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Reviewed, UniProtKB/Swiss-Prot Q6BI19 (KYNU_DEBHA)

Last modified February 9, 2010. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase
    Biosynthesis of nicotinic acid protein 5
Gene names
Name: BNA5
Ordered Locus Names: DEHA2G14080g
OrganismDebaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier4959 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeDebaryomyces

Protein attributes

Sequence length460 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.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

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 processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

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: 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 – 460460Kynureninase
PRO_0000218662

Regions

Region144 – 1474Pyridoxal phosphate binding By similarity

Sites

Binding site1161Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1171Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2311Pyridoxal phosphate By similarity
Binding site2531Pyridoxal phosphate By similarity
Binding site2881Pyridoxal phosphate By similarity
Binding site3161Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2541N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6BI19-1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 56DB4A0D03FBFF9C

FASTA46052,093
        10         20         30         40         50         60 
MSIEQAKKLD ECFPTYKEEF EIPTFKSLGI QNDEYEDSTD SIYLCGNSLG LMPKITRTAI 

        70         80         90        100        110        120 
NDELNAWSER GVESHFRHPG EEKGLTSWVD IDLPLLPLIA PIVGGKENEV AVMGTLTSNL 

       130        140        150        160        170        180 
NAMLMSFYKP SGKKTKILFE KQAFPSDYYA FLNAAKIFGY NEDHLIQIEI KEGKTYIETE 

       190        200        210        220        230        240 
DIIETITNHQ DELALVCFSG IQYYTGQFFN IGEITECAKS FGITVGWDLA HAVGNVPLQL 

       250        260        270        280        290        300 
HDWDVDFAVW CSYKYLNSGP GGIAGIFVHE KHTKDNSIEQ FKPRLAGWWG NNASDRFKML 

       310        320        330        340        350        360 
EVFDPIKSAL SYRQSNPSVI DVVAVKSSLE LFKKVGGISE LRKKSVELTG FLQALLTSSK 

       370        380        390        400        410        420 
YYIKQEETTD RLGFKILSPL NKGDRGCQLS VLFQPHYEEY SKNIMERVNK YLSDHAIVCD 

       430        440        450        460 
ERRPDVIRLA PLPLYNTFSE TFIAVQRLIE AMDKIAANEI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382139 Genomic DNA. Translation: CAG90638.1.
RefSeqXP_462152.1.

3D structure databases

SMRQ6BI19. Positions 5-453.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6BI19.

Genome annotation databases

GeneID2905066.
GenomeReviewsGene locus DEHA2G14080g in contig CR382139_GR.
KEGGdha:DEHA0G14949g.

Phylogenomic databases

eggNOGfuNOG06509.
HOGENOMHBG523016.
OMAKPRLAGW.
OrthoDBEOG9RZ0G9.
PhylomeDBQ6BI19.

Enzyme and pathway databases

BRENDA3.7.1.3. 74267.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_DEBHA
AccessionPrimary (citable) accession number: Q6BI19
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: August 16, 2004
Last modified: February 9, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents