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A8XKT0 (KYNU_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase

EC=3.7.1.3
Alternative name(s):
Abnormal fluorescence under UV illumination
L-kynurenine hydrolase
Gene names
Name:flu-2
ORF Names:CBG14833
OrganismCaenorhabditis briggsae [Reference proteome]
Taxonomic identifier6238 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_03017

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_03017

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_03017

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_03017

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03017.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkynureninase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Kynureninase HAMAP-Rule MF_03017
PRO_0000356959

Regions

Region182 – 1854Pyridoxal phosphate binding By similarity

Sites

Binding site1541Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1551Pyridoxal phosphate By similarity
Binding site2381Pyridoxal phosphate By similarity
Binding site2671Pyridoxal phosphate By similarity
Binding site2701Pyridoxal phosphate By similarity
Binding site2921Pyridoxal phosphate By similarity
Binding site3221Pyridoxal phosphate By similarity
Binding site3501Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2931N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8XKT0 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: F7BD3B8CB98C956A

FASTA48354,408
        10         20         30         40         50         60 
MAEGQAPAPP QPEGDQECMC TQDKVLQFLN KMADESGIKD LTDPALAEFL TDSDALKGIR 

        70         80         90        100        110        120 
DLFHYPKAGT LPDVDPTLVD PNADSIYLCG NSLGLMPKVT EEVMKEHLDK WAKMGVFGHM 

       130        140        150        160        170        180 
TGEVPWAHSD EHCLEGVGRL VGAKKEEVSI ANSLTVNIHV LLTAFYKPTE TRHKILLESK 

       190        200        210        220        230        240 
AFPSDHYAIE SQIRLKGRTV EESMVCMEPR EGEETLRTED IIDYIENNGD EIAIVFFSGI 

       250        260        270        280        290        300 
QYYTGQLFDI KAITEAGHRK GCLVGWDLAH AFANVPLHLH WWDVDFAAWC SYKYGCTGAG 

       310        320        330        340        350        360 
SIAGLFVHER FLHDKRDRML GWWSHKMSSR FTMDNVLDLD EGAAGYRISN PPIHCVAAML 

       370        380        390        400        410        420 
GSLKIFDQVS LENLRSRSCY LTGYLEYLVK TLFGENSEQR TTKLSILIIT PENFHQRGCQ 

       430        440        450        460        470        480 
LSLKFSSPID VIYPELVKRG VAVDKRYPNV IRVAPVHLYN NYVDVRRFIS VLQEVAHIVE 


DHA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE600983 Genomic DNA. Translation: CAP33254.1.
RefSeqXP_002644815.1. XM_002644769.1.

3D structure databases

ProteinModelPortalA8XKT0.
SMRA8XKT0. Positions 28-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6238.CBG14833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaCBG14833; CBG14833; CBG14833.
GeneID8586811.
KEGGcbr:CBG14833.

Organism-specific databases

CTD8586811.
WormBaseCBG14833; CBP18263; WBGene00035224; Cbr-flu-2.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAWGGRLIR.
OrthoDBEOG7D2FDV.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_CAEBR
AccessionPrimary (citable) accession number: A8XKT0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways