Reviewed,
UniProtKB/Swiss-Prot B0Y7C3 (KMO_ASPFC)
Last modified
September 22, 2009.
Version 10.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Kynurenine 3-monooxygenase EC=1.14.13.9 Alternative name(s): Kynurenine 3-hydroxylase Biosynthesis of nicotinic acid protein 4 | ||||
| Gene names |
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| Organism | Aspergillus fumigatus (strain CEA10 / CBS 144.89 / FGSC A1163) (Sartorya fumigata) [Complete proteome] | ||||
| Taxonomic identifier | 451804 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 512 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid By similarity. |
| Catalytic activity | L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. |
| Cofactor | FAD By similarity. |
| Pathway | Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. |
| Subcellular location | Mitochondrion By similarity. |
| Sequence similarities | Belongs to the aromatic-ring hydroxylase family. KMO subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Cellular component | Mitochondrion |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | kynurenine 3-monooxygenase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 512 | 512 | Kynurenine 3-monooxygenase | PRO_0000361917 | |||
Sequences
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References
| [1] | "Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. Nierman W.C.PLoS Genet. 4:E1000046-E1000046(2008) [PubMed: 18404212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| DS499599 Genomic DNA. Translation: EDP49304.1. | |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002938. mOase_FAD_bd. IPR003042. Rng_hydrolase-like. [Graphical view] |
| Pfam | PF01494. FAD_binding_3. 1 hit. [Graphical view] |
| PRINTS | PR00420. RNGMNOXGNASE. |
| ProtoNet | Search... |
Entry information
| Entry name | KMO_ASPFC | ||||||||
| Accession | Primary (citable) accession number: B0Y7C3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


