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Q5DGJ1 (KYNU_SCHJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase

EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
ORF Names:SJCHGC00887
OrganismSchistosoma japonicum (Blood fluke)
Taxonomic identifier6182 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length436 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
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: UniProtKB-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 – 436436Kynureninase HAMAP-Rule MF_03017
PRO_0000356960

Regions

Region116 – 1194Pyridoxal phosphate binding By similarity

Sites

Binding site881Pyridoxal phosphate; via amide nitrogen By similarity
Binding site891Pyridoxal phosphate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2051Pyridoxal phosphate By similarity
Binding site2271Pyridoxal phosphate By similarity
Binding site2801Pyridoxal phosphate By similarity
Binding site3081Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5DGJ1 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: D2585D22865EC083

FASTA43650,248
        10         20         30         40         50         60 
MKILQYKSIE NVQYSKNILY FCGHSMGLQP KSTKIYINKI LNQWKNLGVL SYHYGELPAS 

        70         80         90        100        110        120 
YCDEQLSIDC AQWIVNAKFN EVSITCNLTV NMHVLIAKFY RPTNEKYCIL IENDIFPSDY 

       130        140        150        160        170        180 
YVLESHIQWH GYNTNDCFIK LKPRLHEYCL RNDDILPEII KNQHRIALIW LPGIQYITGQ 

       190        200        210        220        230        240 
LFNMKLITEW GHQYAKCPVG WDLAHAVGNI PLYLHDWNID MAVWCSYKYL NGSPGAIGGL 

       250        260        270        280        290        300 
FIHEKHHHEE GSYGPKFIEF TNNNNITIFN NINGPQLTGW WSHRSETRFN MTGNMELAKG 

       310        320        330        340        350        360 
ANAYRLSNPP LLLAAALTVS VNIIKSCGGM INLREKSIKL TDYLEYLITN SSLALKHDHY 

       370        380        390        400        410        420 
CLVTPSNSNE RGAQLTISVT HMNIQVVYEN LLKLGVICDY RLPNFLRITP IPLYNSFEDV 

       430 
YLLAKCLHQV LNDTLN 

« Hide

References

[1]"New perspectives on host-parasite interplay by comparative transcriptomic and proteomic analyses of Schistosoma japonicum."
Liu F., Lu J., Hu W., Wang S.-Y., Cui S.-J., Chi M., Yan Q., Wang X.-R., Song H.-D., Xu X.-N., Wang J.-J., Zhang X.-L., Zhang X., Wang Z.-Q., Xue C.-L., Brindley P.J., McManus D.P., Yang P.-Y. expand/collapse author list , Feng Z., Chen Z., Han Z.-G.
PLoS Pathog. 2:268-281(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY813333 mRNA. Translation: AAW25065.1.

3D structure databases

ProteinModelPortalQ5DGJ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6182.Q5DGJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3844.

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. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_SCHJA
AccessionPrimary (citable) accession number: Q5DGJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 29, 2005
Last modified: February 19, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways