Reviewed,
UniProtKB/Swiss-Prot Q5B0H8 (KYNU1_EMENI)
Last modified
February 9, 2010.
Version 27.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Kynureninase 1 EC=3.7.1.3 Alternative name(s): L-kynurenine hydrolase 1 Biosynthesis of nicotinic acid protein 5-1 | ||||
| Gene names |
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| 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 | 487 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity. |
| Catalytic activity | L-kynurenine + H2O = anthranilate + L-alanine. L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the kynureninase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | NAD biosynthetic process Inferred from electronic annotation. Source: InterPro tryptophan catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | kynureninase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 487 | 487 | Kynureninase 1 | PRO_0000356977 | |||||
Regions | |||||||||
| Region | 177 – 180 | 4 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 149 | 1 | Pyridoxal phosphate; via amide nitrogen By similarity | ||||||
| Binding site | 150 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 263 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 266 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 288 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 329 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 357 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 289 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
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 A4 / M139. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AACD01000101 Genomic DNA. Translation: EAA57815.1. |
| RefSeq | XP_663556.1. |
3D structure databases | |
| SMR | Q5B0H8. Positions 22-478. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2870933. |
| KEGG | ani:AN5952.2. |
Phylogenomic databases | |
| PhylomeDB | Q5B0H8. |
Family and domain databases | |
| InterPro | IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| PANTHER | PTHR14084. Kynureninase. 1 hit. |
| Pfam | PF00266. Aminotran_5. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01814. kynureninase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | KYNU1_EMENI | ||||||||
| Accession | Primary (citable) accession number: Q5B0H8 | ||||||||
| Entry history |
| ||||||||
| 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


