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Q18026 (KYNU_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Kynureninase
EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
ORF Names:C15H9.7
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_03017

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_03017

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_03017

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_03017

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03017.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkynureninase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478Kynureninase HAMAP-Rule MF_03017
PRO_0000218660

Regions

Region178 – 1814Pyridoxal phosphate binding By similarity

Sites

Binding site1501Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1511Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate By similarity
Binding site2661Pyridoxal phosphate By similarity
Binding site2881Pyridoxal phosphate By similarity
Binding site3181Pyridoxal phosphate By similarity
Binding site3461Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2891N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q18026 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E889450929EC94BD

FASTA47854,050
        10         20         30         40         50         60 
MSDAPPQPEN EQECMCTQDK VLQFLNKMAD ESGIKDLTDP ALAEFLSDSD ALKEIRDLFH 

        70         80         90        100        110        120 
YPKAGTLPDA DPSLVDPESD SIYLCGNSLG LMPKATGEVM KDHLDKWAKM GVFGHMSGEV 

       130        140        150        160        170        180 
PWAHCDEYCL EGVGRLVGAK KEEVSVCNSL TVNIHVLLTS FYKPTETRHK ILLESKAFPS 

       190        200        210        220        230        240 
DHYAIESQIR LKGRTVQDSM VCLEPREGEE TLRTEDILDY IEKNGDEIAI VFFSGIQYYT 

       250        260        270        280        290        300 
GQLFDMRAIT EAGHRKGCFV GFDLAHAFAN VPLHLHWWDV DFACWCSYKY GCTGAGSIGG 

       310        320        330        340        350        360 
LFVHERFLND QRERMLGWWS HKMSSRFVMD NVLDLDEGAA GYRISNPPIH TVAAMLGSLK 

       370        380        390        400        410        420 
VFDQVSLENL RSRSCYLTGY LEYLVKTLFG ENSEQRTTKL SISIITPEEF HQRGCQLSLK 

       430        440        450        460        470 
FSSPIDIIYP ELVKRGCAVD KRYPNVIRVA PVHLYNNYVD IRRFISVLQE VAHIVESE

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FO080555 Genomic DNA. Translation: CCD64633.1.
AF303267 mRNA. Translation: AAG50225.1.
PIRT15516.
RefSeqNP_509023.1. NM_076622.4.
UniGeneCel.19413.

3D structure databases

ProteinModelPortalQ18026.
SMRQ18026. Positions 38-471.
ModBaseSearch...

Protein-protein interaction databases

IntActQ18026. 1 interaction.
STRING6239.C15H9.7.

Proteomic databases

PaxDbQ18026.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC15H9.7.1; C15H9.7.1; C15H9.7.
C15H9.7.2; C15H9.7.2; C15H9.7.
GeneID180883.
KEGGcel:CELE_C15H9.7.
UCSCC15H9.7. c. elegans.

Organism-specific databases

CTD180883.
WormBaseC15H9.7; CE06835; WBGene00015802.

Phylogenomic databases

eggNOGCOG3844.
GeneTreeENSGT00390000008033.
HOGENOMHOG000242438.
InParanoidQ18026.
KOK01556.
OMAMVSFYRP.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Other

NextBio911400.

Entry information

Entry nameKYNU_CAEEL
AccessionPrimary (citable) accession number: Q18026
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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