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A2QJI5 (KYNU2_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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 2

EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2
L-kynurenine hydrolase 2
Gene names
Name:bna5-2
ORF Names:An04g07200
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length463 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 – 463463Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356968

Regions

Region162 – 1654Pyridoxal phosphate binding By similarity

Sites

Binding site1341Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1351Pyridoxal phosphate By similarity
Binding site2471Pyridoxal phosphate By similarity
Binding site2501Pyridoxal phosphate By similarity
Binding site2721Pyridoxal phosphate By similarity
Binding site3121Pyridoxal phosphate By similarity
Binding site3401Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2QJI5 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 69BFF4F248B8AB07

FASTA46351,300
        10         20         30         40         50         60 
MSKSNGVSLA FPAEAATKEY AASLDSSDRL AAFREKFIVP SKANIASKKL AKPGLSPESC 

        70         80         90        100        110        120 
IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VGGHFTDLEG SPLKQWQLLS EQAADSMSKI 

       130        140        150        160        170        180 
VGAKPEEVAA MGTLTTNLHL LLASFYKPTQ TKHKILMDWK AFPSDHYAIE SHIAWHDLDP 

       190        200        210        220        230        240 
KESMVLIGPD EGEYEISTQK IFSYIDKHAD EAAMILLPGI QYYTGQLFDI QKITKYAHSR 

       250        260        270        280        290        300 
NMVVGWDLAH AFANVELKLH DWNVDFAAWC TYKYGNAGPG AMGGLFVHEQ HGEVDYSAGE 

       310        320        330        340        350        360 
DAPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLACLC AALSVFDETS 

       370        380        390        400        410        420 
MADLRRKSLK LTAYLEFLLL RDYEEESRPF SIITPKDPEA RGAQLSLLLK PGLLQNVAQK 

       430        440        450        460 
LQEAGIVCDK REPGVVRVAP VPLYNSFSEV WTFVKIFKDA LQQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270081 Genomic DNA. Translation: CAK44720.1.
RefSeqXP_001402081.1. XM_001402044.2.

3D structure databases

ProteinModelPortalA2QJI5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00004336.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00004431; CADANGAP00004336; CADANGAG00004431.
GeneID4991124.
KEGGang:ANI_1_1148184.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
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 nameKYNU2_ASPNC
AccessionPrimary (citable) accession number: A2QJI5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 6, 2007
Last modified: June 11, 2014
This is version 50 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