Reviewed,
UniProtKB/Swiss-Prot Q1RLY6 (KMO_DANRE)
Last modified
October 13, 2009.
Version 33.
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 | ||||
| Gene names |
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| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) | ||||
| Taxonomic identifier | 7955 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio |
Protein attributes
| Sequence length | 474 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
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 outer membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the aromatic-ring hydroxylase family. KMO subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Cellular component | Membrane Mitochondrion Mitochondrion outer membrane |
| Domain | Transmembrane |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | NAD metabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membraneInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | kynurenine 3-monooxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | NIH - Zebrafish Gene Collection (ZGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| BC115227 mRNA. Translation: AAI15228.1. | |
| IPI | IPI00921737. |
| UniGene | Dr.79892 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1RLY6. |
Proteomic databases | |
| PRIDE | Q1RLY6. |
Genome annotation databases | |
| Ensembl | ENSDART00000003706; ENSDARP00000024051; ENSDARG00000009160; Danio rerio. [Genome view] |
Organism-specific databases | |
| ZFIN | ZDB-GENE-030424-4. kmo. |
Phylogenomic databases | |
| HOGENOM | Q1RLY6. |
| HOVERGEN | Q1RLY6. |
Gene expression databases | |
| ArrayExpress | Q1RLY6. |
| Bgee | Q1RLY6. |
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_DANRE | ||||||||
| Accession | Primary (citable) accession number: Q1RLY6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Zebrafish annotation project | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


