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Q6BI19 (KYNU_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Kynureninase
EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase
Gene names
Name:BNA5
Ordered Locus Names:DEHA2G14080g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces ›

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. 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.

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.

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_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: 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 HAMAP-Rule MF_03017
PRO_0000218662

Regions

Region144 – 1474Pyridoxal phosphate binding By similarity

Sites

Binding site1161Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1171Pyridoxal phosphate By similarity
Binding site1991Pyridoxal 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 [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. XM_462152.1.

3D structure databases

ProteinModelPortalQ6BI19.
ModBaseSearch...

Protein-protein interaction databases

STRING4959.Q6BI19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2905066.
KEGGdha:DEHA2G14080g.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAMLTHVNY.
OrthoDBEOG4TB7KQ.

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. PyrdxlP-dep_Trfase_major. 1 hit.
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: May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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