NADPH-dependent FMN reductase family protein contains a flavodoxin-like fold, which is characterized by an open twisted/alpha beta structure consisting of five parallel beta-sheets connected by alpha-helices which surround the sheet
FMN reductase, MsuE subfamily; Members of this protein family use NAD(P)H to reduce FMN and ...
6-177
1.70e-73
FMN reductase, MsuE subfamily; Members of this protein family use NAD(P)H to reduce FMN and regenerate FMNH2. Members include the NADH-dependent enzyme MsuE from Pseudomonas aeruginosa, which serves as a partner to an FMNH2-dependent alkanesulfonate monooxygenase. The NADP-dependent enzyme from E. coli is outside the scope of this model.
Pssm-ID: 211840 Cd Length: 174 Bit Score: 218.74 E-value: 1.70e-73
FMN reductase, MsuE subfamily; Members of this protein family use NAD(P)H to reduce FMN and ...
6-177
1.70e-73
FMN reductase, MsuE subfamily; Members of this protein family use NAD(P)H to reduce FMN and regenerate FMNH2. Members include the NADH-dependent enzyme MsuE from Pseudomonas aeruginosa, which serves as a partner to an FMNH2-dependent alkanesulfonate monooxygenase. The NADP-dependent enzyme from E. coli is outside the scope of this model.
Pssm-ID: 211840 Cd Length: 174 Bit Score: 218.74 E-value: 1.70e-73
LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within ...
6-178
5.91e-36
LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within pfam03358. That family includes enzymes such as the NADH-dependent FMN reductase MsuE. Members of the present family regularly co-occur in genomes, typically as gene pairs, with members of TIGR04036, a probable FMN-dependent member of the bacterial luciferase-like monooxygenase (LLM) family. At least one member, RF|YP_001509627.1 from Frankia sp. EAN1pec, is fused to the LLM protein. The function of these gene pairs is unknown.
Pssm-ID: 274935 Cd Length: 198 Bit Score: 124.31 E-value: 5.91e-36
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
5-171
1.30e-06
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.
Pssm-ID: 426816 [Multi-domain] Cd Length: 193 Bit Score: 46.56 E-value: 1.30e-06
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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