| Identification | |||||||||||||||||||||||||||||||||||||||||||
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| Name | Flavin-Adenine Dinucleotide | ||||||||||||||||||||||||||||||||||||||||||
| Accession Number | DB03147 (EXPT01391) | ||||||||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||||||||
| Groups | experimental | ||||||||||||||||||||||||||||||||||||||||||
| Description | A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Salts | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand mixtures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Categories | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| CAS number | 146-14-5 | ||||||||||||||||||||||||||||||||||||||||||
| Weight |
Average: 785.5497 Monoisotopic: 785.157134455 |
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| Chemical Formula | C27H33N9O15P2 | ||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=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
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| 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-2H,3H,4H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy})phosphinic acid
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| 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
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| Mass Spec | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Classes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacology | |||||||||||||||||||||||||||||||||||||||||||
| Indication | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Absorption | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Metabolism | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Toxicity | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Affected organisms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacoeconomics | |||||||||||||||||||||||||||||||||||||||||||
| Manufacturers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Packagers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Dosage forms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Prices | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Patents | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Properties | |||||||||||||||||||||||||||||||||||||||||||
| State | solid | ||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Predicted Properties |
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| References | |||||||||||||||||||||||||||||||||||||||||||
| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| External Links |
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| ATC Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| AHFS Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| PDB Entries | |||||||||||||||||||||||||||||||||||||||||||
| FDA label | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| MSDS | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Interactions | |||||||||||||||||||||||||||||||||||||||||||
| Drug Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Targets |
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Pharmacological action: unknown
Involved in the conversion of UDP-GalP into UDP-GalF through a 2-keto intermediate Organism class: bacterialUniProt ID: P37747 ![]() Gene: glf Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity Organism class: bacterialUniProt ID: P39662 ![]() Gene: hmp Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
This deaminating oxidase catalyzes the oxidation of sarcosine (N-methylglycine), N-ethylglycine and glycine. Lower activities on D-alanine, D-valine, and D-proline are detected. Does not act on L-amino acids and other D-amino acids Organism class: bacterialUniProt ID: O31616 ![]() Gene: thiO Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 4. NADPH--cytochrome P450 reductase Pharmacological action: unknownThis enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5 Organism class: humanUniProt ID: P16435 ![]() Gene: POR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
5. Glutaryl-CoA dehydrogenase, mitochondrial Pharmacological action: unknownCatalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. The short isoform is inactive Organism class: humanUniProt ID: Q92947 ![]() Gene: GCDH ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 6. Medium-chain specific acyl-CoA dehydrogenase, mitochondrial Pharmacological action: unknownThis enzyme is specific for acyl chain lengths of 4 to 16 Organism class: humanUniProt ID: P11310 ![]() Gene: ACADM ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids Organism class: humanUniProt ID: P14920 ![]() Gene: DAO ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
8. Bifunctional protein putA [Includes: Proline dehydrogenase Pharmacological action: unknownOxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon Organism class: bacterialUniProt ID: P09546 ![]() Gene: putA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 9. Deoxyribodipyrimidine photo-lyase Pharmacological action: unknownInvolved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation Organism class: bacterialUniProt ID: P61497 ![]() Gene: phr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 10. Amine oxidase [flavin-containing] A Pharmacological action: unknownCatalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine Organism class: humanUniProt ID: P21397 ![]() Gene: MAOA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
11. Short-chain specific acyl-CoA dehydrogenase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P16219 ![]() Gene: ACADS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: Q96RQ9 ![]() Gene: IL4I1 SNPs: SNPJam Report ![]() References:
