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Reviewed, UniProtKB/Swiss-Prot Q59QC4 (KYNU_CANAL)

Last modified November 3, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: CaO19.394, CaO19.8024
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length461 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
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 – 461461Kynureninase
PRO_0000356973

Regions

Region142 – 1454Pyridoxal phosphate binding By similarity

Sites

Binding site1141Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1151Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2311Pyridoxal phosphate By similarity
Binding site2531Pyridoxal phosphate By similarity
Binding site2881Pyridoxal phosphate By similarity
Binding site3161Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2541N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59QC4-1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: C96FCFF707B7CEDB

FASTA46152,384
        10         20         30         40         50         60 
MSLAEAKKLD KKFPTFKNEF AIPTFGSLGI KNNKYESSTE SIYLCGNSLG LMPKNTKKAI 

        70         80         90        100        110        120 
NDELNAWVER GVESHFNHPD KSLTPWVDID LPLLPLIAPI VGAKENEVAV MGSLTANLNA 

       130        140        150        160        170        180 
LLIHFYKPEG KRTKILFEKQ AFPSDYYAFL NIVKLFGYDE KHLIQLEVQP GETYIKTERI 

       190        200        210        220        230        240 
IKAIDENSDE LALVCFPGIQ YYTGQFFKIE EITKYAKEKS QQIKVGWDLA HAVGNVPLNL 

       250        260        270        280        290        300 
HDWGVDFAAW CSYKYLNSGP GAIGGIFVHE KYTIENKKSS FVPRLAGWWG NNSQERFKML 

       310        320        330        340        350        360 
EEFDPINSAL SYRQSNPSVL DVVAVKSSLE VYAKVGGVSK LREKSVALTQ FLQDLLTNSK 

       370        380        390        400        410        420 
YYIPQSSTSN SKFGFKILTP LNPAERGCQL SIMFQPHFDE KDKNVMERVN AYLHDHAIIC 

       430        440        450        460 
DERRPDVIRL APLPLYNTFE ETFIAVQRLF EALDNISKEY M 

« Hide

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314.

Cross-references

Sequence databases

AACQ01000176 Genomic DNA. Translation: EAK92703.1.
AACQ01000177 Genomic DNA. Translation: EAK92674.1.
RefSeqXP_711882.1.
XP_711911.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3646483.
3646492.
KEGGcal:CaO19.394.
cal:CaO19.8024.

Organism-specific databases

CGDCAL0004950. orf19.394.

Phylogenomic databases

OMANFPTDVY.

Family and domain databases

InterProIPR010111. 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.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_CANAL
AccessionPrimary (citable) accession number: Q59QC4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 26, 2005
Last modified: November 3, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Candida albicans

Candida albicans: entries and gene names

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