Q0CRI5 (KMO_ASPTN) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 30.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Kynurenine 3-monooxygenase EC=1.14.13.9 Alternative name(s): Biosynthesis of nicotinic acid protein 4 Kynurenine 3-hydroxylase | ||||
| Gene names |
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| Organism | Aspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome] | ||||
| Taxonomic identifier | 341663 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 500 AA. |
| Sequence status | Complete. |
| 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 | pyridine nucleotide biosynthetic process Inferred 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 – 500 | 500 | Kynurenine 3-monooxygenase | PRO_0000361923 | |||
Sequences
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References
| [1] | "Annotation of the Aspergillus terreus NIH2624 genome." Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K. Madden K.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NIH 2624 / FGSC A1156. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CH476598 Genomic DNA. Translation: EAU35501.1. |
| RefSeq | XP_001212877.1. XM_001212877.1. |
3D structure databases | |
| ProteinModelPortal | Q0CRI5. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADATEAT00009639; CADATEAP00009639; CADATEAG00009639. |
| GeneID | 4318193. |
Phylogenomic databases | |
| GeneTree | EFGT00050000002229. |
| OrthoDB | EOG4QG0P2. |
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_ASPTN | ||||||||
| Accession | Primary (citable) accession number: Q0CRI5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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