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Q0CZX6 (KYNU2_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:ATEG_00758
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

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.

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 – 463463Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356972

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
Q0CZX6 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 402C2BC2BD9A167A

FASTA46351,310
        10         20         30         40         50         60 
MSENNCSKPS FPDNAASKEY AASLDAADPL ASFRDQFIIP SKANIACKRL AKPNLSPEPC 

        70         80         90        100        110        120 
IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VCGHFTNLED SPMKSWQLLA EQAAESMSKI 

       130        140        150        160        170        180 
VGADPAEVAA MGTLTANLHL LMASFYKPTA TKHKILMDWK AFPSDHYAIE SHIAWHNLDP 

       190        200        210        220        230        240 
KESMVLIGPD EGEYEISTDK ILSYIDQHAE DAALLLLPGI QYYTGQLFDI PKITEYAKSR 

       250        260        270        280        290        300 
NLVVGWDLAH AYGNVELKLH DWNVDFAAWC TYKYGNAGPG AMAGLFVHDK HGQVDYSQGE 

       310        320        330        340        350        360 
DSPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLSCLC AALSVFDQTS 

       370        380        390        400        410        420 
VSELRRKSLK LTAYLEYLLL KDTTEDSRPF RIITPTNPEA RGAQLSLLLK PGLLQGVSER 

       430        440        450        460 
LQDAGIICDK REPGVVRVAP VPLYNTYSEV WEFVQQFRAA LQL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH476594 Genomic DNA. Translation: EAU39404.1.
RefSeqXP_001210844.1. XM_001210844.1.

3D structure databases

ProteinModelPortalQ0CZX6.
ModBaseSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00007194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00007194; CADATEAP00007194; CADATEAG00007194.
GeneID4355513.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
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_ASPTN
AccessionPrimary (citable) accession number: Q0CZX6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 17, 2006
Last modified: April 3, 2013
This is version 37 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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