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Protein

Kynureninase

Gene

BNA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei112 – 1121Pyridoxal phosphateUniRule annotation
Binding sitei196 – 1961Pyridoxal phosphateUniRule annotation
Binding sitei226 – 2261Pyridoxal phosphateUniRule annotation
Binding sitei229 – 2291Pyridoxal phosphateUniRule annotation
Binding sitei251 – 2511Pyridoxal phosphateUniRule annotation
Binding sitei286 – 2861Pyridoxal phosphateUniRule annotation
Binding sitei314 – 3141Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. kynureninase activity Source: SGD
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: SGD
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8163.
YEAST:YLR231C-MONOMER.
ReactomeiREACT_341524. Tryptophan catabolism.
UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5UniRule annotation
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:BNA5UniRule annotation
Ordered Locus Names:YLR231C
ORF Names:L8083.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR231c.
EuPathDBiFungiDB:YLR231C.
SGDiS000004221. BNA5.

Subcellular locationi

  1. Cytoplasm UniRule annotation1 Publication
  2. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453KynureninasePRO_0000218665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

MaxQBiQ05979.
PaxDbiQ05979.
PeptideAtlasiQ05979.

Expressioni

Gene expression databases

GenevestigatoriQ05979.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-10016,EBI-16219

Protein-protein interaction databases

BioGridi31501. 39 interactions.
DIPiDIP-6518N.
IntActiQ05979. 6 interactions.
MINTiMINT-706654.
STRINGi4932.YLR231C.

Structurei

3D structure databases

ProteinModelPortaliQ05979.
SMRiQ05979. Positions 4-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 1424Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
GeneTreeiENSGT00390000008033.
HOGENOMiHOG000242438.
InParanoidiQ05979.
KOiK01556.
OMAiRFWQPLS.
OrthoDBiEOG7V1G0J.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q05979-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKALELDGE YPESLRDEFN IPTFKSMGLS SDDKPVTYLC GNSLGLMPKS
60 70 80 90 100
TRNSINAELD AWSDCAVESH FKHPEEARGK VPWVSIDLPI LPLLAPIVGA
110 120 130 140 150
QENEVAVMNS LTANLNSLLI TFYKPTEKRF KILFEKGSFP SDYYAFYNQC
160 170 180 190 200
KIHGISEPEN VFIQIEPREG ETYIRTQDIL DTIEVNQDEL ALVCLSGVQY
210 220 230 240 250
YTGQYFDIGR ITSFAHQFPD ILVGWDLAHA VGNVPLQLHD WGVDFACWCS
260 270 280 290 300
YKYLNAGPGG IGGLFVHSKH TKPDPAKESL PRLAGWWGND PAKRFQMLEV
310 320 330 340 350
FEPIPGALGF RQSNPSVIDT VALRSSLELF AKFNGINEVR KRSLLLTNYM
360 370 380 390 400
TELLEASKYY KHPLRIEKLP CFFTILTPTS TDEEHGAQLS LYFDSDTGKE
410 420 430 440 450
DIMPKVFQYL HDHGVIGDAR RPNVIRLAPA PLYNTFSDVY IAVNALNEAM

DKL
Length:453
Mass (Da):51,032
Last modified:November 1, 1996 - v1
Checksum:i95C84CBB4F6FCF9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19027 Genomic DNA. Translation: AAB67417.1.
BK006945 Genomic DNA. Translation: DAA09548.1.
PIRiS51453.
RefSeqiNP_013332.1. NM_001182118.1.

Genome annotation databases

EnsemblFungiiYLR231C; YLR231C; YLR231C.
GeneIDi850933.
KEGGisce:YLR231C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19027 Genomic DNA. Translation: AAB67417.1.
BK006945 Genomic DNA. Translation: DAA09548.1.
PIRiS51453.
RefSeqiNP_013332.1. NM_001182118.1.

3D structure databases

ProteinModelPortaliQ05979.
SMRiQ05979. Positions 4-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31501. 39 interactions.
DIPiDIP-6518N.
IntActiQ05979. 6 interactions.
MINTiMINT-706654.
STRINGi4932.YLR231C.

Proteomic databases

MaxQBiQ05979.
PaxDbiQ05979.
PeptideAtlasiQ05979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR231C; YLR231C; YLR231C.
GeneIDi850933.
KEGGisce:YLR231C.

Organism-specific databases

CYGDiYLR231c.
EuPathDBiFungiDB:YLR231C.
SGDiS000004221. BNA5.

Phylogenomic databases

eggNOGiCOG3844.
GeneTreeiENSGT00390000008033.
HOGENOMiHOG000242438.
InParanoidiQ05979.
KOiK01556.
OMAiRFWQPLS.
OrthoDBiEOG7V1G0J.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
BioCyciMetaCyc:MONOMER-8163.
YEAST:YLR231C-MONOMER.
ReactomeiREACT_341524. Tryptophan catabolism.

Miscellaneous databases

NextBioi967372.
PROiQ05979.

Gene expression databases

GenevestigatoriQ05979.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKYNU_YEAST
AccessioniPrimary (citable) accession number: Q05979
Secondary accession number(s): D6VYN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 29, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3060 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.