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Q2UJE8 (KYNU2_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:AO090003001247
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length468 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.

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.

Subcellular location

Cytoplasm By similarity.

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

de novo NAD biosynthetic process from tryptophan

Inferred from electronic annotation. Source: EnsemblFungi

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: 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 – 468468Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356970

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
Q2UJE8 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 1FA4063ABD51773C

FASTA46851,623
        10         20         30         40         50         60 
MSNVKSSKPV FPENAGSNEY AASLDAADPL ASFRDKFIIP SKANINSKKL AKPGLSSDPC 

        70         80         90        100        110        120 
IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VSGHFVDLEG SPLKQWQLLS EQAAASMSKI 

       130        140        150        160        170        180 
VGAQAEEVAA MGTLTANLHL LLASFYKPTP TKHKILLDWK AFPSDHYAIE SHLAWHNLDP 

       190        200        210        220        230        240 
KQSMVLIGPD EGEYEISTEK ILSYIDEHAE SAALILLPGI QYYTGQLFDI QKITAYAQSR 

       250        260        270        280        290        300 
DLTVGWDLAH AYGNVELKLH DWDVDFAAWC TYKYGNAGPG AMGGLFVHER HGRVDYSEGE 

       310        320        330        340        350        360 
DAPKFRHRLT GWYGGDRSVR FKMDNNFKPI PGAGGWQLSN PSAIDLACLC ASLSVFDETS 

       370        380        390        400        410        420 
MAELRKKSVM LTAYLEHLLL KDTTDETRPF RIVTPADPEA RGAQLSVLLK PGLLQNVSQK 

       430        440        450        460 
LQEGGIVCDK REPGVVRVAP TPLYNTFTDV WKFVSYFKAA LDEPELKN

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP007155 Genomic DNA. Translation: BAE58317.1.
RefSeqXP_001820319.1. XM_001820267.2.

3D structure databases

ProteinModelPortalQ2UJE8.
ModBaseSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00001751.

Proteomic databases

PRIDEQ2UJE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00001778; CADAORAP00001751; CADAORAG00001778.
GeneID5992302.
KEGGaor:AOR_1_2198154.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OrthoDBEOG4TB7KQ.

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. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU2_ASPOR
AccessionPrimary (citable) accession number: Q2UJE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 24, 2006
Last modified: May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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