Reviewed,
UniProtKB/Swiss-Prot Q5B2N0 (KMO_EMENI)
Last modified
September 22, 2009.
Version 38.
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 |
| ||||
| Organism | Emericella nidulans (Aspergillus nidulans) [Complete proteome] | ||||
| Taxonomic identifier | 162425 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 506 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. |
| Sequence caution | The sequence EAA62381.1 differs from that shown. Reason: Erroneous gene model prediction. |
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 – 506 | 506 | Kynurenine 3-monooxygenase | PRO_0000361928 | |||
Sequences
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References
| [1] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4. |
Cross-references
Sequence databases | |
|---|---|
| AACD01000089 Genomic DNA. Translation: EAA62381.1. Sequence problems. | |
| RefSeq | XP_662804.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2871494. |
| KEGG | ani:AN5200.2. |
Family and domain databases | |
| InterPro | IPR003042. Rng_hydrolase-like. [Graphical view] |
| PRINTS | PR00420. RNGMNOXGNASE. |
| ProtoNet | Search... |
Entry information
| Entry name | KMO_EMENI | ||||||||
| Accession | Primary (citable) accession number: Q5B2N0 | ||||||||
| 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


