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Q59QC4 (KYNU_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:CaO19.394, CaO19.8024
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length461 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 – 461461Kynureninase HAMAP-Rule MF_03017
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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000176 Genomic DNA. Translation: EAK92703.1.
AACQ01000177 Genomic DNA. Translation: EAK92674.1.
RefSeqXP_711882.1. XM_706789.1.
XP_711911.1. XM_706818.1.

3D structure databases

ProteinModelPortalQ59QC4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0004950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CGDCAL0004950. orf19.394.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
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_CANAL
AccessionPrimary (citable) accession number: Q59QC4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 26, 2005
Last modified: February 19, 2014
This is version 57 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

Candida albicans

Candida albicans: entries and gene names