Q8PM33 (KYNU_XANAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
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 |
| ||||
| Organism | Xanthomonas axonopodis pv. citri (Citrus canker) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 92829 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas |
Protein attributes
| Sequence length | 423 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 – 423 | 423 | Kynureninase | PRO_0000357014 | |||||
Regions | |||||||||
| Region | 133 – 136 | 4 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 105 | 1 | Pyridoxal phosphate; via amide nitrogen By similarity | ||||||
| Binding site | 106 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 218 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 221 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 243 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 273 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 301 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 244 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. Kitajima J.P.Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008923 Genomic DNA. Translation: AAM36469.1. |
| RefSeq | NP_641933.1. NC_003919.1. |
3D structure databases | |
| ProteinModelPortal | Q8PM33. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1155672. |
| GenomeReviews | Gene locus XAC1601 in contig AE008923_GR. |
| KEGG | xac:XAC1601. |
| NMPDR | fig|190486.1.peg.1577. |
| PATRIC | 24055203. VBIXanAxo33670_1680. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG523016. |
| OMA | TAEAHKR. |
| ProtClustDB | CLSK903751. |
Enzyme and pathway databases | |
| BioCyc | XAXO190486:XAC1601-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_XANAC | ||||||||
| Accession | Primary (citable) accession number: Q8PM33 | ||||||||
| 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