Q1DDU5 (KYNU_MYXXD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 42.
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 EC=3.7.1.3 Alternative name(s): L-kynurenine hydrolase | ||||
| Gene names |
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| Organism | Myxococcus xanthus (strain DK 1622) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 246197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Myxococcus |
Protein attributes
| Sequence length | 426 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. |
| Sequence similarities | Belongs to the kynureninase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridine nucleotide biosynthesis |
| 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: InterPro |
| 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 – 426 | 426 | Kynureninase | PRO_0000357009 | |||||
Regions | |||||||||
| Region | 138 – 141 | 4 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 110 | 1 | Pyridoxal phosphate; via amide nitrogen By similarity | ||||||
| Binding site | 111 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 223 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 226 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 248 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 279 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 307 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 249 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Evolution of sensory complexity recorded in a myxobacterial genome." Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A. Kaplan H.B.Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006) [PubMed: 17015832] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DK 1622. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000113 Genomic DNA. Translation: ABF87345.1. |
| RefSeq | YP_629178.1. NC_008095.1. |
3D structure databases | |
| ProteinModelPortal | Q1DDU5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1DDU5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4104929. |
| GenomeReviews | Gene locus MXAN_0917 in contig CP000113_GR. |
| KEGG | mxa:MXAN_0917. |
| PATRIC | 22644409. VBIMyxXan43560_0907. |
| TIGR | MXAN_0917. |
Phylogenomic databases | |
| eggNOG | COG3844. |
| HOGENOM | HBG523016. |
| OMA | TAEAHKR. |
| PhylomeDB | Q1DDU5. |
| ProtClustDB | CLSK2486953. |
Enzyme and pathway databases | |
| BioCyc | MXAN246197:MXAN_0917-MONOMER. |
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 | KYNU_MYXXD | ||||||||
| Accession | Primary (citable) accession number: Q1DDU5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with