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A7ESB8 (KYNU_SCLS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:SS1G_08223
OrganismSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) [Reference proteome]
Taxonomic identifier665079 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia

Protein attributes

Sequence length475 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

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

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: UniProtKB-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 – 475475Kynureninase HAMAP-Rule MF_03017
PRO_0000360872

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 site3191Pyridoxal phosphate By similarity
Binding site3471Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2801N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ESB8 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: DC42B2E8ED59B7C4

FASTA47552,956
        10         20         30         40         50         60 
MGSIAKEEQP SKVEKPTFSS KANTLEYAQS LDANDHMRRF RDQFIIPSKA NIKATKLEKP 

        70         80         90        100        110        120 
GLSDESSIYF CGNSLGLQPK CVKEYLQAHL DTWSSIGVHG HFRDLEDSPL TQWQLLAEHA 

       130        140        150        160        170        180 
SKQCAPIVGA KASEVAMMGT LTTNLHLLMA SFYTPTPEKN KIIMEWKAFP SDHYAIESQI 

       190        200        210        220        230        240 
RGHGYNPQEA MVMIGPEEGS YEISTEKILR TIDEHASTTA LVLLPGIQYY TGQLFDVKTI 

       250        260        270        280        290        300 
TAYAQSKGLI VGWDLAHAAG NVPLQLHDWN VDFAVWCTYK YMNAGPGSIA GAFIHERHGE 

       310        320        330        340        350        360 
VDYSEGEEKP KYRHRLMGWY GGDQSCRFLM NNKFRPSPGA SGYQVSNPSV VDLTSLCAAL 

       370        380        390        400        410        420 
SIFNQTSMEE ISQKTLHLTA YLEHLLLTSN PSNTNPAFRI ITPSDPSARG TQLSVLLKPG 

       430        440        450        460        470 
RLETLSDMLE EAGIVADKRK PDVIRVAPVP LYNTYEDVWR FVQIFNAALE KCEEA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476631 Genomic DNA. Translation: EDN92360.1.
RefSeqXP_001590483.1. XM_001590433.1.

3D structure databases

ProteinModelPortalA7ESB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING665079.A7ESB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEDN92360; EDN92360; SS1G_08223.
GeneID5486837.
KEGGssl:SS1G_08223.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAGWYGGDK.
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_SCLS1
AccessionPrimary (citable) accession number: A7ESB8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 44 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