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Information on EC 1.5.1.37 - FAD reductase (NADH)
for references in articles please use BRENDA:EC1.5.1.37
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.1 With NAD+ or NADP+ as acceptor
1.5.1.37 FAD reductase (NADH)
IUBMB Comments
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
The enzyme appears in viruses and cellular organisms
- 1.5.1.37
- reductases
-
enediyne
-
two-component
-
peptidyl
-
protein-tethered
- chromophore
-
pathway-specific
-
burkholderia
- cepacia
- halogenase
-
halogenation
- globisporus
-
fadh2-dependent
-
chloro
-
4-monooxygenase
- chlorophenol
- 2,4,5-trichlorophenol
-
flavin-dependent
- fluorescens
-
arylamine
showSynonyms
sgce6, nadh-fad reductase, nadh:fad oxidoreductase, fad:nadh reductase, nad(p)h:fad reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
flavin reductase
flavin:NADH reductase
fre
Fred
NAD(P)H:FAD reductase
NADH-dependent FAD reductase
NADH-FAD reductase
NADH:FAD oxidoreductase
NADH:flavin adenine dinucleotide oxidoreductase
PrnF
TftC
NADH-dependent FAD reductase
-
-
-
-
NADH-FAD reductase
-
-
-
-
NADH:FAD oxidoreductase
-
-
-
-
NADH:flavin adenine dinucleotide oxidoreductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FADH2 + NAD+ = FAD + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
FADH2:NAD+ oxidoreductase
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lumiflavin + NADH + H+
reduced lumiflavin + NAD+
-
Substrates: 6% of the activity with FAD
Products: -
Products: -
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
Substrates: 9% of the activity with FAD
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
-
Substrates: FAD is a better substrate than FMN. The enzyme does not use NADPH or riboflavin as substrate
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
-
Substrates: the reductase catalyzes the reduction of FAD by NADH and releases the FADH- product into solution, but unlike the reductase from Actinetobacter baumannii, this catalysis is not influenced by p-hydroxyphenylacetate
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
-
Substrates: involved in pyrrolnitrin biosynthesis. PrnF is the flavin:NADH reductase component of the two-component arylamine oxygenase system in Pseudomonas fluorescens Pf-5. PrnF reduces FAD to FADH2, which is then directly transferred to PrnD, where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
-
Substrates: no activity with NADPH. PrnF reduces FAD to FADH2, which is then directly transferred to aminopyrrolnitrin oxygenase (PrnD), where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine. Other flavin reductases present in the host cell would not supplant the role of PrnF. The turnover rate of PrnD in the presence of PrnF is almost two times higher than that in the presence of the Escherichia coli flavin SsuE reductase (EC 1.5.1.29)
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
Substrates: FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
Substrates: FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
Substrates: the enzyme can adequately supply reduced flavin under saturating substrate conditions to support catalysis of flavin-dependent halogenase SgcC3 and monooxygenase SgcC during biosynthesis of C-1027
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
Substrates: strictly NADH- and FAD-specific enzyme: No activity with NADPH or FMN
Products: -
Products: -
?
FADH2 + NAD+
FAD + NADH + H+
-
Substrates: -
Products: -
Products: -
r
FADH2 + NAD+
FAD + NADH + H+
-
Substrates: -
Products: -
Products: -
r
FMN + NADH + H+
FMNH2 + NAD+
-
Substrates: FAD is a better substrate than FMN. The enzyme does not use NADPH or riboflavin as substrate
Products: -
Products: -
?
FMN + NADH + H+
FMNH2 + NAD+
-
Substrates: HpaC can reduce either FAD or FMN
Products: -
Products: -
?
FMN + NADH + H+
FMNH2 + NAD+
-
Substrates: 12% of the activity with FAD
Products: -
Products: -
?
FMN + NADH + H+
FMNH2 + NAD+
Substrates: FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
Products: -
Products: -
?
FMN + NADH + H+
FMNH2 + NAD+
Substrates: FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Fre can effectively dehalogenate dihalophenols. Degradation of dichlorophenol (DCP) structural analogues by recombinant 2,4,6-trichlorophenol monooxygenase (TcpA) with NAD(P)H:FAD reductase (Fre), substrate specificities with 2,3-dichlorophenol (2,3-DCP), 2,4-dichlorophenol (2,4-DCP), 2,5-dichlorophenol (2,5-DCP), 2,6-dichlorophenol (2,6-DCP), 3,4-dichlorophenol (3,4 DCP), and 3,5-dichlorophenol (3,5-DCP), overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: Fre can effectively dehalogenate dihalophenols. Degradation of dichlorophenol (DCP) structural analogues by recombinant 2,4,6-trichlorophenol monooxygenase (TcpA) with NAD(P)H:FAD reductase (Fre), substrate specificities with 2,3-dichlorophenol (2,3-DCP), 2,4-dichlorophenol (2,4-DCP), 2,5-dichlorophenol (2,5-DCP), 2,6-dichlorophenol (2,6-DCP), 3,4-dichlorophenol (3,4 DCP), and 3,5-dichlorophenol (3,5-DCP), overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: Fre can effectively dehalogenate dihalophenols. Degradation of dichlorophenol (DCP) structural analogues by recombinant 2,4,6-trichlorophenol monooxygenase (TcpA) with NAD(P)H:FAD reductase (Fre), substrate specificities with 2,3-dichlorophenol (2,3-DCP), 2,4-dichlorophenol (2,4-DCP), 2,5-dichlorophenol (2,5-DCP), 2,6-dichlorophenol (2,6-DCP), 3,4-dichlorophenol (3,4 DCP), and 3,5-dichlorophenol (3,5-DCP), overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: methylene blue and ferricyanide are less than 5% as effective as FAD
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FAD + NADH + H+
FADH2 + NAD+
-
Substrates: involved in pyrrolnitrin biosynthesis. PrnF is the flavin:NADH reductase component of the two-component arylamine oxygenase system in Pseudomonas fluorescens Pf-5. PrnF reduces FAD to FADH2, which is then directly transferred to PrnD, where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
Substrates: the enzyme can adequately supply reduced flavin under saturating substrate conditions to support catalysis of flavin-dependent halogenase SgcC3 and monooxygenase SgcC during biosynthesis of C-1027
Products: -
Products: -
?
