SubmitCancel

Skip Header

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

Q18026

- KYNU_CAEEL

UniProt

Q18026 - KYNU_CAEEL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Kynureninase
Gene
flu-2, C15H9.7
Organism
Caenorhabditis elegans
Status
Reviewed - 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.1 Publication

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

Pyridoxal phosphate By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei150 – 1501Pyridoxal phosphate; via amide nitrogen By similarity
Binding sitei151 – 1511Pyridoxal phosphate By similarity
Binding sitei234 – 2341Pyridoxal phosphate By similarity
Binding sitei263 – 2631Pyridoxal phosphate By similarity
Binding sitei266 – 2661Pyridoxal phosphate By similarity
Binding sitei288 – 2881Pyridoxal phosphate By similarity
Binding sitei318 – 3181Pyridoxal phosphate By similarity
Binding sitei346 – 3461Pyridoxal phosphate By similarity

GO - Molecular functioni

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  3. anthranilate metabolic process Source: UniProtKB-HAMAP
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
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:
Kynureninase (EC:3.7.1.3)
Alternative name(s):
Abnormal fluorescence under UV illumination
L-kynurenine hydrolase
Gene namesi
Name:flu-2
ORF Names:C15H9.7
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome X

Organism-specific databases

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

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478KynureninaseUniRule annotation
PRO_0000218660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei289 – 2891N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

PaxDbiQ18026.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiQ18026. 1 interaction.
STRINGi6239.C15H9.7.

Structurei

3D structure databases

ProteinModelPortaliQ18026.
SMRiQ18026. Positions 38-471.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 1814Pyridoxal phosphate binding By similarity

Sequence similaritiesi

Belongs to the kynureninase family.

Phylogenomic databases

eggNOGiCOG3844.
GeneTreeiENSGT00390000008033.
HOGENOMiHOG000242438.
InParanoidiQ18026.
KOiK01556.
OMAiHVAYRSA.
PhylomeDBiQ18026.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V/Cys_dSase.
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

MSDAPPQPEN EQECMCTQDK VLQFLNKMAD ESGIKDLTDP ALAEFLSDSD    50
ALKEIRDLFH YPKAGTLPDA DPSLVDPESD SIYLCGNSLG LMPKATGEVM 100
KDHLDKWAKM GVFGHMSGEV PWAHCDEYCL EGVGRLVGAK KEEVSVCNSL 150
TVNIHVLLTS FYKPTETRHK ILLESKAFPS DHYAIESQIR LKGRTVQDSM 200
VCLEPREGEE TLRTEDILDY IEKNGDEIAI VFFSGIQYYT GQLFDMRAIT 250
EAGHRKGCFV GFDLAHAFAN VPLHLHWWDV DFACWCSYKY GCTGAGSIGG 300
LFVHERFLND QRERMLGWWS HKMSSRFVMD NVLDLDEGAA GYRISNPPIH 350
TVAAMLGSLK VFDQVSLENL RSRSCYLTGY LEYLVKTLFG ENSEQRTTKL 400
SISIITPEEF HQRGCQLSLK FSSPIDIIYP ELVKRGCAVD KRYPNVIRVA 450
PVHLYNNYVD IRRFISVLQE VAHIVESE 478
Length:478
Mass (Da):54,050
Last modified:November 1, 1996 - v1
Checksum:iE889450929EC94BD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
FO080555 Genomic DNA. Translation: CCD64633.1 .
AF303267 mRNA. Translation: AAG50225.1 .
PIRi T15516.
RefSeqi NP_509023.1. NM_076622.4.
UniGenei Cel.19413.

3D structure databases

ProteinModelPortali Q18026.
SMRi Q18026. Positions 38-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q18026. 1 interaction.
STRINGi 6239.C15H9.7.

Proteomic databases

PaxDbi Q18026.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai C15H9.7 ; C15H9.7 ; WBGene00015802 .
GeneIDi 180883.
KEGGi cel:CELE_C15H9.7.
UCSCi C15H9.7. c. elegans.

Organism-specific databases

CTDi 180883.
WormBasei C15H9.7 ; CE06835 ; WBGene00015802 ; flu-2.

Phylogenomic databases

eggNOGi COG3844.
GeneTreei ENSGT00390000008033.
HOGENOMi HOG000242438.
InParanoidi Q18026.
KOi K01556.
OMAi HVAYRSA.
PhylomeDBi Q18026.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .

Miscellaneous databases

NextBioi 911400.
PROi Q18026.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_01970. Kynureninase.
InterProi IPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR14084. PTHR14084. 1 hit.
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF038800. KYNU. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01814. kynureninase. 1 hit.
ProtoNeti Search...

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 11, 2014
This is version 97 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