Reviewed,
UniProtKB/Swiss-Prot Q05979 (KYNU_YEAST)
Last modified
February 9, 2010.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Kynureninase EC=3.7.1.3 Alternative name(s): L-kynurenine hydrolase Biosynthesis of nicotinic acid protein 5 | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 453 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
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. Ref.2 |
| Catalytic activity | L-kynurenine + H2O = anthranilate + L-alanine. L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. Ref.2 Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. Ref.2 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | |
| Miscellaneous | Present with 3060 molecules/cell in log phase SD medium. Ref.4 |
| Sequence similarities | Belongs to the kynureninase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| Cellular component | Cytoplasm Nucleus |
| Ligand | Pyridoxal phosphate |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | de novo NAD biosynthetic process from tryptophan Ref.2 Inferred from genetic interaction. Source: SGD tryptophan catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Ref.3 Inferred from direct assay. Source: SGD nucleus Ref.3Inferred from direct assay. Source: SGD |
| Molecular function | kynureninase activity Ref.2 Inferred from mutant phenotype. Source: SGD protein bindingInferred from physical interaction. Source: IntAct pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| P43582 | 1 | EBI-10016,EBI-22766 | ||
| ESS1 | P22696 | 1 | EBI-10016,EBI-6679 | |
| PRP40 | P33203 | 1 | EBI-10016,EBI-701 | |
| RSP5 | P39940 | 1 | EBI-10016,EBI-16219 | |
| SSM4 | P40318 | 1 | EBI-10016,EBI-18208 | |
| URN1 | Q06525 | 1 | EBI-10016,EBI-35138 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 453 | 453 | Kynureninase | PRO_0000218665 | |||||
Regions | |||||||||
| Region | 139 – 142 | 4 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 111 | 1 | Pyridoxal phosphate; via amide nitrogen By similarity | ||||||
| Binding site | 112 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 226 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 229 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 251 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 286 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 314 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 252 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U19027 Genomic DNA. Translation: AAB67417.1. |
| PIR | S51453. |
| RefSeq | NP_013332.1. |
3D structure databases | |
| SMR | Q05979. Positions 3-451. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-6518N. |
| IntAct | Q05979. 7 interactions. |
| STRING | Q05979. |
Proteomic databases | |
| PeptideAtlas | Q05979. |
Genome annotation databases | |
| Ensembl | YLR231C; YLR231C; YLR231C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 850933. |
| KEGG | sce:YLR231C. |
| NMPDR | fig|4932.3.peg.4345. |
Organism-specific databases | |
| CYGD | YLR231c. |
| SGD | S000004221. BNA5. |
Phylogenomic databases | |
| eggNOG | fuNOG06509. |
| HOGENOM | HBG523016. |
| OMA | FAVGCTY. |
| OrthoDB | EOG9RZ0G9. |
| PhylomeDB | Q05979. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-8163. |
| BRENDA | 3.7.1.3. 250. |
Gene expression databases | |
| ArrayExpress | Q05979. |
| Genevestigator | Q05979. |
| GermOnline | YLR231C. Saccharomyces cerevisiae. |
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... |
Other Resources | |
| NextBio | 967372. |
Entry information
| Entry name | KYNU_YEAST | ||||||||
| Accession | Primary (citable) accession number: Q05979 | ||||||||
| Entry history |
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| 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 |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


