Reviewed,
UniProtKB/Swiss-Prot A8Y432 (KMO_CAEBR)
Last modified
November 3, 2009.
Version 18.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Kynurenine 3-monooxygenase EC=1.14.13.9 Alternative name(s): Kynurenine 3-hydroxylase | ||
| Gene names |
| ||
| Organism | Caenorhabditis briggsae [Complete proteome] | ||
| Taxonomic identifier | 6238 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 461 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. Membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Belongs to the aromatic-ring hydroxylase family. KMO subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Cellular component | Membrane Mitochondrion |
| Domain | Transmembrane |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| 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
| ||||||||||||||||||
References
| [1] | "The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. Waterston R.H.PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16. |
Cross-references
Sequence databases | |
|---|---|
| CAAC02000606 Genomic DNA. Translation: CAP39652.1. | |
3D structure databases | |
| ModBase | Search... |
Organism-specific databases | |
| WormBase | WBGene00041735. CBG23368. |
Phylogenomic databases | |
| OMA | HTDVLAD. |
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_CAEBR | ||||||||
| Accession | Primary (citable) accession number: A8Y432 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Caenorhabditis annotation project | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


