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A2R7T0 (KYNU1_ASPNC) 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 1

EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1
L-kynurenine hydrolase 1
Gene names
Name:bna5-1
ORF Names:An16g04630
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length472 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 – 472472Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356967

Regions

Region174 – 1774Pyridoxal phosphate binding By similarity

Sites

Binding site1461Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1471Pyridoxal phosphate By similarity
Binding site2311Pyridoxal phosphate By similarity
Binding site2601Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate By similarity
Binding site2851Pyridoxal phosphate By similarity
Binding site3261Pyridoxal phosphate By similarity
Binding site3541Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2861N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2R7T0 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 36CAC1D632AA5607

FASTA47253,008
        10         20         30         40         50         60 
MSSQLGHESS VSSPLSYKTD SNAFTREYAE SLDAQDPLRD FRKEFIIPSK VDLKRKTLAI 

        70         80         90        100        110        120 
DDSSKDESDP RCIYLCGNSL GVQPRNARKY IDYYLRTWAI KGVTGHFLPH EDQLLPPFVD 

       130        140        150        160        170        180 
VDDAGAKLMA PIVGALESEV AVMGTLTANL HFLMASFYRP TQERYKIILE GKAFPSDHYA 

       190        200        210        220        230        240 
IESQIRHHNL RPEDAMVLIE PEDRLKPILR TEQILRVIDE HASSTALVLL SGIQFYTGQY 

       250        260        270        280        290        300 
FDIEKITAHA QSKGILVGWD CAHAAGNVDL RLHDWNVDFA AWCNYKYLNS GPGGMAALFV 

       310        320        330        340        350        360 
HERHGRVDMD KVGSDEEPFR PRLSGWWGGD KKTRFLMNNN FLPQTGAAGF QLSNPSVLDM 

       370        380        390        400        410        420 
NAVVASLELF NRTSMAEIRQ KSLNATGYLE HLLLNYPADF STGKRPFSII TPSNPAERGA 

       430        440        450        460        470 
QLSLLLEPGL LDSVLETLEE HGVVVDERKP DVIRVAPAPL YNTYTEYPTY RT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270369 Genomic DNA. Translation: CAK42891.1.

3D structure databases

ProteinModelPortalA2R7T0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00012690.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00012932; CADANGAP00012690; CADANGAG00012932.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
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 nameKYNU1_ASPNC
AccessionPrimary (citable) accession number: A2R7T0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 6, 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