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A7TR79 (KYNU_VANPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. 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:Kpol_1029p21
OrganismVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]
Taxonomic identifier436907 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeVanderwaltozyma

Protein attributes

Sequence length455 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Kynureninase HAMAP-Rule MF_03017
PRO_0000360873

Regions

Region122 – 1254Pyridoxal phosphate binding By similarity

Sites

Binding site941Pyridoxal phosphate; via amide nitrogen By similarity
Binding site951Pyridoxal phosphate By similarity
Binding site2081Pyridoxal phosphate By similarity
Binding site2111Pyridoxal phosphate By similarity
Binding site2331Pyridoxal phosphate By similarity
Binding site2751Pyridoxal phosphate By similarity
Binding site3031Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2341N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7TR79 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 066B64E94CDA5EFE

FASTA45551,982
        10         20         30         40         50         60 
MGIPVNSENV NDETEGDVAG KEVYYLCGNS LGLMPKDTKE TVTRELDAWR DRAVESHFKH 

        70         80         90        100        110        120 
PTDTSWVDID LPVVPLLAPI VGGKNEEVAV MNTLTANLNS LLVSFYRPTK KRFKIVFEKK 

       130        140        150        160        170        180 
AFPSDYYAFY NQCRLHNFDP NECILQISAR PNETFLRTED ILKVIEENNE SIALVCLPGI 

       190        200        210        220        230        240 
QYYSGQLFEI ERITKFAHQY PEIIVGWDLA HAVGNVPLKL HDWGVDFACW CSYKYLNSGP 

       250        260        270        280        290        300 
GSIGGLFIHE KWHHSALKFG DDVNHDEYRP RLAGWWGNNN EKRFQMLEKF EPIKGALGFR 

       310        320        330        340        350        360 
QSNPSVLDVV CLQSSLKIFQ KYGGVENLRL KSLKLTKYLI NQLQKSPYYH PKKQSSKEEL 

       370        380        390        400        410        420 
GFRIITPIQN ESQYGAQISI QLTPSRLTGK NKDTMEIVFE YMHRHGVVVD ERKPNVIRIS 

       430        440        450 
PVPLYNTFQD VFTTVAILNS ALDSVKKSIK ALKSN 

« Hide

References

[1]"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 22028 / DSM 70294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS480471 Genomic DNA. Translation: EDO15247.1.
RefSeqXP_001643105.1. XM_001643055.1.

3D structure databases

ProteinModelPortalA7TR79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436907.A7TR79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5543316.
KEGGvpo:Kpol_1029p21.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
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_VANPO
AccessionPrimary (citable) accession number: A7TR79
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 2, 2007
Last modified: June 11, 2014
This is version 42 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