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P70712 (KYNU_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. 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
Name:Kynu
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. Ref.2

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. Ref.2

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. Ref.2

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Inhibited by o-methylbenzoylalanine (OMBA). Ref.2

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.

Subcellular location

Cytoplasm HAMAP-Rule MF_03017.

Tissue specificity

High levels in liver and kidney. Also detected in heart, retina, ovary. Lung, testis and brain. Ref.2

Induction

Inhibited by thiol reagents and heavy metal ions. Ref.2

Sequence similarities

Belongs to the kynureninase family.

Biophysicochemical properties

Kinetic parameters:

KM=440 µM for L-kynurenine Ref.2

KM=32 µM for DL-3-hydroxykynurenine

pH dependence:

Optimum pH is about 9.0 with L-kynurenine as substrate, and about 8.5 with DL-3-hydroxykynurenine as substrate.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Kynureninase HAMAP-Rule MF_03017
PRO_0000218659

Regions

Region165 – 1684Pyridoxal phosphate binding By similarity

Sites

Binding site1371Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1381Pyridoxal phosphate By similarity
Binding site2211Pyridoxal phosphate By similarity
Binding site2501Pyridoxal phosphate By similarity
Binding site2531Pyridoxal phosphate By similarity
Binding site2751Pyridoxal phosphate By similarity
Binding site3051Pyridoxal phosphate By similarity
Binding site3331Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine HAMAP-Rule MF_03017
Modified residue2761N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict181T → A in AAC53206. Ref.2
Sequence conflict261D → N AA sequence Ref.1
Sequence conflict1181S → T in AAC53206. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P70712 [UniParc].

Last modified November 9, 2004. Version 2.
Checksum: 1490A74EFF7287AC

FASTA46452,470
        10         20         30         40         50         60 
MEPSPLELPV DAVRRIATEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK MRDLPSIDLS 

        70         80         90        100        110        120 
LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY GHEVGKRPWI IGDESIVSLM 

       130        140        150        160        170        180 
KDIVGAHEKE IALMNALTVN LHLLLLSFFK PTPKRHKILL EAKAFPSDHY AIESQIQLHG 

       190        200        210        220        230        240 
LDVEKSMRMI KPREGEETLR MEDILEVIEK EGDSIAVVLF SGLHFYTGQL FNIPAITQAG 

       250        260        270        280        290        300 
HAKGCFVGFD LAHAVGNVEL HLHDWDVDFA CWCSYKYLNS GAGGLAGAFI HEKHAHTIKP 

       310        320        330        340        350        360 
ALVGWFGHEL STRFNMDNKL QLIPGVNGFR ISNPPILLVC SLHASLEIFQ QATMTALRRK 

       370        380        390        400        410        420 
SILLTGYLEY LLKHYHGGND TENKRPVVNI ITPSRAEERG CQLTLTFSIS KKGVFKELEK 

       430        440        450        460 
RGVVCDKREP EGIRVAPVPL YNSFHDVYKF IRLLTAILDS TERN 

« Hide

References

« Hide 'large scale' references
[1]"Amino-acid sequence of rat liver kynureninase."
Takeuchi F., Tsubouchi R., Yoshino M., Shibata Y.
Biochim. Biophys. Acta 1252:185-188(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION.
Strain: Wistar.
Tissue: Liver.
[2]"Cloning and recombinant expression of rat and human kynureninase."
Toma S., Nakamura M., Tone S., Okuno E., Kido R., Breton J., Avanzi N., Cozzi L., Speciale C., Mostardini M., Gatti S., Benatti L.
FEBS Lett. 408:5-10(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Isolation and expression of a cDNA clone encoding human kynureninase."
Alberati-Giani D., Buchli R., Malherbe P., Broger C., Lang G., Koehler C., Lahm H.-W., Cesura A.M.
Eur. J. Biochem. 239:460-468(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-117, PARTIAL PROTEIN SEQUENCE.
Tissue: Kidney and Liver.
[5]Matsui Lee I.S., Okuno E., Kido R.
Submitted (JUN-1992) to the PIR data bank
Cited for: PROTEIN SEQUENCE OF 83-116 AND 273-319.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U68168 mRNA. Translation: AAC53206.1.
BC078762 mRNA. Translation: AAH78762.1.
PIRPS0370.
S59898.
T48675.
RefSeqNP_446354.1. NM_053902.2.
UniGeneRn.10575.

3D structure databases

ProteinModelPortalP70712.
SMRP70712. Positions 6-460.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP70712.
ChEMBLCHEMBL2969.

Proteomic databases

PRIDEP70712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000043533; ENSRNOP00000050947; ENSRNOG00000029993.
GeneID116682.
KEGGrno:116682.
UCSCRGD:71061. rat.

Organism-specific databases

CTD8942.
RGD71061. Kynu.

Phylogenomic databases

eggNOGCOG3844.
GeneTreeENSGT00390000008033.
HOGENOMHOG000242438.
HOVERGENHBG001170.
KOK01556.
OMAGWYGGDK.
OrthoDBEOG7D2FDV.
PhylomeDBP70712.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15007.
SABIO-RKP70712.
UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Gene expression databases

GenevestigatorP70712.

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...

Other

NextBio619528.
PROP70712.

Entry information

Entry nameKYNU_RAT
AccessionPrimary (citable) accession number: P70712
Secondary accession number(s): Q68G25, Q7M0D0, Q9QW90
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 9, 2004
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways