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Q9CXF0

- KYNU_MOUSE

UniProt

Q9CXF0 - KYNU_MOUSE

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Protein

Kynureninase

Gene

Kynu

Organism
Mus musculus (Mouse)
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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.UniRule annotation

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei137 – 1371Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei138 – 1381Pyridoxal phosphateUniRule annotation
Binding sitei221 – 2211Pyridoxal phosphateUniRule annotation
Binding sitei250 – 2501Pyridoxal phosphateUniRule annotation
Binding sitei253 – 2531Pyridoxal phosphateUniRule annotation
Binding sitei275 – 2751Pyridoxal phosphateUniRule annotation
Binding sitei305 – 3051Pyridoxal phosphateUniRule annotation
Binding sitei333 – 3331Pyridoxal phosphateUniRule annotation

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. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. response to interferon-gamma Source: Ensembl
  6. response to vitamin B6 Source: Ensembl
  7. tryptophan catabolic process to acetyl-CoA Source: Ensembl
  8. tryptophan catabolic process to kynurenine Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_240936. Tryptophan catabolism.
UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:Kynu
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1918039. Kynu.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464KynureninasePRO_0000218658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineUniRule annotation
Modified residuei276 – 2761N6-(pyridoxal phosphate)lysineUniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CXF0.
PaxDbiQ9CXF0.
PRIDEiQ9CXF0.

PTM databases

PhosphoSiteiQ9CXF0.

Expressioni

Gene expression databases

BgeeiQ9CXF0.
CleanExiMM_KYNU.
ExpressionAtlasiQ9CXF0. baseline and differential.
GenevestigatoriQ9CXF0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9CXF0.
SMRiQ9CXF0. Positions 6-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 1684Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOVERGENiHBG001170.
InParanoidiQ9CXF0.
KOiK01556.
OMAiGWYGGDK.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
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.

Q9CXF0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEPSPLELPV DAVRRIAAEL NCDPTDERVA LRLDEEDKLS HFRNCFYIPK
60 70 80 90 100
MRDLPSIDLS LVSEDDDAIY FLGNSLGLQP KMVRTYLEEE LDKWAKMGAY
110 120 130 140 150
GHDVGKRPWI VGDESIVSLM KDIVGAHEKE IALMNALTIN LHLLLLSFFK
160 170 180 190 200
PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMV KPREGEETLR
210 220 230 240 250
MEDILEVIEE EGDSIAVILF SGLHFYTGQL FNIPAITKAG HAKGCFVGFD
260 270 280 290 300
LAHAVGNVEL RLHDWGVDFA CWCSYKYLNS GAGGLAGAFV HEKHAHTVKP
310 320 330 340 350
ALVGWFGHDL STRFNMDNKL QLIPGANGFR ISNPPILLVC SLHASLEVFQ
360 370 380 390 400
QATMTALRRK SILLTGYLEY MLKHYHSKDN TENKGPIVNI ITPSRAEERG
410 420 430 440 450
CQLTLTFSIP KKSVFKELEK RGVVCDKREP DGIRVAPVPL YNSFHDVYKF
460
IRLLTSILDS SERS
Length:464
Mass (Da):52,325
Last modified:December 16, 2008 - v3
Checksum:iFF51BE81F935E79E
GO

Sequence cautioni

The sequence BAB29386.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC34035.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014484 mRNA. Translation: BAB29386.2. Different initiation.
AK050024 mRNA. Translation: BAC34035.1. Different initiation.
RefSeqiNP_001276522.1. NM_001289593.1.
NP_001276523.1. NM_001289594.1.
NP_081828.1. NM_027552.2.
XP_006498388.1. XM_006498325.1.
UniGeneiMm.105278.

Genome annotation databases

GeneIDi70789.
KEGGimmu:70789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014484 mRNA. Translation: BAB29386.2 . Different initiation.
AK050024 mRNA. Translation: BAC34035.1 . Different initiation.
RefSeqi NP_001276522.1. NM_001289593.1.
NP_001276523.1. NM_001289594.1.
NP_081828.1. NM_027552.2.
XP_006498388.1. XM_006498325.1.
UniGenei Mm.105278.

3D structure databases

ProteinModelPortali Q9CXF0.
SMRi Q9CXF0. Positions 6-460.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9CXF0.

Proteomic databases

MaxQBi Q9CXF0.
PaxDbi Q9CXF0.
PRIDEi Q9CXF0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 70789.
KEGGi mmu:70789.

Organism-specific databases

CTDi 8942.
MGIi MGI:1918039. Kynu.

Phylogenomic databases

eggNOGi COG3844.
HOVERGENi HBG001170.
InParanoidi Q9CXF0.
KOi K01556.
OMAi GWYGGDK.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .
Reactomei REACT_240936. Tryptophan catabolism.

Miscellaneous databases

ChiTaRSi Kynu. mouse.
NextBioi 332254.
PROi Q9CXF0.
SOURCEi Search...

Gene expression databases

Bgeei Q9CXF0.
CleanExi MM_KYNU.
ExpressionAtlasi Q9CXF0. baseline and differential.
Genevestigatori Q9CXF0.

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_dom.
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

  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.
    , 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.

Entry informationi

Entry nameiKYNU_MOUSE
AccessioniPrimary (citable) accession number: Q9CXF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: December 16, 2008
Last modified: November 26, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3