| Official Name |
| FMN reductase.
|
| Alternative Name(s) |
| Flavin mononucleotide reductase. |
| Flavine mononucleotide reductase. |
| NAD(P)H dehydrogenase (FMN). |
| NAD(P)H(2) dehydrogenase (FMN). |
| NAD(P)H(2):FMN oxidoreductase. |
| NAD(P)H-dependent FMN reductase. |
| NAD(P)H-FMN reductase. |
| NAD(P)H:flavin oxidoreductase. |
| NAD(P)H:FMN oxidoreductase. |
| Riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide
(phosphate)) reductase. |
| Riboflavin mononucleotide reductase. |
| Riboflavine mononucleotide reductase. |
| Reaction catalysed |
| FMNH(2) + NAD(P)(+) <=> FMN + NAD(P)H |
| Comment(s) |
- The enzyme from luminescent bacteria and the SsuE enzyme from
Escherichia coli also reduce riboflavin and FAD, but more slowly.
- In E.coli, this enzyme, in conjunction with EC 1.14.14.5, forms a
two-component alkanesulfonate monooxygenase, which allows for
utilization of alkanesulfonates as sulfur sources under conditions of
sulfate and cysteine starvation.
- Formerly EC 1.6.8.1.
|
| Cross-references |
| BRENDA | 1.5.1.29 |
| PUMA2 | 1.5.1.29 |
| PRIAM enzyme-specific profiles | 1.5.1.29 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.5.1.29 |
| IUBMB Enzyme Nomenclature | 1.5.1.29 |
| IntEnz | 1.5.1.29 |
| MEDLINE | Find literature relating to 1.5.1.29 |
| MetaCyc | 1.5.1.29 |
| UniProtKB/Swiss-Prot |
| Q9USJ6, FMNR_SCHPO; | P0AEN3, FRE_ECO57; | P0AEN2, FRE_ECOL6; |
| P0AEN1, FRE_ECOLI; | Q9L6L9, FRE_SALTY; | Q07923, LOT6_YEAST; |
| O31038, MSUE_PSEAE; | Q88J85, MSUE_PSEPK; | P80644, SSUE_ECOLI; |
| Q88R97, SSUE_PSEPK; | O85762, SSUE_PSEPU; |
|