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A6RSP5 (KYNU_BOTFB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:BC1G_03468
OrganismBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifier332648 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotryotinia

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
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_0000360867

Regions

Region170 – 1734Pyridoxal phosphate binding By similarity

Sites

Binding site1421Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1431Pyridoxal phosphate By similarity
Binding site2551Pyridoxal phosphate By similarity
Binding site2581Pyridoxal phosphate By similarity
Binding site2801Pyridoxal phosphate By similarity
Binding site3201Pyridoxal phosphate By similarity
Binding site3481Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2811N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6RSP5 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 42BFAB823F77B9F2

FASTA47552,872
        10         20         30         40         50         60 
MGSIAKEEQP STKVEKPTFS SKANTLEFAQ SLDAKDHMRR FRDQYIIPSK ANIKTKKLAK 

        70         80         90        100        110        120 
PGLSDEPSIY FCGNSLGLQP KCVQEYLQAH LDTWSSIAVH GHFRDLEDSP LTQWQLLAEH 

       130        140        150        160        170        180 
AAKQCAPIVG AKASEVAIMG TLTTNLHLLM ASFYTPTPEK SKIIMEWKAF PSDHYAIESQ 

       190        200        210        220        230        240 
IRGHGYNPEE AMVMIAPDEG SYEISTEKIL RTIDEHASTT ALLLLPGIQY YTGQLFDIKT 

       250        260        270        280        290        300 
ITAYAQSKGL TVGWDLAHAA GNVPLQLHDW NVDFAVWCTY KYMNAGPGSI AGAYVHERHG 

       310        320        330        340        350        360 
EVDYSEGEEK PKYRHRLMGW YGGDQSCRFL MNNKFRPSPG ASGYQVSNPS VVDLTSLCAA 

       370        380        390        400        410        420 
LSIFNQTSMA EISQKTLHLT AYLEHLLLST NSSDSPAFRI ITPSDPSARG TQLSVLLKPG 

       430        440        450        460        470 
RLETLSDMLE EAGIVADKRK PDVIRVAPVP LYNTYEDVWN FVQIFNKALE KCEEA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476854 Genomic DNA. Translation: EDN20078.1.
RefSeqXP_001557886.1. XM_001557836.1.

3D structure databases

ProteinModelPortalA6RSP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING332648.A6RSP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5438547.
KEGGbfu:BC1G_03468.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAGWYGGDK.

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_BOTFB
AccessionPrimary (citable) accession number: A6RSP5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 49 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