Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kynureninase

Gene

flu-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

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 (flu-2)
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 (kmo-1)
  2. Kynureninase (flu-2)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (haao-1)
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 sitei150 – 1501Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei151 – 1511Pyridoxal phosphateUniRule annotation
Binding sitei234 – 2341Pyridoxal phosphateUniRule annotation
Binding sitei263 – 2631Pyridoxal phosphateUniRule annotation
Binding sitei266 – 2661Pyridoxal phosphateUniRule annotation
Binding sitei288 – 2881Pyridoxal phosphateUniRule annotation
Binding sitei318 – 3181Pyridoxal phosphateUniRule annotation
Binding sitei346 – 3461Pyridoxal 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

ReactomeiREACT_336244. Tryptophan catabolism.
UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
Abnormal fluorescence under UV illumination
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:flu-2
ORF Names:C15H9.7
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiC15H9.7; CE06835; WBGene00015802; flu-2.

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 – 478478KynureninasePRO_0000218660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei289 – 2891N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PaxDbiQ18026.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ18026. 1 interaction.
STRINGi6239.C15H9.7.1.

Structurei

3D structure databases

ProteinModelPortaliQ18026.
SMRiQ18026. Positions 38-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 1814Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
GeneTreeiENSGT00390000008033.
HOGENOMiHOG000242438.
InParanoidiQ18026.
KOiK01556.
OMAiHICCIPS.
PhylomeDBiQ18026.

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.

Q18026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAPPQPEN EQECMCTQDK VLQFLNKMAD ESGIKDLTDP ALAEFLSDSD
60 70 80 90 100
ALKEIRDLFH YPKAGTLPDA DPSLVDPESD SIYLCGNSLG LMPKATGEVM
110 120 130 140 150
KDHLDKWAKM GVFGHMSGEV PWAHCDEYCL EGVGRLVGAK KEEVSVCNSL
160 170 180 190 200
TVNIHVLLTS FYKPTETRHK ILLESKAFPS DHYAIESQIR LKGRTVQDSM
210 220 230 240 250
VCLEPREGEE TLRTEDILDY IEKNGDEIAI VFFSGIQYYT GQLFDMRAIT
260 270 280 290 300
EAGHRKGCFV GFDLAHAFAN VPLHLHWWDV DFACWCSYKY GCTGAGSIGG
310 320 330 340 350
LFVHERFLND QRERMLGWWS HKMSSRFVMD NVLDLDEGAA GYRISNPPIH
360 370 380 390 400
TVAAMLGSLK VFDQVSLENL RSRSCYLTGY LEYLVKTLFG ENSEQRTTKL
410 420 430 440 450
SISIITPEEF HQRGCQLSLK FSSPIDIIYP ELVKRGCAVD KRYPNVIRVA
460 470
PVHLYNNYVD IRRFISVLQE VAHIVESE
Length:478
Mass (Da):54,050
Last modified:November 1, 1996 - v1
Checksum:iE889450929EC94BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080555 Genomic DNA. Translation: CCD64633.1.
AF303267 mRNA. Translation: AAG50225.1.
PIRiT15516.
RefSeqiNP_509023.1. NM_076622.4.
UniGeneiCel.19413.

Genome annotation databases

EnsemblMetazoaiC15H9.7; C15H9.7; WBGene00015802.
GeneIDi180883.
KEGGicel:CELE_C15H9.7.
UCSCiC15H9.7. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080555 Genomic DNA. Translation: CCD64633.1.
AF303267 mRNA. Translation: AAG50225.1.
PIRiT15516.
RefSeqiNP_509023.1. NM_076622.4.
UniGeneiCel.19413.

3D structure databases

ProteinModelPortaliQ18026.
SMRiQ18026. Positions 38-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ18026. 1 interaction.
STRINGi6239.C15H9.7.1.

Proteomic databases

PaxDbiQ18026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC15H9.7; C15H9.7; WBGene00015802.
GeneIDi180883.
KEGGicel:CELE_C15H9.7.
UCSCiC15H9.7. c. elegans.

Organism-specific databases

CTDi180883.
WormBaseiC15H9.7; CE06835; WBGene00015802; flu-2.

Phylogenomic databases

eggNOGiCOG3844.
GeneTreeiENSGT00390000008033.
HOGENOMiHOG000242438.
InParanoidiQ18026.
KOiK01556.
OMAiHICCIPS.
PhylomeDBiQ18026.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
ReactomeiREACT_336244. Tryptophan catabolism.

Miscellaneous databases

NextBioi911400.
PROiQ18026.

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. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "The Caenorhabditis elegans transcriptome project, a complementary view of the genome."
    Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y., Thierry-Mieg D., Thierry-Mieg J.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Bristol N2.
  3. "Mutagen sensitivity of kynureninase mutants of the nematode Caenorhabditis elegans."
    Bhat S.G., Babu P.
    Mol. Gen. Genet. 180:635-638(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiKYNU_CAEEL
AccessioniPrimary (citable) accession number: Q18026
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.