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Reviewed, UniProtKB/Swiss-Prot A3LQD7 (KYNU_PICST)

Last modified November 3, 2009. Version 19. 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

Names and origin

Protein namesRecommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase
    Biosynthesis of nicotinic acid protein 5
Gene names
Name: BNA5
ORF Names: PICST_55542
OrganismPichia stipitis (Yeast) [Complete proteome]
Taxonomic identifier4924 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaePichia

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Kynureninase
PRO_0000356984

Regions

Region144 – 1474Pyridoxal phosphate binding By similarity

Sites

Binding site1161Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1171Pyridoxal phosphate By similarity
Binding site2311Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2561Pyridoxal phosphate By similarity
Binding site2911Pyridoxal phosphate By similarity
Binding site3191Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2571N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3LQD7-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: AB373BBF56454822

FASTA46552,840
        10         20         30         40         50         60 
MSLEKAQELD TKYPTYKDEF AVPTFKSLGI ETSQFNENTD SIYLCGNSLG LMPKSTKQAI 

        70         80         90        100        110        120 
NDELNAWIER GVESHFNHPG QSEGKTPWVD IDLPLVPLVA PIVGAKENEV AVMGSLTSNL 

       130        140        150        160        170        180 
NALLINFYKP KDKRTKILFE KQAFPSDYYA FLNLVKLHGY DESHLVQLKV LPGNTYLTTE 

       190        200        210        220        230        240 
QIKKAVDDNI DELAMVCFPG IQYYTGQFFK IEEITNYVKN KGKNEIVVGW DLAHAVGNVP 

       250        260        270        280        290        300 
LKLHDWNVDF AAWCSYKYLN SGPGGIAGIY VHEQYTKDNS KTSFSPRLAG WWGNNASDRF 

       310        320        330        340        350        360 
KMLEEFDPIN SALSYRQSNP SVIDVVAVKS SLELFKKVGG VPKLRKKSIA LTQFLQDLLV 

       370        380        390        400        410        420 
SSKYYFRSDN DTDRSKIGFT ILTPLNQEER GAQLSVLFQP HYDDKQKNIM ERVSGYLHNH 

       430        440        450        460 
AIICDERRPD VIRFAPLPLY NTFEETYYAA QRLFEALDKI SSEEI 

« Hide

References

[1]"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.
Nat. Biotechnol. 25:319-326(2007) [PubMed: 17334359] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545.

Cross-references

Sequence databases

CP000496 Genomic DNA. Translation: ABN65189.1.
RefSeqXP_001383218.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA3LQD7.

Genome annotation databases

GeneID4836702.
GenomeReviewsGene locus BNA5 in contig CP000496_GR.
KEGGpic:PICST_55542.

Phylogenomic databases

OMAWQPLSGW.

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...

Entry information

Entry nameKYNU_PICST
AccessionPrimary (citable) accession number: A3LQD7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 3, 2007
Last modified: November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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