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Protein

Kynureninase

Gene

BNA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

Present with 3060 molecules/cell in log phase SD medium.1 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: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase (BNA5)
This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (BNA4)
  2. Kynureninase (BNA5)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (BNA1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei111Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei112Pyridoxal phosphateUniRule annotation1
Binding sitei196Pyridoxal phosphateUniRule annotation1
Binding sitei226Pyridoxal phosphateUniRule annotation1
Binding sitei229Pyridoxal phosphateUniRule annotation1
Binding sitei251Pyridoxal phosphateUniRule annotation1
Binding sitei286Pyridoxal phosphateUniRule annotation1
Binding sitei314Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

  • kynureninase activity Source: SGD
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processPyridine nucleotide biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:YLR231C-MONOMER
YEAST:YLR231C-MONOMER
ReactomeiR-SCE-71240 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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR231C
SGDiS000004221 BNA5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002186651 – 453KynureninaseAdd BLAST453

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei252N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

MaxQBiQ05979
PaxDbiQ05979
PRIDEiQ05979

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Binary interactionsi

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

Protein-protein interaction databases

BioGridi31501, 56 interactors
DIPiDIP-6518N
IntActiQ05979, 16 interactors
MINTiQ05979
STRINGi4932.YLR231C

Structurei

3D structure databases

ProteinModelPortaliQ05979
SMRiQ05979
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni139 – 142Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000008033
HOGENOMiHOG000242438
InParanoidiQ05979
KOiK01556
OMAiVCSLHAS
OrthoDBiEOG092C20ON

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_01970 Kynureninase, 1 hit
InterProiView protein in InterPro
IPR000192 Aminotrans_V_dom
IPR010111 Kynureninase
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR14084 PTHR14084, 1 hit
PfamiView protein in Pfam
PF00266 Aminotran_5, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiKYNU_YEAST
AccessioniPrimary (citable) accession number: Q05979
Secondary accession number(s): D6VYN2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health