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Protein

Kynureninase

Gene

BNA5

Organism
Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 annotation

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

Pathway: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
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.

Pathway: NAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei94 – 941Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei95 – 951Pyridoxal phosphateUniRule annotation
Binding sitei208 – 2081Pyridoxal phosphateUniRule annotation
Binding sitei211 – 2111Pyridoxal phosphateUniRule annotation
Binding sitei233 – 2331Pyridoxal phosphateUniRule annotation
Binding sitei275 – 2751Pyridoxal phosphateUniRule annotation
Binding sitei303 – 3031Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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
ORF Names:Kpol_1029p21
OrganismiVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus)
Taxonomic identifieri436907 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeVanderwaltozyma
ProteomesiUP000000267 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455KynureninasePRO_0000360873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei234 – 2341N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi436907.XP_001643105.1.

Structurei

3D structure databases

ProteinModelPortaliA7TR79.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1254Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
InParanoidiA7TR79.
KOiK01556.
OrthoDBiEOG7V1G0J.
PhylomeDBiA7TR79.

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.

A7TR79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIPVNSENV NDETEGDVAG KEVYYLCGNS LGLMPKDTKE TVTRELDAWR
60 70 80 90 100
DRAVESHFKH PTDTSWVDID LPVVPLLAPI VGGKNEEVAV MNTLTANLNS
110 120 130 140 150
LLVSFYRPTK KRFKIVFEKK AFPSDYYAFY NQCRLHNFDP NECILQISAR
160 170 180 190 200
PNETFLRTED ILKVIEENNE SIALVCLPGI QYYSGQLFEI ERITKFAHQY
210 220 230 240 250
PEIIVGWDLA HAVGNVPLKL HDWGVDFACW CSYKYLNSGP GSIGGLFIHE
260 270 280 290 300
KWHHSALKFG DDVNHDEYRP RLAGWWGNNN EKRFQMLEKF EPIKGALGFR
310 320 330 340 350
QSNPSVLDVV CLQSSLKIFQ KYGGVENLRL KSLKLTKYLI NQLQKSPYYH
360 370 380 390 400
PKKQSSKEEL GFRIITPIQN ESQYGAQISI QLTPSRLTGK NKDTMEIVFE
410 420 430 440 450
YMHRHGVVVD ERKPNVIRIS PVPLYNTFQD VFTTVAILNS ALDSVKKSIK

ALKSN
Length:455
Mass (Da):51,982
Last modified:October 2, 2007 - v1
Checksum:i066B64E94CDA5EFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS480471 Genomic DNA. Translation: EDO15247.1.
RefSeqiXP_001643105.1. XM_001643055.1.

Genome annotation databases

GeneIDi5543316.
KEGGivpo:Kpol_1029p21.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS480471 Genomic DNA. Translation: EDO15247.1.
RefSeqiXP_001643105.1. XM_001643055.1.

3D structure databases

ProteinModelPortaliA7TR79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi436907.XP_001643105.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5543316.
KEGGivpo:Kpol_1029p21.

Phylogenomic databases

eggNOGiCOG3844.
InParanoidiA7TR79.
KOiK01556.
OrthoDBiEOG7V1G0J.
PhylomeDBiA7TR79.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

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

  1. "Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
    Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
    Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 22028 / DSM 70294.

Entry informationi

Entry nameiKYNU_VANPO
AccessioniPrimary (citable) accession number: A7TR79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 2, 2007
Last modified: June 24, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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.