Q2H7G2 (KYNU2_CHAGB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 33.
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 |
| ||||
| Organism | Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus) [Complete proteome] | ||||
| Taxonomic identifier | 306901 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › Chaetomium |
Protein attributes
| Sequence length | 539 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 – 539 | 539 | Kynureninase 2 | PRO_0000356975 | |||||
Regions | |||||||||
| Region | 199 – 202 | 4 | Pyridoxal phosphate binding By similarity | ||||||
| Compositional bias | 321 – 381 | 61 | Gly-rich | ||||||
Sites | |||||||||
| Binding site | 171 | 1 | Pyridoxal phosphate; via amide nitrogen By similarity | ||||||
| Binding site | 172 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 290 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 293 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 315 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 379 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 407 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 316 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Annotation of the Chaetomium globosum CBS 148.51 genome." The Broad Institute Genome Sequencing Platform Birren B.W., Lander E.S., Galagan J.E., Devon K., Nusbaum C., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., Pushparaj V. Untereiner W.Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CH408031 Genomic DNA. Translation: EAQ88784.1. |
| RefSeq | XP_001221498.1. XM_001221497.1. |
3D structure databases | |
| ProteinModelPortal | Q2H7G2. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4391213. |
Phylogenomic databases | |
| 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. 3 hits. |
| 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_CHAGB | ||||||||
| Accession | Primary (citable) accession number: Q2H7G2 | ||||||||
| 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