Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0UIN2 (KYNU1_PHANO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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 1

EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1
L-kynurenine hydrolase 1
Gene names
Name:BNA5-1
ORF Names:SNOG_08382
OrganismPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum) [Reference proteome]
Taxonomic identifier321614 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaeParastagonospora

Protein attributes

Sequence length506 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 506506Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356982

Regions

Region169 – 1724Pyridoxal phosphate binding By similarity

Sites

Binding site1411Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1421Pyridoxal phosphate By similarity
Binding site2541Pyridoxal phosphate By similarity
Binding site2571Pyridoxal phosphate By similarity
Binding site2791Pyridoxal phosphate By similarity
Binding site3341Pyridoxal phosphate By similarity
Binding site3621Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2801N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0UIN2 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 065722108D062DF3

FASTA50655,984
        10         20         30         40         50         60 
MSQTTNSYDS FQDADLCSAA FAEKQDEKDK LTKLREDFYI PTKGDLINKK YGFQKSGNNA 

        70         80         90        100        110        120 
KGHENGKCIY FCGNSLGLQP TRTKEYINRY LDTWASKGVF GHFTDYEGGL PPWLHIDDAV 

       130        140        150        160        170        180 
KEQTSKIVGA LPSEVVIMET LTANLHLLMS SFYRPTKDRW KIIIEGKAFP SDHYAALSQI 

       190        200        210        220        230        240 
AHHDLDPSAL ITIEPPSSSA PYLSNEHILS VISKHAATTA LVLLPGIQFY SGQFFDIELI 

       250        260        270        280        290        300 
TRHCRALGIT VGWDLAHAVG NVPLKLHDWN VDFAAWCNYK YMSGGPGVIG GAFVHERHGT 

       310        320        330        340        350        360 
VGETAPTTTP DGTNGNPKTI SDESLTYRPR LSGWWGNDKS SRFTMDNKFV PIPGASGYQL 

       370        380        390        400        410        420 
SNPSALDMTS VMASLDVFAL TTMDALRERS IRLTGYLEAR LLRYPGGEPP YTIITPTNPA 

       430        440        450        460        470        480 
ERGAQLSVML RPGMLDSVLH HLEKEGVVVD ERKPDVLRIA PAPLYNTFRD VHDFIGIFHE 

       490        500 
ACRKALVKPA EAPKHSEGVP KAIQTT 

« Hide

References

[1]"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH445336 Genomic DNA. Translation: EAT84658.1.
RefSeqXP_001798697.1. XM_001798645.1.

3D structure databases

ProteinModelPortalQ0UIN2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSNOT_08382; SNOT_08382; SNOG_08382.
GeneID5975595.
KEGGpno:SNOG_08382.

Phylogenomic databases

KOK01556.
OMAGLMNDIV.
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 nameKYNU1_PHANO
AccessionPrimary (citable) accession number: Q0UIN2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: September 5, 2006
Last modified: June 11, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways