Reviewed,
UniProtKB/Swiss-Prot Q84HF5 (KMO_PSEFL)
Last modified
September 22, 2009.
Version 31.
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 Short name=PfKMO EC=1.14.13.9 Alternative name(s): Kynurenine 3-hydroxylase | ||||
| Gene names |
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| Organism | Pseudomonas fluorescens | ||||
| Taxonomic identifier | 294 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 461 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Probably required for the synthesis of quinolinic acid and the siderophore quinolobactin. Ref.1 |
| Catalytic activity | L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. Ref.2 |
| Cofactor | FAD. Ref.2 |
| Pathway | Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. Ref.1 |
| Sequence similarities | Belongs to the aromatic-ring hydroxylase family. KMO subfamily. |
| Biophysicochemical properties | Kinetic parameters: KM=11.8 µM for L-kynurenine (at 25 degrees Celsius) KM=8.5 µM for NADPH (at 25 degrees Celsius) KM=34.2 µM for oxygen (at 25 degrees Celsius) pH dependence: Optimum pH is 8.5. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 461 | 461 | Kynurenine 3-monooxygenase | PRO_0000361942 | |||
Sequences
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References
| [1] | "The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic acid, an intermediate of the kynurenine pathway." Matthijs S., Baysse C., Koedam N., Tehrani K.A., Verheyden L., Budzikiewicz H., Schaefer M., Hoorelbeke B., Meyer J.-M., De Greve H., Cornelis P. Mol. Microbiol. 52:371-384(2004) [PubMed: 15066027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, PATHWAY. Strain: ATCC 17400. |
| [2] | "Heterologous expression and purification of kynurenine-3-monooxygenase from Pseudomonas fluorescens strain 17400." Crozier K.R., Moran G.R. Protein Expr. Purif. 51:324-333(2007) [PubMed: 16973376] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 17400. |
Cross-references
Sequence databases | |
|---|---|
| AY271621 Genomic DNA. Translation: AAL65289.1. | |
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_PSEFL | ||||||||
| Accession | Primary (citable) accession number: Q84HF5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


