| EC |
2.7.1.180 |
| Accepted name: |
FAD:protein FMN transferase |
| Reaction: |
FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP |
| Other name(s): |
flavin transferase; apbE (gene name) |
| Systematic name: |
FAD:protein riboflavin-5′-phosphate transferase |
| Comments: |
The enzyme catalyses the transfer of the FMN portion of FAD and its covalent binding to the hydroxyl group of an L-threonine residue in a target flavin-binding protein such as the B and C subunits of EC 7.2.1.1, NADH:ubiquinone reductase (Na+-transporting). Requires Mg2+. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Bertsova, Y.V., Fadeeva, M.S., Kostyrko, V.A., Serebryakova, M.V., Baykov, A.A. and Bogachev, A.V. Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins. J. Biol. Chem. 288 (2013) 14276–14286. [PMID: 23558683] |
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| [EC 2.7.1.180 created 2013, modified 2018] |
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