Record Information
Version2.0
Creation Date2012-05-31 13:47:23 -0600
Update Date2015-09-13 15:15:22 -0600
Secondary Accession Numbers
  • ECMDB01197
Identification
Name:FADH2
Description:FADH2 is a reduced form of Flavin adenine dinucleotide (FAD). FAD is a redox cofactor involved in several important reactions in metabolism. It can exist in two different redox states, which it converts between by accepting or donating electrons. The molecule consists of a riboflavin moiety (vitamin B2) bound to the phosphate group of an ADP molecule. The flavin group is bound to ribitol, a sugar alcohol, by a carbon-nitrogen bond, not a glycosidic bond. Thus, riboflavin is not technically a nucleotide; the name flavin adenine dinucleotide is a misnomer. FAD can be reduced to FADH2, whereby it accepts two hydrogen atoms.
Structure
Thumb
Synonyms:
  • 1,5-Dihydro-FAD
  • 1,5-Dihydro-P-5-ester with adenosine
  • 1,5-dihydro-Riboflavin 5'-(trihydrogen diphosphate) P'->5'-ester with adenosine
  • 1,5-dihydro-Riboflavin 5'-(trihydrogen diphosphoric acid) p'->5'-ester with adenosine
  • Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (8CI)
  • Adenosine 5'-(trihydrogen pyrophosphate), 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-(trihydrogen pyrophosphoric acid), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-(trihydrogen pyrophosphoric acid), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (8ci)
  • Adenosine 5'-(trihydrogen pyrophosphoric acid), 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-{3-[D-ribo-5-(7,8-dimethyl-2,4-dioxo-1,2,3,4,5,10-tetrahydrobenzo[g]pteridin-10-yl)-2,3,4-trihydroxypentyl] dihydrogen diphosphate}
  • Adenosine 5'-{3-[D-ribo-5-(7,8-dimethyl-2,4-dioxo-1,2,3,4,5,10-tetrahydrobenzo[g]pteridin-10-yl)-2,3,4-trihydroxypentyl] dihydrogen diphosphoric acid}
  • Adenosine 5-(trihydrogen pyrophosphate)
  • Adenosine 5-(trihydrogen pyrophosphoric acid)
  • Adenosine pyrophosphate 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphate 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (7CI)
  • Adenosine pyrophosphate, 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphate, 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphoric acid 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphoric acid 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (7ci)
  • Adenosine pyrophosphoric acid, 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphoric acid, 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Benzo[gr]pteridine riboflavin 5'-(trihydrogen diphosphate) deriv
  • benzo[GR]Pteridine riboflavin 5'-(trihydrogen diphosphoric acid) deriv
  • Benzo[g]pteridine riboflavin 5'-(trihydrogen diphosphate) deriv
  • Benzo[g]pteridine riboflavin 5'-(trihydrogen diphosphate) deriv.
  • benzo[g]Pteridine riboflavin 5'-(trihydrogen diphosphoric acid) deriv
  • benzo[g]Pteridine riboflavin 5'-(trihydrogen diphosphoric acid) deriv.
  • Dihydro-FAD
  • Dihydroflavine-adenine dinucleotide
  • FAD
  • FADH
  • FADH2
  • FDA
  • Flavin adenine dinucleotide (reduced)
  • Flavin adenine dinucleotide reduced
  • Reduced flavine adenine dinucleotide
  • Riboflavin 5'-(trihydrogen diphosphate), 1,5-dihydro-, P'-5'-ester with adenosine
  • Riboflavin 5'-(trihydrogen diphosphate), 1,5-dihydro-, P'-5'-ester with adenosine (9CI)
  • Riboflavin 5'-(trihydrogen diphosphoric acid), 1,5-dihydro-, p'-5'-ester with adenosine
  • Riboflavin 5'-(trihydrogen diphosphoric acid), 1,5-dihydro-, p'-5'-ester with adenosine (9ci)
Chemical Formula:C27H35N9O15P2
Weight:Average: 787.5656
Monoisotopic: 787.172784519
InChI Key:YPZRHBJKEMOYQH-UYBVJOGSSA-N
InChI:InChI=1S/C27H35N9O15P2/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/h3-4,8-9,14-16,19-21,26,32,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H2,33,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
CAS number:1910-41-4
IUPAC Name:[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]({[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-1H,2H,3H,4H,5H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy})phosphinic acid
Traditional IUPAC Name:fadh(.)
