI KeyFVTCRASFADXXNN-SCRDCRAPSA-N
InChIInChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
IUPAC Name{[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-2H,3H,4H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy}phosphonic acid
Traditional IUPAC Nameriboflavin 5'-phosphate
Chemical FormulaC17H21N4O9P
SMILES[H]O[C@]([H])(C([H])([H])OP(=O)(O[H])O[H])[C@@]([H])(O[H])[C@@]([H])(O[H])C([H])([H])N1C2=NC(=O)N([H])C(=O)C2=NC2=C1C([H])=C(C(=C2[H])C([H])([H])[H])C([H])([H])[H]
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.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
ClassFlavin nucleotides
Sub ClassNot Available
Direct ParentFlavin nucleotides
Alternative Parents
Substituents
  • Flavin nucleotide
  • Flavin
  • Isoalloxazine
  • Diazanaphthalene
  • Pteridine
  • Quinoxaline
  • Monoalkyl phosphate
  • Pyrimidone
  • Pyrazine
  • Organic phosphoric acid derivative
  • Phosphoric acid ester
  • Benzenoid
  • Alkyl phosphate
  • Pyrimidine
  • Heteroaromatic compound
  • Vinylogous amide
  • Secondary alcohol
  • Lactam
  • Azacycle
  • Polyol
  • Organoheterocyclic compound
  • Organooxygen compound
  • Organonitrogen compound
  • Hydrocarbon derivative
  • Organic oxide
  • Organopnictogen compound
  • Organic oxygen compound
  • Alcohol
  • Organic nitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point290 °C
Experimental Properties
PropertyValueReference
Water Solubility92 mg/mL [HMP experimental]PhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility0.67 g/LALOGPS
logP-0.78ALOGPS
logP-1ChemAxon
logS-2.8ALOGPS
pKa (Strongest Acidic)1.49ChemAxon
pKa (Strongest Basic)-2.6ChemAxon
Physiological Charge-3ChemAxon
Hydrogen Acceptor Count11ChemAxon
Hydrogen Donor Count6ChemAxon
Polar Surface Area201.58 ŲChemAxon
Rotatable Bond Count7ChemAxon
Refractivity107.14 m³·mol⁻¹ChemAxon
Polarizability42.19 ųChemAxon
Number of Rings3ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • mitochondrion
  • extracellular
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Oxidative phosphorylationPW002461 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyrimidine metabolismPW002469 ThumbThumb?image type=greyscaleThumb?image type=simple
Riboflavin metabolismPW002443 ThumbThumb?image type=greyscaleThumb?image type=simple
Sulfur metabolismPW002483 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Oxidative phosphorylationec00190 Map00190
Pyrimidine metabolismec00240 Map00240
Riboflavin metabolismec00740 Map00740
Sulfur metabolismec00920 Map00920
SMPDB Reactions
Adenosine triphosphate + RiboflavinADP + Flavin Mononucleotide
Adenosine triphosphate + Flavin MononucleotidePyrophosphate + FAD
alkylsulfonate + FMNH2 + oxygen → Betaine aldehyde + Sulfite + Flavin Mononucleotide + water + hydron
KEGG Reactions
Flavin Mononucleotide + water Riboflavin + phosphate
Flavin Mononucleotide + Adenosine triphosphate + hydronPyrophosphate + FAD
NADH + Flavin Mononucleotide + hydronNAD + FMNH2
Flavin Mononucleotide + NADPH + hydronNADP + FMNH2
Fumaric acid + FMNH2Flavin Mononucleotide + Succinic acid
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Wu, M., Repetto, B., Glerum, D. M., Tzagoloff, A. (1995). "Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae." Mol Cell Biol 15:264-271.7799934
  • KEARNEY, E. B., ENGLARD, S. (1951). "The enzymatic phosphorylation of riboflavin." J Biol Chem 193:821-834.14907770
  • TSUBOI, K. K., WIENER, G., HUDSON, P. B. (1957). "Acid phosphatase. VII. Yeast phosphomonoesterase; isolation procedure and stability characteristics." J Biol Chem 224:621-635.13405892
  • Liger, D., Graille, M., Zhou, C. Z., Leulliot, N., Quevillon-Cheruel, S., Blondeau, K., Janin, J., van Tilbeurgh, H. (2004). "Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities." J Biol Chem 279:34890-34897.15184374
Synthesis Reference:Ono, Shigeru; Hirano, Hiroko; Sato, Yoshiyuki. Formation of flavin adenine dinucleotide and flavin mononucleotide by lens homogenate. Experimental Eye Research (1982), 34(2), 297-301.
External Links:
ResourceLink
CHEBI ID17621
HMDB IDHMDB01520
Pubchem Compound ID710
Kegg IDC00061
ChemSpider ID24608082
FOODB IDFDB030862
WikipediaFlavin_mononucleotide
BioCyc IDFMN

Enzymes

General function:
Involved in nitronate monooxygenase activity
Specific function:
Catalyzes the oxidation of alkyl nitronates to produce the corresponding carbonyl compounds and nitrites
Gene Name:
Not Available
Uniprot ID:
P47177
Molecular weight:
45142.60156
Reactions
Ethylnitronate + O(2) + FMNH(2) → acetaldehyde + nitrite + FMN + H(2)O.
General function:
Involved in pyridoxamine-phosphate oxidase activity
Specific function:
Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)
Gene Name:
PDX3
Uniprot ID:
P38075
Molecular weight:
26908.0
Reactions
Pyridoxamine 5'-phosphate + H(2)O + O(2) → pyridoxal 5'-phosphate + NH(3) + H(2)O(2).
Pyridoxine 5'-phosphate + O(2) → pyridoxal 5'-phosphate + H(2)O(2).
General function:
Involved in electron carrier activity
Specific function:
Could be a fumarate reductase
Gene Name:
Not Available
Uniprot ID:
P32614
Molecular weight:
50843.69922
Reactions
Succinate + NAD(+) → fumarate + NADH.
General function:
Involved in electron carrier activity
Specific function:
Could be a fumarate reductase
Gene Name:
OSM1
Uniprot ID:
P21375
Molecular weight:
55064.80078
Reactions
General function:
Involved in acid phosphatase activity
Specific function:
A phosphate monoester + H(2)O = an alcohol + phosphate
Gene Name:
PHO11
Uniprot ID:
P35842
Molecular weight:
52757.39844
Reactions
A phosphate monoester + H(2)O → an alcohol + phosphate.
General function:
Involved in riboflavin kinase activity
Specific function:
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme
Gene Name:
FMN1
Uniprot ID:
Q03778
Molecular weight:
24536.90039
Reactions
ATP + riboflavin → ADP + FMN.
General function:
Involved in acid phosphatase activity
Specific function:
Partially mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and NPP2
Gene Name:
PHO5
Uniprot ID:
P00635
Molecular weight:
52858.10156
Reactions
A phosphate monoester + H(2)O → an alcohol + phosphate.
General function:
Involved in FMN reductase activity
Specific function:
Has several reductase activities that are NAD(P)H- dependent and involve FMN as a cofactor, ferricyanide being the best substrate for reduction. May be involved in ferric iron assimilation
Gene Name:
LOT6
Uniprot ID:
Q07923
Molecular weight:
21280.40039
Reactions
FMNH(2) + NAD(P)(+) → FMN + NAD(P)H.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme
Gene Name:
FAD1
Uniprot ID:
P38913
Molecular weight:
35545.80078
Reactions
ATP + FMN → diphosphate + FAD.

Transporters

General function:
Involved in binding
Specific function:
Transport of FAD from the cytosol to the mitochondrial matrix
Gene Name:
FLX1
Uniprot ID:
P40464
Molecular weight:
34408.89844