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Protein

Kynureninase

Gene

BNA5

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
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

Pathwayi: 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.

Pathwayi: 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)DescriptionActionsGraphical viewLength
Binding sitei116Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei117Pyridoxal phosphateUniRule annotation1
Binding sitei199Pyridoxal phosphateUniRule annotation1
Binding sitei228Pyridoxal phosphateUniRule annotation1
Binding sitei231Pyridoxal phosphateUniRule annotation1
Binding sitei253Pyridoxal phosphateUniRule annotation1
Binding sitei288Pyridoxal phosphateUniRule annotation1
Binding sitei316Pyridoxal phosphateUniRule annotation1

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
Ordered Locus Names:DEHA2G14080g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
Proteomesi
  • UP000000599 Componenti: Chromosome G

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002186621 – 460KynureninaseAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei254N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6BI19.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 147Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242438.
InParanoidiQ6BI19.
KOiK01556.
OMAiVWDLAHS.
OrthoDBiEOG092C20ON.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase. 1 hit.
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.

Q6BI19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIEQAKKLD ECFPTYKEEF EIPTFKSLGI QNDEYEDSTD SIYLCGNSLG
60 70 80 90 100
LMPKITRTAI NDELNAWSER GVESHFRHPG EEKGLTSWVD IDLPLLPLIA
110 120 130 140 150
PIVGGKENEV AVMGTLTSNL NAMLMSFYKP SGKKTKILFE KQAFPSDYYA
160 170 180 190 200
FLNAAKIFGY NEDHLIQIEI KEGKTYIETE DIIETITNHQ DELALVCFSG
210 220 230 240 250
IQYYTGQFFN IGEITECAKS FGITVGWDLA HAVGNVPLQL HDWDVDFAVW
260 270 280 290 300
CSYKYLNSGP GGIAGIFVHE KHTKDNSIEQ FKPRLAGWWG NNASDRFKML
310 320 330 340 350
EVFDPIKSAL SYRQSNPSVI DVVAVKSSLE LFKKVGGISE LRKKSVELTG
360 370 380 390 400
FLQALLTSSK YYIKQEETTD RLGFKILSPL NKGDRGCQLS VLFQPHYEEY
410 420 430 440 450
SKNIMERVNK YLSDHAIVCD ERRPDVIRLA PLPLYNTFSE TFIAVQRLIE
460
AMDKIAANEI
Length:460
Mass (Da):52,093
Last modified:August 16, 2004 - v1
Checksum:i56DB4A0D03FBFF9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382139 Genomic DNA. Translation: CAG90638.1.
RefSeqiXP_462152.1. XM_462152.1.

Genome annotation databases

EnsemblFungiiCAG90638; CAG90638; DEHA2G14080g.
GeneIDi2905066.
KEGGidha:DEHA2G14080g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382139 Genomic DNA. Translation: CAG90638.1.
RefSeqiXP_462152.1. XM_462152.1.

3D structure databases

ProteinModelPortaliQ6BI19.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG90638; CAG90638; DEHA2G14080g.
GeneIDi2905066.
KEGGidha:DEHA2G14080g.

Phylogenomic databases

HOGENOMiHOG000242438.
InParanoidiQ6BI19.
KOiK01556.
OMAiVWDLAHS.
OrthoDBiEOG092C20ON.

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. 1 hit.
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...

Entry informationi

Entry nameiKYNU_DEBHA
AccessioniPrimary (citable) accession number: Q6BI19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: August 16, 2004
Last modified: September 7, 2016
This is version 75 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

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 one 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.