13. 2,4-dienoyl-CoA reductase [NADPH] Pharmacological action: unknownCatalyzes the NADP-dependent reduction of 2,4-dienoyl- CoA to yield trans-2- enoyl-CoA Organism class: bacterialUniProt ID: P42593 ![]() Gene: fadH Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 14. 2-oxopropyl-CoM reductase, carboxylating Pharmacological action: unknownCatalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M Organism class: bacterialUniProt ID: Q56839 ![]() Gene: xecC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 15. P-hydroxybenzoate hydroxylase Pharmacological action: unknown4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O Organism class: bacterialUniProt ID: P20586 ![]() Gene: pobA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 16. Nitric-oxide synthase, brain Pharmacological action: unknownProduces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter Organism class: humanUniProt ID: P29475 ![]() Gene: NOS1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
17. NAD(P)H dehydrogenase [quinone] 1 Pharmacological action: unknownThe enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis Organism class: humanUniProt ID: P15559 ![]() Gene: NQO1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
18. P-hydroxybenzoate hydroxylase Pharmacological action: unknown4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O Organism class: bacterialUniProt ID: P00438 ![]() Gene: pobA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 19. Fumarate reductase flavoprotein subunit Pharmacological action: unknownCatalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional Organism class: bacterialUniProt ID: P83223 ![]() Gene: SO_0970 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: Q86YB8 ![]() Gene: ERO1LB SNPs: SNPJam Report ![]() References:
21. Glutathione reductase, mitochondrial Pharmacological action: unknownMaintains high levels of reduced glutathione in the cytosol Organism class: humanUniProt ID: P00390 ![]() Gene: GSR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 22. NADPH-ferredoxin reductase fprA Pharmacological action: unknownMay serve as electron transfer protein and supply electrons to P450 systems Organism class: bacterialUniProt ID: O05783 ![]() Gene: fprA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 23. NADH-cytochrome b5 reductase 3 Pharmacological action: unknownDesaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction Organism class: humanUniProt ID: P00387 ![]() Gene: CYB5R3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Cholesterol + O(2) = cholest-4-en-3-one + H(2)O(2) Organism class: bacterialUniProt ID: P12676 ![]() Gene: choA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate Organism class: bacterialUniProt ID: Q9WYT0 ![]() Gene: thyX Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 26. Pyruvate oxidase Pharmacological action: unknownImportant for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate Organism class: bacterialUniProt ID: P37063 ![]() Gene: pox5 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH Organism class: bacterialUniProt ID: P0A9P4 ![]() Gene: trxB Protein Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Maintains high levels of reduced glutathione in the cytosol Organism class: bacterialUniProt ID: P06715 ![]() Gene: gor Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 29. 5,10-methylenetetrahydrofolate reductase Pharmacological action: unknown5-methyltetrahydrofolate + NAD(P)(+) = 5,10- methylenetetrahydrofolate + NAD(P)H Organism class: bacterialUniProt ID: P0AEZ1 ![]() Gene: metF Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 30. Monomeric sarcosine oxidase Pharmacological action: unknownCatalyzes the oxidative demethylation of sarcosine. Can also oxidize other secondary amino acids such as N-methyl-L- alanine Organism class: bacterialUniProt ID: P40859 ![]() Gene: soxA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase Organism class: parasiticUniProt ID: P28593 ![]() Gene: TPR Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 32. Ribosyldihydronicotinamide dehydrogenase [quinone] Pharmacological action: unknownThe enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis Organism class: humanUniProt ID: P16083 ![]() Gene: NQO2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 33. Isovaleryl-CoA dehydrogenase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P26440 ![]() Gene: IVD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 34. Xanthine dehydrogenase/oxidase Pharmacological action: unknownThis enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups Organism class: humanUniProt ID: P47989 ![]() Gene: XDH ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Cholesterol + O(2) = cholest-4-en-3-one + H(2)O(2) Organism class: bacterialUniProt ID: P22637 ![]() Gene: choB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 36. N,N-dimethylglycine oxidase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9AGP8 ![]() Gene: dmg Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 37. NADH peroxidase Pharmacological action: unknownPeroxidase whose active site is a redox-active cysteine- sulfenic acid Organism class: bacterialUniProt ID: P37062 ![]() Gene: npr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 38. Dihydropyrimidine dehydrogenase [NADP+] Pharmacological action: unknownInvolved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil Organism class: humanUniProt ID: Q12882 ![]() Gene: DPYD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
39. Ferredoxin--NADP reductase Pharmacological action: unknownReduced ferredoxin + NADP(+) = oxidized ferredoxin + NADPH Organism class: bacterialUniProt ID: P21890 ![]() Gene: petH Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
