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A3LQD7 (KYNU_PICST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 51. 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

EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase
Gene names
Name:BNA5
ORF Names:PICST_55542
OrganismScheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) [Complete proteome]
Taxonomic identifier322104 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeScheffersomyces

Protein attributes

Sequence length465 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Kynureninase HAMAP-Rule MF_03017
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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000496 Genomic DNA. Translation: ABN65189.1.
RefSeqXP_001383218.1. XM_001383181.1.

3D structure databases

ProteinModelPortalA3LQD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4924.PICST_55542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4836702.
KEGGpic:PICST_55542.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAVWDLAHS.
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 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: June 11, 2014
This is version 51 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