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Reviewed, UniProtKB/Swiss-Prot Q05979 (KYNU_YEAST)

Last modified November 25, 2008. Version 66. 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 · Binary interactions · 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
Gene names
Name: BNA5
Ordered Locus Names: YLR231C
ORF Names: L8083.14
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic (AA) and 3-hydroxyanthranilic acids (3-OHAA), respectively.

Catalytic activity

L-kynurenine + H(2)O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H(2)O = 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; pyridine-2,3-dicarboxylate from L-kynurenine: step 2/3.

Subcellular location

Cytoplasm. Nucleus.

Miscellaneous

Present with 3060 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the kynureninase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Kynureninase
PRO_0000218665

Sites

Binding site2521Pyridoxal phosphate (covalent) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05979-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 95C84CBB4F6FCF9B

FASTA45351,032
        10         20         30         40         50         60 
MEKALELDGE YPESLRDEFN IPTFKSMGLS SDDKPVTYLC GNSLGLMPKS TRNSINAELD 

        70         80         90        100        110        120 
AWSDCAVESH FKHPEEARGK VPWVSIDLPI LPLLAPIVGA QENEVAVMNS LTANLNSLLI 

       130        140        150        160        170        180 
TFYKPTEKRF KILFEKGSFP SDYYAFYNQC KIHGISEPEN VFIQIEPREG ETYIRTQDIL 

       190        200        210        220        230        240 
DTIEVNQDEL ALVCLSGVQY YTGQYFDIGR ITSFAHQFPD ILVGWDLAHA VGNVPLQLHD 

       250        260        270        280        290        300 
WGVDFACWCS YKYLNAGPGG IGGLFVHSKH TKPDPAKESL PRLAGWWGND PAKRFQMLEV 

       310        320        330        340        350        360 
FEPIPGALGF RQSNPSVIDT VALRSSLELF AKFNGINEVR KRSLLLTNYM TELLEASKYY 

       370        380        390        400        410        420 
KHPLRIEKLP CFFTILTPTS TDEEHGAQLS LYFDSDTGKE DIMPKVFQYL HDHGVIGDAR 

       430        440        450 
RPNVIRLAPA PLYNTFSDVY IAVNALNEAM DKL 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae."
Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M., Rytka J., Herbert C.J.
FEBS Lett. 517:97-102(2002) [PubMed: 12062417] [Abstract]
Cited for: FUNCTION, PATHWAY.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

U19027 Genomic DNA. Translation: AAB67417.1.
PIRS51453.
RefSeqNP_013332.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6518N.
IntActQ05979.

Proteomic databases

PeptideAtlasQ05979.

Genome annotation databases

EnsemblYLR231C. Saccharomyces cerevisiae. [Contig view]
GeneID850933.
GenomeReviewsGene locus YLR231C in contig Y13138_GR.
KEGGsce:YLR231C.
NMPDRfig|4932.3.peg.4345.

Organism-specific databases

CYGDYLR231c.
SGDS000004221. BNA5.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMQ05979.

Enzyme and pathway databases

BioCycMetaCyc:MON-8163.

Gene expression databases

GermOnlineYLR231C. Saccharomyces cerevisiae.

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...

Other Resources

LinkHubQ05979.
NextBio967372.

Entry information

Entry nameKYNU_YEAST
AccessionPrimary (citable) accession number: Q05979
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents