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A5DTF4 (KYNU_LODEL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase
Gene names
Name:BNA5
ORF Names:LELG_00640
OrganismLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]
Taxonomic identifier379508 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeLodderomyces

Protein attributes

Sequence length461 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
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 – 461461Kynureninase HAMAP-Rule MF_03017
PRO_0000360869

Regions

Region142 – 1454Pyridoxal phosphate binding By similarity

Sites

Binding site1141Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1151Pyridoxal 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
A5DTF4 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: EB63A54FFB82D793

FASTA46152,331
        10         20         30         40         50         60 
MSSDKAKAFD AQFPTYKSEF QIPTFESLGI QNSKYSPETN SIYLCGNSLG LMPRNTTELI 

        70         80         90        100        110        120 
NRELQAWSSR GVEAHFNHSH PQGTDWVDID LPLLPLLAPL VGAKQNEVAV MGSLTSNLNA 

       130        140        150        160        170        180 
LLIHFYKPKG KRTKILFEKQ AFPSDYYAFL NIVQVFGYDA SHLIQIEIPK GETYIKTETI 

       190        200        210        220        230        240 
LDVFDKYEDE IAIVCLPGIQ YYTGQFFDIA KITKHVKTSA PDVVVGWDLA HAVGNVPLSL 

       250        260        270        280        290        300 
HDWGVDFAAW CSYKYLNAGP GAIAGIFVNE KYTEQNKPEN YKPRLAGWWG NNSSQRFQML 

       310        320        330        340        350        360 
EKFDPIASAL SYRQLNPSVL DCVALKSSLE IFNKVGGMLS LRDKSLAMTQ FLQDILTKSN 

       370        380        390        400        410        420 
YYIEQGETDV NKFGFKIITP LDPNQRGCQL SLLFQPHRDE KKQNVMERVF EYLHQHAIIC 

       430        440        450        460 
DERRPDVIRL APLPLYNTFE ETRIGATRLL EALEAIKDDY I 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH981524 Genomic DNA. Translation: EDK42462.1.
RefSeqXP_001528120.1. XM_001528070.1.

3D structure databases

ProteinModelPortalA5DTF4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36914.A5DTF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5235575.
KEGGlel:LELG_00640.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG7V1G0J.

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_LODEL
AccessionPrimary (citable) accession number: A5DTF4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways