fmn1 (SPCC18.16c; UniProt O74866) encodes riboflavin kinase (EC 2.7.1.26), which phosphorylates riboflavin to FMN with ATP, the first step in making flavin cofactors; FAD synthetase (nad1) then makes FAD. The 1.6 Å crystal structure of S. pombe riboflavin kinase, with ADP and FMN bound, defined a new beta-barrel phosphoryl-transfer fold. The enzyme is cytosolic in a genome-wide screen.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT inference of mitochondrial location from S. cerevisiae Fmn1, which has a mitochondrial pool; S. pombe Fmn1 is cytosolic in the ORFeome screen. Reason: Not established for S. pombe. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005743 mitochondrial inner membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Curator transfer from S. cerevisiae FMN1 (Q03778) inner-membrane association; not shown in S. pombe. Reason: Not established. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005829 cytosol | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: ORFeome YFP screen placed fmn1 in the cytosol, consistent with a soluble metabolic enzyme. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0006771 riboflavin metabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Broad parent. Supporting Evidence: PMID:12595258 Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. |
| GO:0008270 zinc ion binding | IDA PMID:12595258 Crystal structure of Schizosaccharomyces pombe riboflavin ki... | KEEP AS NON CORE | Summary: Metal ion (zinc in the crystal) at the active site; Mg2+ is the physiological kinase cofactor. Subsidiary. Supporting Evidence: PMID:12595258 Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. |
| GO:0008531 riboflavin kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; consistent. Supporting Evidence: PMID:12595258 Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. |
| GO:0008531 riboflavin kinase activity | IDA PMID:12595258 Crystal structure of Schizosaccharomyces pombe riboflavin ki... | ACCEPT | Summary: Crystal structure of S. pombe riboflavin kinase with ADP and FMN bound. Supporting Evidence: PMID:12595258 Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. PMID:12595258 The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. |
| GO:0008531 riboflavin kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EC/InterPro mapping; consistent. Supporting Evidence: PMID:12595258 Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. |
| GO:0009231 riboflavin biosynthetic process | IEA GO_REF:0000002 | REMOVE | Summary: InterPro mapping to riboflavin biosynthesis. Riboflavin kinase uses riboflavin to make FMN, downstream of riboflavin synthesis; FMN biosynthesis is the correct process. Reason: Riboflavin kinase consumes riboflavin, the end product of riboflavin biosynthesis, to make FMN; it performs no step in forming riboflavin. The InterPro2GO mapping of the riboflavin kinase domain to riboflavin biosynthesis is therefore wrong for this enzyme, as for S. cerevisiae FMN1 and the bacterial RibF proteins. The correct process, FMN biosynthesis, is already annotated. Supporting Evidence: PMID:12595258 The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. |
| GO:0009398 FMN biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; riboflavin -> FMN. Supporting Evidence: PMID:12595258 The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. |
| GO:0009398 FMN biosynthetic process | IDA PMID:12595258 Crystal structure of Schizosaccharomyces pombe riboflavin ki... | ACCEPT | Summary: Structure with product FMN. Supporting Evidence: PMID:12595258 The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. |
| GO:0009398 FMN biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: InterPro/UniPathway mapping; consistent. Supporting Evidence: PMID:12595258 The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. |
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