1.5.1.39: FMN reductase [NAD(P)H]
This is an abbreviated version!
For detailed information about FMN reductase [NAD(P)H], go to the full flat file.
Reaction
Synonyms
ChuY, EC 1.5.1.29, EC 1.6.8.1, flavin mononucleotide reductase, FMN reductase, fre, FRG, H2O-forming FOR, LrFOR, NAD(P)H-flavin reductase, NAD(P)H:FMN-oxidoreductase, NADH: FMN oxidoreductase, NADPH-dependent FMN reductase, NfoR, non-specific NAD(P)H-FMN reductase, pden_5119, Red, SsuE, two-component FMN-dependent monooxygenase, water forming NADH: FMN oxidoreductase
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General Information
General Information on EC 1.5.1.39 - FMN reductase [NAD(P)H]
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evolution
malfunction
physiological function
additional information
gene chuY is highly conserved in a broad range of pathogenic bacteria
evolution
comparison of wild-type and Y118A variants of SsuE with related wild-type and mutant H126Y MsuE from Pseudomonas fluorescens (EC 1.5.1.42), overview
evolution
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NADH: FMN oxidoreductases (FOR) are old yellow enzyme members with a (beta/alpha) 8-barrel structure and can catalyze the oxidation of NADH to NAD+ with the flavin mononucleotide (FMN) functions as the prosthetic group
evolution
the Pden_5119 protein is closely related to the SsuE and MsuE FRs that are parts of the two-component flavin-dependent monooxygenase systems involved in oxygenolytic cleavage of alkanesulfonates into aldehyde and sulfite
evolution
Lacticaseibacillus rhamnosus ATCC 53103
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NADH: FMN oxidoreductases (FOR) are old yellow enzyme members with a (beta/alpha) 8-barrel structure and can catalyze the oxidation of NADH to NAD+ with the flavin mononucleotide (FMN) functions as the prosthetic group
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evolution
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the Pden_5119 protein is closely related to the SsuE and MsuE FRs that are parts of the two-component flavin-dependent monooxygenase systems involved in oxygenolytic cleavage of alkanesulfonates into aldehyde and sulfite
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evolution
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gene chuY is highly conserved in a broad range of pathogenic bacteria
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a chuY deletion-insertion strain shows reduced survival potential compared to wild-type and complemented strains in mammalian cells
malfunction
inactivation of the pden_5119 gene increases susceptibility to oxidative stress, decreases growth rate and increases growth yield of Paracoccus denitrificans, growth on lower alkanesulfonates as sulfur sources is not specifically influenced. Changes in growth on alkanesulfonates and sulfate occurring as a result of mutation indicate that the Pden_5119 protein is not an obligatory component in the desulfurization pathway
malfunction
unlike wild-type SsuE, which crystallizes as a tetramer, the Tyr118 variant structures determined here all crystallize as dimers. The Pi-helices do not contribute to the dimeric assembly, and the variants show no difference at the dimeric interface compared to wild-type. While the Y118A SsuE variant clearly cannot hydrogen bond to Ala78 through the deleted hydroxyl, the Ala78-FMN hydrogen bond remains intact and the loop containing Ala78 has not shifted in conformation. The structure of the loop containing Ala78 is also maintained in the DELTA118 SsuE structure.
malfunction
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inactivation of the pden_5119 gene increases susceptibility to oxidative stress, decreases growth rate and increases growth yield of Paracoccus denitrificans, growth on lower alkanesulfonates as sulfur sources is not specifically influenced. Changes in growth on alkanesulfonates and sulfate occurring as a result of mutation indicate that the Pden_5119 protein is not an obligatory component in the desulfurization pathway
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malfunction
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a chuY deletion-insertion strain shows reduced survival potential compared to wild-type and complemented strains in mammalian cells
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ChuY has flavin mononucleotide (FMN) reductase activity, using NAD(P)H as a cofactor, and shows porphyrin ring binding affinity. ChuY acts as a reductase in heme homeostasis to maintain the virulence potential of Escherichia coli strain CFT073
physiological function
NfoR, an enzyme claimed to be a chromate reductase, is in fact an FMN reductase
physiological function
role for the Pden_5119 protein in maintaining the cellular redox state. The Pden_5119 protein confers increased resistance to oxidative stress. Dispensability of the Pden_5119 protein in sulfur acquisition from alkanesulfonates
physiological function
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role for the Pden_5119 protein in maintaining the cellular redox state. The Pden_5119 protein confers increased resistance to oxidative stress. Dispensability of the Pden_5119 protein in sulfur acquisition from alkanesulfonates
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physiological function
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ChuY has flavin mononucleotide (FMN) reductase activity, using NAD(P)H as a cofactor, and shows porphyrin ring binding affinity. ChuY acts as a reductase in heme homeostasis to maintain the virulence potential of Escherichia coli strain CFT073
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enzyme structure homology modeling and docking using the structure of Thermoanaerobacter pseudethanolicus strain E39 enzyme (PDB ID 3KRZ) as the template, overview. Molecular dynamic simulation
additional information
the functioning of NAD(P)H:FMN-oxidoreductase (Red) from Vibrio fischeri is not affected under conditions of macromolecular crowding (MMC) simulated in vitro by adding biopolymers (starch and gelatin). The functioning of Red both under conditions of MMC and in diluted solutions is the same
additional information
the Pi-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The Pi-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved alpha4-helix. Enzyme-substrate binding structure analysis. In the wild-type structure, a hydrogen bond forms between the Tyr118 and a carbonyl oxygen of Ala78 from the opposing dimer, which in turn hydrogen bonds to the isoalloxazine ring system of the FMN. This network is hypothesized to aid in communication between the oligomerization interface and FMN binding
additional information
Lacticaseibacillus rhamnosus ATCC 53103
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enzyme structure homology modeling and docking using the structure of Thermoanaerobacter pseudethanolicus strain E39 enzyme (PDB ID 3KRZ) as the template, overview. Molecular dynamic simulation
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