First component of the membrane-bound D-lactate oxidase, which is believed to play an important role in the energization of the active transport of a variety of sugars and amino acids Organism class: bacterialUniProt ID: P06149 ![]() Gene: dld Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 41. Sulfite reductase [NADPH] flavoprotein alpha-component Pharmacological action: unknownCatalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavo-protein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component Organism class: bacterialUniProt ID: P38038 ![]() Gene: cysJ Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 42. Thioredoxin reductase 1, cytoplasmic Pharmacological action: unknownThioredoxin + NADP(+) = thioredoxin disulfide + NADPH Organism class: humanUniProt ID: Q16881 ![]() Gene: TXNRD1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
43. Ferredoxin--NADP reductase Pharmacological action: unknownReduced ferredoxin + NADP(+) = oxidized ferredoxin + NADPH Organism class: bacterialUniProt ID: Q44532 ![]() Gene: fpr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 44. Acyl-CoA dehydrogenase family member 8, mitochondrial Pharmacological action: unknownHas very high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex Organism class: humanUniProt ID: Q9UKU7 ![]() Gene: ACAD8 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 45. Acyl-CoA dehydrogenase, short-chain specific Pharmacological action: unknownHas an optimum specificity for 4-carbon length fatty acyl-CoAs Organism class: bacterialUniProt ID: Q06319 ![]() Protein Sequence: FASTA 46. Apoptosis-inducing factor 1, mitochondrial Pharmacological action: unknownProbable oxidoreductase that acts as a caspase- independent mitochondrial effector of apoptotic cell death. Extramitochondrial AIF induces nuclear chromatin condensation and large scale DNA fragmentation (in vitro) Organism class: humanUniProt ID: O95831 ![]() Gene: AIFM1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q52437 ![]() Gene: bphA4 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 48. Dihydrolipoyl dehydrogenase Pharmacological action: unknownThe pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) Organism class: bacterialUniProt ID: P18925 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 49. Amine oxidase, flavin-containing Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q888A4 ![]() Gene: PSPTO1126 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 50. Deoxyribodipyrimidine photo-lyase Pharmacological action: unknownInvolved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation Organism class: bacterialUniProt ID: P00914 ![]() Gene: phrB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 51. Deoxyribodipyrimidine photo-lyase Pharmacological action: unknownInvolved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation Organism class: bacterialUniProt ID: P05327 ![]() Gene: phr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Catalyzes the oxidation of L-aspartate to iminoaspartate Organism class: bacterialUniProt ID: P10902 ![]() Gene: nadB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
May have a photoreceptor function. Binds DNA; represses transcription of at least 8 genes, including slr0364 and slr1866. Does not encode a DNA photolyase function. Its disruption does not affect circadian rhythm Organism class: bacterialUniProt ID: P77967 ![]() Gene: cry Protein Sequence: FASTA SNPs: SNPJam Report ![]() 54. Dihydrolipoyl dehydrogenase, mitochondrial Pharmacological action: unknownLipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes Organism class: humanUniProt ID: P09622 ![]() Gene: DLD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
55. Fumarate reductase flavoprotein subunit Pharmacological action: unknownCatalyzes unidirectional fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown Organism class: bacterialUniProt ID: Q9Z4P0 ![]() Gene: ifcA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 56. NADH-cytochrome b5 reductase 1 Pharmacological action: unknownOrganism class: human UniProt ID: Q9UHQ9 ![]() Gene: CYB5R1 SNPs: SNPJam Report ![]() References:
57. Oxidoreductase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7SID9 ![]() Protein Sequence: FASTA 58. Amine oxidase [flavin-containing] B Pharmacological action: unknownCatalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine Organism class: humanUniProt ID: P27338 ![]() Gene: MAOB ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 59. NADPH:adrenodoxin oxidoreductase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P22570 ![]() Gene: FDXR SNPs: SNPJam Report ![]() References:
60. Peroxisomal acyl-coenzyme A oxidase 1 Pharmacological action: unknownCatalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs Organism class: humanUniProt ID: Q15067 ![]() Gene: ACOX1 ![]() Protein Sequence: FASTA SNPs: SNPJam Report ![]() References:
61. UDP-N-acetylenolpyruvoylglucosamine reductase Pharmacological action: unknownCell wall formation Organism class: bacterialUniProt ID: P08373 ![]() Gene: murB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 62. FAD-linked sulfhydryl oxidase ALR Pharmacological action: unknownOrganism class: human UniProt ID: P55789 ![]() Gene: GFER SNPs: SNPJam Report ![]() References:
