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Literature summary for 1.5.1.30 extracted from

  • Deeva, A.; Zykova, E.; Nemtseva, E.; Kratasyuk, V.
    Functional divergence between evolutionary-related LuxG and Fre oxidoreductases of luminous bacteria (2019), Proteins, 87, 723-729 .
    View publication on PubMed
Search for more literature for 1.5.1.30

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FAD + NADPH + H+ Vibrio harveyi
-
 FADH2 + NADP+
-
 ?
FAD + NADPH + H+ Photorhabdus luminescens
-
 FADH2 + NADP+
-
 ?
FMN + NADPH + H+ Vibrio harveyi
-
 FMNH2 + NADP+
-
 ?
FMN + NADPH + H+ Photorhabdus luminescens
-
 FMNH2 + NADP+
-
 ?
riboflavin + NADPH + H+ Vibrio harveyi
-
 reduced riboflavin + NADP+
-
 ?
riboflavin + NADPH + H+ Photorhabdus luminescens
-
 reduced riboflavin + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Photorhabdus luminescens P43129
-
-
Vibrio harveyi B2XS34
-
-
Vibrio harveyi P43126
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD + NADPH + H+
-
 Vibrio harveyi FADH2 + NADP+
-
 ?
FAD + NADPH + H+
-
 Photorhabdus luminescens FADH2 + NADP+
-
 ?
FMN + NADPH + H+
-
 Vibrio harveyi FMNH2 + NADP+
-
 ?
FMN + NADPH + H+
-
 Photorhabdus luminescens FMNH2 + NADP+
-
 ?
riboflavin + NADPH + H+
-
 Vibrio harveyi reduced riboflavin + NADP+
-
 ?
riboflavin + NADPH + H+
-
 Photorhabdus luminescens reduced riboflavin + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
fre
-
 Vibrio harveyi
fre
-
 Photorhabdus luminescens
LuxG
-
 Vibrio harveyi
More see also EC 1.5.1.36 Vibrio harveyi
More see also EC 1.5.1.36 Photorhabdus luminescens
NAD(P)H:flavin-oxidoreductase
-
 Vibrio harveyi
NAD(P)H:flavin-oxidoreductase
-
 Photorhabdus luminescens

Cofactor

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
NADPH
-
 Vibrio harveyi
NADPH
-
 Photorhabdus luminescens

General Information

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 (ie, 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 (ie, 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 (ie, 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 (ie, 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