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Q54Q04 (KYNU_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
L-kynurenine hydrolase
Gene names
Name:kynu
ORF Names:DDB_G0284203
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length451 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 – 451451Kynureninase HAMAP-Rule MF_03017
PRO_0000331482

Regions

Region159 – 1624Pyridoxal phosphate binding By similarity

Sites

Binding site1311Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1321Pyridoxal phosphate By similarity
Binding site2151Pyridoxal phosphate By similarity
Binding site2441Pyridoxal phosphate By similarity
Binding site2471Pyridoxal phosphate By similarity
Binding site2691Pyridoxal phosphate By similarity
Binding site3031Pyridoxal phosphate By similarity
Binding site3311Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q54Q04 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 99A0FA2091907172

FASTA45150,799
        10         20         30         40         50         60 
MDKFFEYIKN QNLSLEDEKL ADKLDQLDQL SSIKEEFYFP ITKDIATDLS RVKDEDLDKP 

        70         80         90        100        110        120 
VIYLTGNSLG LQPKEIEKQL VCNYLNDWRK YGVEGHHKGD HPFIHIDEEI QASLSKIVGA 

       130        140        150        160        170        180 
LPSEVCPMNS LSTNIHVLLS NFYKPTQTRH KIIIEYGAFP SDLYVTESQI RHNSFNPETS 

       190        200        210        220        230        240 
LIKIKPRDGE YTLRTDDIIN VLKEHGDSVA VVMLSGIQYF TGQFFDMKKI TEVGHEIGAI 

       250        260        270        280        290        300 
VGWDLAHAAG NVELSLHDWN VDFACWCTYK YLNSGPGCIA GIFVHSKHTE SFNLSTDSRL 

       310        320        330        340        350        360 
LGWFGNKLSN RFQKEKEFVA EDGALGFRMS NPSVADCTAL RASLSVFEKA GGIKKLAEKS 

       370        380        390        400        410        420 
TIITGYLEYL LTHKLKTTDV QIITPSEANQ RGSQLSLLIK GIKASQLKVN LSNSGIVCDV 

       430        440        450 
RDPDVIRVAP APLYTSFNDV KYFIQKLNEN M 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000064 Genomic DNA. Translation: EAL65290.1.

3D structure databases

ProteinModelPortalQ54Q04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0231361.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0231361; DDB0231361; DDB_G0284203.
KEGGddi:DDB_G0284203.

Organism-specific databases

dictyBaseDDB_G0284203. kynu.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAGWYGGDK.
PhylomeDBQ54Q04.
ProtClustDBCLSZ2430281.

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...

Other

PROQ54Q04.

Entry information

Entry nameKYNU_DICDI
AccessionPrimary (citable) accession number: Q54Q04
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase