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Q9CXF0 (KYNU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length464 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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity 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.

Sequence caution

The sequence BAB29386.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAC34035.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Kynureninase HAMAP-Rule MF_03017
PRO_0000218658

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 By similarity
Modified residue2761N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CXF0 [UniParc].

Last modified December 16, 2008. Version 3.
Checksum: FF51BE81F935E79E

FASTA46452,325
        10         20         30         40         50         60 
MEPSPLELPV DAVRRIAAEL NCDPTDERVA LRLDEEDKLS HFRNCFYIPK MRDLPSIDLS 

        70         80         90        100        110        120 
LVSEDDDAIY FLGNSLGLQP KMVRTYLEEE LDKWAKMGAY GHDVGKRPWI VGDESIVSLM 

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

       190        200        210        220        230        240 
LDVEKSMRMV KPREGEETLR MEDILEVIEE EGDSIAVILF SGLHFYTGQL FNIPAITKAG 

       250        260        270        280        290        300 
HAKGCFVGFD LAHAVGNVEL RLHDWGVDFA CWCSYKYLNS GAGGLAGAFV HEKHAHTVKP 

       310        320        330        340        350        360 
ALVGWFGHDL STRFNMDNKL QLIPGANGFR ISNPPILLVC SLHASLEVFQ QATMTALRRK 

       370        380        390        400        410        420 
SILLTGYLEY MLKHYHSKDN TENKGPIVNI ITPSRAEERG CQLTLTFSIP KKSVFKELEK 

       430        440        450        460 
RGVVCDKREP DGIRVAPVPL YNSFHDVYKF IRLLTSILDS SERS 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK014484 mRNA. Translation: BAB29386.2. Different initiation.
AK050024 mRNA. Translation: BAC34035.1. Different initiation.
RefSeqNP_081828.1. NM_027552.2.
XP_006498388.1. XM_006498325.1.
UniGeneMm.105278.

3D structure databases

ProteinModelPortalQ9CXF0.
SMRQ9CXF0. Positions 6-460.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CXF0.

Proteomic databases

PaxDbQ9CXF0.
PRIDEQ9CXF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID70789.
KEGGmmu:70789.

Organism-specific databases

CTD8942.
MGIMGI:1918039. Kynu.

Phylogenomic databases

eggNOGCOG3844.
HOVERGENHBG001170.
InParanoidQ9CXF0.
KOK01556.
OMAGWYGGDK.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Gene expression databases

ArrayExpressQ9CXF0.
BgeeQ9CXF0.
CleanExMM_KYNU.
GenevestigatorQ9CXF0.

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

ChiTaRSKYNU. mouse.
NextBio332254.
PROQ9CXF0.
SOURCESearch...

Entry information

Entry nameKYNU_MOUSE
AccessionPrimary (citable) accession number: Q9CXF0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: December 16, 2008
Last modified: March 19, 2014
This is version 98 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot