| UniProt ID | KMO_YEAST | |
|---|---|---|
| UniProt AC | P38169 | |
| Protein Name | Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_03018} | |
| Gene Name | BNA4 {ECO:0000255|HAMAP-Rule:MF_03018} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 460 | |
| Subcellular Localization | Mitochondrion outer membrane . | |
| Protein Description | Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.. | |
| Protein Sequence | MSESVAIIGAGLVGCLAALAFSKEGYNVTLYDFRQDPRLDTTKNKNLKSINLAISARGIDALKSIDPDACEHILQDMIPMKGRMIHDLKGRQESQLYGLHGEAINSINRSVLNNSLLDELEKSTTELKFGHKLVKIEWTDDKQICHFAIGEDLKTPHTEKYDFVIGCDGAYSATRSQMQRKVEMDFSQEYMNLRYIELYIPPTEEFKPNYGGNFAIAPDHLHIWPRHKFMLIALANSDGSFTSTFFGSKDQISDLITSKSRVREFLIENFPDIINIMDLDDAVKRFITYPKESLVCVNCKPYDVPGGKAILLGDAAHAMVPFYGQGMNCGFEDVRILMALLKKHSGDRSRAFTEYTQTRHKDLVSITELAKRNYKEMSHDVTSKRFLLRKKLDALFSIIMKDKWIPLYTMISFRSDISYSRALERAGKQTRILKFLESLTLGMLSIGGYKLFKFLTRERS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Oxidation | -------MSESVAII -------CCCCEEEE | 10.14 | 15665377 | |
| 2 | Phosphorylation | ------MSESVAIIG ------CCCCEEEEH | 38.28 | 28889911 | |
| 4 | Phosphorylation | ----MSESVAIIGAG ----CCCCEEEEHHH | 15.00 | 15665377 | |
| 22 | Phosphorylation | CLAALAFSKEGYNVT HHHHHHHCCCCCCEE | 24.96 | 15665377 | |
| 89 | Ubiquitination | GRMIHDLKGRQESQL CCCCCCCCCCCHHHH | 59.09 | 17644757 | |
| 122 | Ubiquitination | SLLDELEKSTTELKF HHHHHHHHHCCCCCC | 66.77 | 17644757 | |
| 207 | Ubiquitination | IPPTEEFKPNYGGNF CCCCHHCCCCCCCCC | 35.32 | 17644757 | |
| 259 | Ubiquitination | ISDLITSKSRVREFL HHHHHHCHHHHHHHH | 33.36 | 24961812 | |
| 397 | Phosphorylation | KKLDALFSIIMKDKW HHHHHHHHHHHCCCC | 16.44 | 19795423 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of KMO_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KMO_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of KMO_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-22, AND MASSSPECTROMETRY. | |