63. UDP-N-acetylenolpyruvoylglucosamine reductase Pharmacological action: unknownCell wall formation (By similarity) Organism class: bacterialUniProt ID: P61432 ![]() Gene: murB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 64. Flavohemoprotein Pharmacological action: unknownVarious electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if these reactions are of any biological significance in vivo Organism class: bacterialUniProt ID: P24232 ![]() Gene: hmp Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 65. Phenol 2-hydroxylase component B Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9LAG2 ![]() Gene: pheA2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 66. 5,10-methylenetetrahydrofolate reductase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9RA47 ![]() Gene: metF Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation Organism class: bacterialUniProt ID: P16640 ![]() Gene: camA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 68. PROBABLE DIHYDROLIPOAMIDE DEHYDROGENASE LPDA Pharmacological action: unknownOrganism class: bacterial UniProt ID: O53355 ![]() Gene: lpdA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 69. UDP-galactopyranose mutase Pharmacological action: unknownOrganism class: bacterial UniProt ID: O06934 ![]() Gene: glf Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 70. Gamma-aminobutyrate metabolism dehydratase/isomerase Pharmacological action: unknownCatalyzes the reversible conversion of 4-hydroxybutyryl- CoA to crotonyl-CoA. The mechanism of the reaction seems to go through three steps:(1) the FAD-dependent oxidation of 4- hydroxybutyryl-CoA to 4-hydroxycrotonyl-CoA; (2) the hydroxyl group is substituted by a hydride derived from the now reduced FAD in an SN2' reaction leading to vinylacetyl-CoA; (3) isomerization to yield crotonyl-CoA Organism class: bacterialUniProt ID: P55792 ![]() Gene: abfD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 71. 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit Pharmacological action: unknown4-cresol + acceptor + H(2)O = 4- hydroxybenzaldehyde + reduced acceptor Organism class: bacterialUniProt ID: P09788 ![]() Gene: pchF Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 72. Alkyl hydroperoxide reductase subunit F Pharmacological action: unknownServes to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the ahpC protein Organism class: bacterialUniProt ID: P19480 ![]() Gene: ahpF Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 73. Outer membrane protein p64k or PM-6 Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q51225 ![]() Gene: m-6 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Maintains high levels of reduced glutathione in the cytosol (By similarity) Organism class: parasiticUniProt ID: Q94655 ![]() Gene: GR2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 75. Phenylacetone monooxygenase Pharmacological action: unknownCatalyzes a Baeyer-Villiger oxidation reaction, i.e., the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4- hydroxyacetophenone), some alipatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide) Organism class: bacterialUniProt ID: Q47PU3 ![]() Gene: pamO Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 76. Benzoate 1,2-dioxygenase electron transfer component Pharmacological action: unknownElectron transfer component of benzoate 1,2-dioxygenase system Organism class: bacterialUniProt ID: P07771 ![]() Gene: benC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 77. Putative acyl-CoA dehydrogenase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q72JJ3 ![]() Gene: TT_C0779 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 78. FkbI Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9KIE5 ![]() Gene: fkbI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 79. Dihydrolipoyl dehydrogenase Pharmacological action: unknownThe branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) Organism class: bacterialUniProt ID: P09063 ![]() Gene: lpdV Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 80. Dihydrolipoyl dehydrogenase Pharmacological action: unknownThe branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) Organism class: bacterialUniProt ID: P14218 ![]() Gene: lpd Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 81. Alkyl hydroperoxide reductase subunit F Pharmacological action: unknownServes to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the ahpC protein Organism class: bacterialUniProt ID: P35340 ![]() Gene: ahpF Protein Sequence: FASTA SNPs: SNPJam Report ![]() 82. Ferredoxin--NADP reductase Pharmacological action: unknownReduced ferredoxin + NADP(+) = oxidized ferredoxin + NADPH Organism class: bacterialUniProt ID: P58558 ![]() Gene: petH Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 83. Ferredoxin--NADP reductase Pharmacological action: unknownTransports electrons between flavodoxin or ferredoxin and NADPH. Involved in the reductive activation of cobalamin- independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. Also protects against superoxide radicals due to methyl viologen in the presence of oxygen Organism class: bacterialUniProt ID: P28861 ![]() Gene: fpr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Catalyzes the oxidative decarboxylation of the C- terminal cysteine residue of mersacidin to an aminoenethiol residue Organism class: bacterialUniProt ID: Q9RC23 ![]() Gene: mrsD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 85. Fumarate reductase flavoprotein subunit Pharmacological action: unknownCatalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional Organism class: bacterialUniProt ID: P0C278 ![]() Gene: fccA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: |
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1. Amine oxidase [flavin-containing] B Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine UniProt ID: P27338![]() Gene: MAOB ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() |
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