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
ECTree
Advanced search results
Subunits
Subunits on EC 1.5.1.39 - FMN reductase [NAD(P)H]
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
flavin-bound wild-type enzyme, and enzyme mutant Y118A and DELTAY118
monomer
additional information
ChuY exists as a monomer in solution, SDS-PAGE and gel filtration
monomer
-
ChuY exists as a monomer in solution, SDS-PAGE and gel filtration
-
monomer
Lacticaseibacillus rhamnosus ATCC 53103
-
1 * 42000, recombinant His-tagged enzyme, SDS-PAGE
-
the two molecules in the asymmetric unit are related by pseudo 2fold rotation symmetry. ChuY contains six alpha-helices and ten beta-strands. A central beta-sheet, consisting of seven parallel beta-strands, beta1, beta2, beta3, beta4, beta5, beta6, and beta10, is flanked by six alpha-helices, forming alternating beta-strand and alpha-helix repeats, which is a representative feature of Rossmann folds. Three other beta-strands (beta7-beta9) are located on the top of the beta-sheet
additional information
the tetramer of enzyme SsuE binds FMN, and dissociates to a dimer. In a flavin-bound SsuE structure, the hydroxyl group of Tyr118 hydrogen bonds to the oxygen atom backbone carbonyl of Ala78 across the tetramer interface
additional information
-
the two molecules in the asymmetric unit are related by pseudo 2fold rotation symmetry. ChuY contains six alpha-helices and ten beta-strands. A central beta-sheet, consisting of seven parallel beta-strands, beta1, beta2, beta3, beta4, beta5, beta6, and beta10, is flanked by six alpha-helices, forming alternating beta-strand and alpha-helix repeats, which is a representative feature of Rossmann folds. Three other beta-strands (beta7-beta9) are located on the top of the beta-sheet
-
additional information
-
the conserved protein fold of LrFOR is comprised of about eight alpha-helices and eight parallel beta-strands that alternate along the peptide backbones (A (beta/alpha) 8 barrel)
additional information
Lacticaseibacillus rhamnosus ATCC 53103
-
the conserved protein fold of LrFOR is comprised of about eight alpha-helices and eight parallel beta-strands that alternate along the peptide backbones (A (beta/alpha) 8 barrel)
-