Reviewed,
UniProtKB/Swiss-Prot Q2UJE8 (KYNU2_ASPOR)
Last modified
February 9, 2010.
Version 27.
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: Kynureninase 2 EC=3.7.1.3 Alternative name(s): L-kynurenine hydrolase 2 Biosynthesis of nicotinic acid protein 5-2 | ||||
| Gene names |
| ||||
| Organism | Aspergillus oryzae [Complete proteome] | ||||
| Taxonomic identifier | 5062 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 468 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 – 468 | 468 | Kynureninase 2 | PRO_0000356970 | |||||
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
| ||||||||||||||||||
References
| [1] | "Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. Kikuchi H.Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP007155 Genomic DNA. Translation: BAE58317.1. |
| RefSeq | XP_001820319.1. |
3D structure databases | |
| SMR | Q2UJE8. Positions 14-462. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5992302. |
| GenomeReviews | Gene locus bna5-2 in contig AP007155_GR. |
| KEGG | aor:AO090003001247. |
Phylogenomic databases | |
| OrthoDB | EOG9RZ0G9. |
| PhylomeDB | Q2UJE8. |
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 | KYNU2_ASPOR | ||||||||
| Accession | Primary (citable) accession number: Q2UJE8 | ||||||||
| 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


