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Protein

Kynureninase

Gene

BNA5

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
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:iL-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:iNAD(+) 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 sitei106 – 1061Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei107 – 1071Pyridoxal phosphateUniRule annotation
Binding sitei220 – 2201Pyridoxal phosphateUniRule annotation
Binding sitei223 – 2231Pyridoxal phosphateUniRule annotation
Binding sitei245 – 2451Pyridoxal 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
Ordered Locus Names:AGL098W
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
ProteomesiUP000000591 Componenti: Chromosome VII

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 – 447447KynureninasePRO_0000218661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1374Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
InParanoidiQ750P5.
KOiK01556.
OMAiWLPYHEL.
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.

Q750P5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKARALEEQ WPGARDAFHV PSYASLGLGD QTAAVRYLCG HSLGCMPRKT
60 70 80 90 100
RGSVEAELSA WSARAVEAHV RHPGGTEWVN TDLPLVPQMA RMVGASQQEV
110 120 130 140 150
AVMGSLTANL NALLVAFYRP RGRRTKILLE KQVFPSDFHA FWNQAALHGL
160 170 180 190 200
DPAATLVQVA PRAGEHTLRT EDIVAAIETH RAELALVCLP GVQYYTGQLL
210 220 230 240 250
DMASIVAAAR REPSIVVGFD LAHAVGNVQL QLHEWGADFA CWCSYKYLNA
260 270 280 290 300
GPGGIAGLFV HERHHGGTLP RLAGWWGTNA ATRFEMRQTY DPLPDALGFR
310 320 330 340 350
QSNPSVLDVA ALRASLEVFE DFGGMERVRA RSLALTGYLY ELLTQSVFYR
360 370 380 390 400
PEVGADGVGF TILTPANPAE RGAQLSLLFW PHSDDPDKNT MPRVFADLRQ
410 420 430 440
NGVLGDERHP DVIRLTPCAL YNTFMEVFES VQLLNAALER LAPESAV
Length:447
Mass (Da):49,032
Last modified:January 9, 2013 - v2
Checksum:i8B39CBFF1EA2AC8A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016820 Genomic DNA. Translation: AAS54393.2.
RefSeqiNP_986569.2. NM_211631.2.

Genome annotation databases

EnsemblFungiiAAS54393; AAS54393; AGOS_AGL098W.
GeneIDi4622868.
KEGGiago:AGOS_AGL098W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016820 Genomic DNA. Translation: AAS54393.2.
RefSeqiNP_986569.2. NM_211631.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS54393; AAS54393; AGOS_AGL098W.
GeneIDi4622868.
KEGGiago:AGOS_AGL098W.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
InParanoidiQ750P5.
KOiK01556.
OMAiWLPYHEL.
OrthoDBiEOG7V1G0J.

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

« Hide 'large scale' publications
  1. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
    Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
    Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
  2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
    Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
    G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 175; 263 AND 273.
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Entry informationi

Entry nameiKYNU_ASHGO
AccessioniPrimary (citable) accession number: Q750P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: January 9, 2013
Last modified: July 22, 2015
This is version 76 of the entry and version 2 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.