FADH2 + NAD+
FAD + NADH + H+
-
Substrates: -
Products: -
Products: -
r
FADH2 + NAD+
FAD + NADH + H+
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
-
AMP exhibits competitive inhibition versus NADH and noncompetitive inhibition versus FAD
NAD+
-
NAD+ demonstrates competitive inhibition versus NADH and noncompetitive inhibition versus FAD
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.6
-
pH 5.0 (sodium succinate buffer): 52% of maximal activity, pH 7.6: 75% of maximal activity
6 - 8
-
pH 6.0: 73% of maximal activity, pH 8.0: 81% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23 - 45
-
23Ā°C: 85% of maximal activity, 45Ā°C: 70% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
the enzyme is involved in the degradation of (-)-camphor
metabolism
-
the enzyme is involved in the degradation of (-)-camphor
-
physiological function
free FADH2 is generated by NADH:FAD oxidoreductase (TftC), and FADH2-dependent monooxygenase (TftD) uses FADH2 to separately transform 2,4,5-trichlorophenol and 2,5-dichloro-p-hydroquinone
physiological function
-
TftD supplies FADH2 to (FADH2)-utilizing monooxygenase TftD, that converts 2,4,5-trichlorophenol to 2,5-dichloro-p-quinol and then to 5-chlorohydroxyquinol. It also converts 2,4,6-trichlorophenol to 2,6-dichloro-p-quinol as the final product
physiological function
the enzyme can adequately supply reduced flavin under saturating substrate conditions to support catalysis of flavin-dependent halogenase SgcC3 and monooxygenase SgcC during biosynthesis of C-1027
additional information
-
substitution of an NADH dehydrogenase (down-regulated) by an up-regulated NADH:FAD oxidoreductase and upregulation of an ATP synthase subunit, alongside the observed shifts in the TCA cycle, suggested that an oxygen-scavenging electron transport chain likely remains active during low redox conditions
additional information
-
the structure and active site of Fre is constructed and analyzed via homologous modeling and molecular docking
additional information
-
substitution of an NADH dehydrogenase (down-regulated) by an up-regulated NADH:FAD oxidoreductase and upregulation of an ATP synthase subunit, alongside the observed shifts in the TCA cycle, suggested that an oxygen-scavenging electron transport chain likely remains active during low redox conditions
-
additional information
-
the structure and active site of Fre is constructed and analyzed via homologous modeling and molecular docking
-
additional information
-
the structure and active site of Fre is constructed and analyzed via homologous modeling and molecular docking
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HPAC_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
170
0
18616
Swiss-Prot
-
A0A345DCB3_9BURK
164
0
18183
TrEMBL
-
A0A2C9D708_9HYPH
183
0
19886
TrEMBL
-
A0A6J5FW58_9BURK
181
0
19268
TrEMBL
-
A0A6J5BJH6_9BURK
171
0
18424
TrEMBL
-
A0A5B8RI66_9ZZZZ
176
0
18356
TrEMBL
other Location (Reliability: 2)
A0A6J5K5C2_9BURK
171
0
18293
TrEMBL
-
A0A644VLF5_9ZZZZ
172
0
18064
TrEMBL
other Location (Reliability: 4)
A0A5B8RCM7_9ZZZZ
193
0
20182
TrEMBL
Secretory Pathway (Reliability: 5)
A0A6A7SJ80_9ZZZZ
176
0
18356
TrEMBL
other Location (Reliability: 2)
A0A2Z2NMK9_9GAMM
179
0
18879
TrEMBL
-
A0A2S6QET4_9PROT
173
0
18782
TrEMBL
-
A0A1U9Z728_9HYPH
167
0
17277
TrEMBL
-
A0A6A7SGU9_9ZZZZ
193
0
20182
TrEMBL
Secretory Pathway (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the apparent molecular mass of the PrnD-PrnF complex appears to be approximately 120000 Da (gel filtration), confirming a 1:1 stoichiometry for binding of the two proteins, PrnD (86000 Da) and PrnF (39000 Da)