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Reviewed, UniProtKB/Swiss-Prot B0Y6H2 (KYNU2_ASPFC)

Last modified September 22, 2009. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Kynureninase 2
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase 2
    Biosynthesis of nicotinic acid protein 5-2
Gene names
Name: bna5-2
ORF Names: AFUB_066950
OrganismAspergillus fumigatus (strain CEA10 / CBS 144.89 / FGSC A1163) (Sartorya fumigata) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the kynureninase family.

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Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Kynureninase 2
PRO_0000356964

Regions

Region163 – 1664Pyridoxal phosphate binding By similarity

Sites

Binding site1351Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1361Pyridoxal phosphate By similarity
Binding site2481Pyridoxal phosphate By similarity
Binding site2511Pyridoxal phosphate By similarity
Binding site2731Pyridoxal phosphate By similarity
Binding site3131Pyridoxal phosphate By similarity
Binding site3411Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
B0Y6H2-1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 4143524AE1667152

FASTA46451,198
        10         20         30         40         50         60 
MSTNGTLSKP EFPANAASKE YAASLDAADP FAGFREKFII PSKANIASTK LAKPGLSSEP 

        70         80         90        100        110        120 
CIYFCGNSLG IQPKATQKYL EAQLDTWSSI GVCGHFTKIE DSPLKEWQNL AEQAAESMSK 

       130        140        150        160        170        180 
IVGAAPEEVA AMGTLTMNLH LLLASFFKPT ATKRKILMDW KAFPSDHYAI ESHLAWHHLD 

       190        200        210        220        230        240 
PKETMVLIGP DEGTYEIPTE KILSYIDQHA DEAALILLPG IQYYTGQLFD IPKITEYAHS 

       250        260        270        280        290        300 
RGLIVGWDLA HAYANVPLKL HDWDVDFAAW CTYKYGNAGP GAMAGLFVHE KHGQVDYSEG 

       310        320        330        340        350        360 
EDAPKFRHRL TGWYGGDKSV RFKMDNKFKP IPGAGGYQIS NPSAIDLACL CAALSVFDET 

       370        380        390        400        410        420 
SIAELRKKSV LMTAYLEYLL LKDTTDESRQ FQIITPSDPA ARGAQLSLLL KPGLLHKVAH 

       430        440        450        460 
RLQEAGIICD KREPGVVRVA PVPLYNTFTE IWMFVQQLKA ALEG

« Hide

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Cross-references

Sequence databases

DS499598 Genomic DNA. Translation: EDP50357.1.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameKYNU2_ASPFC
AccessionPrimary (citable) accession number: B0Y6H2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 8, 2008
Last modified: September 22, 2009
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents