Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
flavin + NADH + H+ | Vibrio harveyi | - |
reduced flavin + NAD+ | - |
? | |
flavin + NADH + H+ | Photorhabdus luminescens | - |
reduced flavin + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Photorhabdus luminescens | P43129 | - |
- |
Vibrio harveyi | B2XS34 | - |
- |
Vibrio harveyi | P43127 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FAD + NADH + H+ | - |
Vibrio harveyi | FADH2 + NAD+ | - |
? | |
FAD + NADH + H+ | - |
Photorhabdus luminescens | reduced FADH2 + NAD+ | - |
? | |
flavin + NADH + H+ | - |
Vibrio harveyi | reduced flavin + NAD+ | - |
? | |
flavin + NADH + H+ | - |
Photorhabdus luminescens | reduced flavin + NAD+ | - |
? | |
FMN + NADH + H+ | - |
Vibrio harveyi | FMNH2 + NAD+ | - |
? | |
FMN + NADH + H+ | - |
Photorhabdus luminescens | FMNH2 + NAD+ | - |
? | |
riboflavin + NADH + H+ | - |
Vibrio harveyi | reduced riboflavin + NAD+ | - |
? | |
riboflavin + NADH + H+ | - |
Photorhabdus luminescens | reduced riboflavin + NAD+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
fre | - |
Vibrio harveyi |
fre | - |
Photorhabdus luminescens |
LuxG | - |
Vibrio harveyi |
More | see also EC 1.5.1.30 | Vibrio harveyi |
More | see also EC 1.5.1.30 | Photorhabdus luminescens |
NAD(P)H:flavin-oxidoreductase | - |
Vibrio harveyi |
NAD(P)H:flavin-oxidoreductase | - |
Photorhabdus luminescens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the nicotinamide ribose phosphate part of NAD(P)H plays a major role in binding to Fre, whereas the impact of adenosine phosphate part is negligible | Vibrio harveyi | |
additional information | the nicotinamide ribose phosphate part of NAD(P)H plays a major role in binding to Fre, whereas the impact of adenosine phosphate part is negligible | Photorhabdus luminescens | |
NADH | - |
Vibrio harveyi | |
NADH | - |
Photorhabdus luminescens |
General Information | Comment | Organism |
---|---|---|
evolution | in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning | Vibrio harveyi |
evolution | in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning | Photorhabdus luminescens |
metabolism | in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate | Vibrio harveyi |
metabolism | in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate | Photorhabdus luminescens |
additional information | enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases | Vibrio harveyi |
additional information | enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases | Photorhabdus luminescens |