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Q2U038 (KYNU1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:AO090011000602
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length487 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 – 487487Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356969

Regions

Region175 – 1784Pyridoxal phosphate binding By similarity

Sites

Binding site1471Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1481Pyridoxal phosphate By similarity
Binding site2321Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate By similarity
Binding site2861Pyridoxal phosphate By similarity
Binding site3271Pyridoxal phosphate By similarity
Binding site3551Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2871N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2U038 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 8492F301C147F4F7

FASTA48754,916
        10         20         30         40         50         60 
MGSRLHVQEI KKGPPLPFKD DIRAFTREYA ESLDAQDPLR HFRDEFIIPS KKDLKRKTLN 

        70         80         90        100        110        120 
ANENIEDSSD PRSIYLCGNS LGLQPRNTRK YLEHYLRTWA IKGVTGHFTP HDDQLLPPFV 

       130        140        150        160        170        180 
DVDDAGAKLM APIVGALESE VAVMGTLTAN LHFLMASFYQ PTKEKYKIIL EGKAFPSDHY 

       190        200        210        220        230        240 
AVESQIQHHN LDPKDAMVLI ELENLDRPIL DTEKILRVID EHASSTALIL LSGIQFYTGQ 

       250        260        270        280        290        300 
YFDIEKITAY AHSKGIIIGW DCAHAAGNVE LKLHDWNVDF AAWCNYKYLN SGPGGMAGLF 

       310        320        330        340        350        360 
VHENHGRVDM TKVGSKDEPF RPRLSGWWGD DKKTRFRMEN RFVPQPGAAG FQLSNPSVLD 

       370        380        390        400        410        420 
MNAVAASLEI FNRTSMAEIR KKSLDLTGYL EHLLLKYPLD AAPEDKPFSI ITPSNPAERG 

       430        440        450        460        470        480 
AQLSLRLGPG LLDNVLEVLE ENGVVIDERK PDVIRVAPAP LYNTYADVWQ FCQIFFDACQ 


KAVRARK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007171 Genomic DNA. Translation: BAE65077.1.
RefSeqXP_001826210.1. XM_001826158.2.

3D structure databases

ProteinModelPortalQ2U038.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00005235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00005329; CADAORAP00005235; CADAORAG00005329.
GeneID5998313.
KEGGaor:AOR_1_1026054.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAWGGRLIR.
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_ASPOR
AccessionPrimary (citable) accession number: Q2U038
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 53 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