SMILES:CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC3=C1N=CN=C3N)C1=C(N2)C(=O)NC(=O)N1
Chemical Taxonomy
DescriptionThis compound belongs to the class of chemical entities 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.
KingdomChemical entities
Super ClassOrganic compounds
ClassNucleosides, nucleotides, and analogues
Sub ClassFlavin nucleotides
Direct ParentFlavin nucleotides
Alternative Parents
Substituents
  • Flavin nucleotide
  • Purine ribonucleoside diphosphate
  • Purine ribonucleoside monophosphate
  • Flavin
  • Pentose-5-phosphate
  • Pentose phosphate
  • Alkyldiarylamine
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Pteridine
  • Pentose monosaccharide
  • Monosaccharide phosphate
  • Organic pyrophosphate
  • Imidazopyrimidine
  • Purine
  • Monoalkyl phosphate
  • Pyrimidone
  • Aminopyrimidine
  • Monosaccharide
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Imidolactam
  • Benzenoid
  • Phosphoric acid ester
  • Primary aromatic amine
  • Alkyl phosphate
  • Pyrimidine
  • Vinylogous amide
  • Oxolane
  • Azole
  • Heteroaromatic compound
  • Imidazole
  • Secondary alcohol
  • Urea
  • Lactam
  • Secondary amine
  • Polyol
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Hydrocarbon derivative
  • Organic nitrogen compound
  • Alcohol
  • Amine
  • Organonitrogen compound
  • Primary amine
  • Organopnictogen compound
  • Organic oxide
  • Organooxygen compound
  • Organic oxygen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
State:Not Available
Charge:-2
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility2.65 mg/mLALOGPS
logP-0.93ALOGPS
logP-5.4ChemAxon
logS-2.5ALOGPS
pKa (Strongest Acidic)1.86ChemAxon
pKa (Strongest Basic)5ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count18ChemAxon
Hydrogen Donor Count11ChemAxon
Polar Surface Area355.76 Å2ChemAxon
Rotatable Bond Count13ChemAxon
Refractivity188.8 m3·mol-1ChemAxon
Polarizability72.42 Å3ChemAxon
Number of Rings6ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
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
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
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
Palmityl-CoA + FAD <> (2E)-Hexadecenoyl-CoA + FADH2

SMPDB Pathways:Not Available
KEGG Pathways:
EcoCyc Pathways:Not Available
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
38± 0 uMBW2511348 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoStationary Phase, glucose limitedBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37 oCPMID: 17379776
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-000i-0001200900-b0740b3d33d50996ccdeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-000m-0105900000-3abff26d5bb35f8527b8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-000i-0931700000-73f360589a13230eea7aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, NegativeNot Available
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,1H] 2D NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Jorns MS: DNA photorepair: chromophore composition and function in two classes of DNA photolyases. Biofactors. 1990 Oct;2(4):207-11. Pubmed: 2282137
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Ramsey AJ, Alderfer JL, Jorns MS: Energy transduction during catalysis by Escherichia coli DNA photolyase. Biochemistry. 1992 Aug 11;31(31):7134-42. Pubmed: 1643047
  • Ramsey AJ, Jorns MS: Effect of 5-deazaflavin on energy transduction during catalysis by Escherichia coli DNA photolyase. Biochemistry. 1992 Sep 15;31(36):8437-41. Pubmed: 1390627
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Zeller HD, Hille R, Jorns MS: Bacterial sarcosine oxidase: identification of novel substrates and a biradical reaction intermediate. Biochemistry. 1989 Jun 13;28(12):5145-54. Pubmed: 2475174
Synthesis Reference:Kavakli I Halil; Sancar Aziz Analysis of the role of intraprotein electron transfer in photoreactivation by DNA photolyase in vivo. Biochemistry (2004), 43(48), 15103-10.
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI ID17877
HMDB IDHMDB01197
Pubchem Compound ID446013
Kegg IDC01352
ChemSpider ID393487
WikipediaFADH
BioCyc IDFADH2
EcoCyc IDFADH2
Ligand ExpoFDA

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 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