A2QJI5 (KYNU2_ASPNC) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 35.
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: Kynureninase 2 EC=3.7.1.3 Alternative name(s): Biosynthesis of nicotinic acid protein 5-2 L-kynurenine hydrolase 2 | ||||
| Gene names |
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| Organism | Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome] | ||||
| Taxonomic identifier | 425011 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 463 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 – 463 | 463 | Kynureninase 2 | PRO_0000356968 | |||||
Regions | |||||||||
| Region | 162 – 165 | 4 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 134 | 1 | Pyridoxal phosphate; via amide nitrogen By similarity | ||||||
| Binding site | 135 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 247 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 250 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 272 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 312 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 340 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 273 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. Stam H.Nat. Biotechnol. 25:221-231(2007) [PubMed: 17259976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM270081 Genomic DNA. Translation: CAK44720.1. |
| RefSeq | XP_001402081.1. XM_001402044.2. |
3D structure databases | |
| ProteinModelPortal | A2QJI5. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADANGAT00004431; CADANGAP00004336; CADANGAG00004431. |
| GeneID | 4991124. |
| GenomeReviews | Gene locus bna5-2 in contig AM270983_GR. |
| KEGG | ang:ANI_1_1148184. |
Phylogenomic databases | |
| GeneTree | EFGT00050000005118. |
| HOGENOM | HBG523016. |
| OrthoDB | EOG4TB7KQ. |
Family and domain databases | |
| InterPro | IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits. |
| KO | K01556. |
| PANTHER | PTHR14084. Kynureninase. 1 hit. |
| Pfam | PF00266. Aminotran_5. 1 hit. [Graphical view] |
| PIRSF | PIRSF038800. KYNU. 1 hit. |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| TIGRFAMs | TIGR01814. Kynureninase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | KYNU2_ASPNC | ||||||||
| Accession | Primary (citable) accession number: A2QJI5 | ||||||||
| 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 |

Clusters with