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Reviewed, UniProtKB/Swiss-Prot Q05979 (KYNU_YEAST)

Last modified February 9, 2010. Version 80. 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

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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
Ordered Locus Names: YLR231C
ORF Names: L8083.14
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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. Ref.2

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. Ref.2

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. Ref.2

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm. Nucleus Ref.3.

Miscellaneous

Present with 3060 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the kynureninase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Kynureninase
PRO_0000218665

Regions

Region139 – 1424Pyridoxal phosphate binding By similarity

Sites

Binding site1111Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1121Pyridoxal phosphate By similarity
Binding site2261Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2511Pyridoxal phosphate By similarity
Binding site2861Pyridoxal phosphate By similarity
Binding site3141Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2521N6-(pyridoxal phosphate)lysine By similarity

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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

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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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U19027 Genomic DNA. Translation: AAB67417.1.
PIRS51453.
RefSeqNP_013332.1.

3D structure databases

SMRQ05979. Positions 3-451.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6518N.
IntActQ05979. 7 interactions.
STRINGQ05979.

Proteomic databases

PeptideAtlasQ05979.

Genome annotation databases

EnsemblYLR231C; YLR231C; YLR231C; Saccharomyces cerevisiae. [Genome view]
GeneID850933.
KEGGsce:YLR231C.
NMPDRfig|4932.3.peg.4345.

Organism-specific databases

CYGDYLR231c.
SGDS000004221. BNA5.

Phylogenomic databases

eggNOGfuNOG06509.
HOGENOMHBG523016.
OMAFAVGCTY.
OrthoDBEOG9RZ0G9.
PhylomeDBQ05979.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-8163.
BRENDA3.7.1.3. 250.

Gene expression databases

ArrayExpressQ05979.
GenevestigatorQ05979.
GermOnlineYLR231C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Other Resources

NextBio967372.

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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: February 9, 2010
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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