SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9CXF0

- KYNU_MOUSE

UniProt

Q9CXF0 - KYNU_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Kynureninase
Gene
Kynu
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Pyridoxal phosphate By similarity.UniRule annotation

Pathwayi

Sites

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

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. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  3. anthranilate metabolic process Source: UniProtKB-HAMAP
  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

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:1918039. Kynu.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464KynureninaseUniRule annotation
PRO_0000218658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei276 – 2761N6-(pyridoxal phosphate)lysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CXF0.
PaxDbiQ9CXF0.
PRIDEiQ9CXF0.

PTM databases

PhosphoSiteiQ9CXF0.

Expressioni

Gene expression databases

ArrayExpressiQ9CXF0.
BgeeiQ9CXF0.
CleanExiMM_KYNU.
GenevestigatoriQ9CXF0.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9CXF0.
SMRiQ9CXF0. Positions 6-460.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 1684Pyridoxal phosphate binding By similarity

Sequence similaritiesi

Belongs to the kynureninase family.

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/Cys_dSase.
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

MEPSPLELPV DAVRRIAAEL NCDPTDERVA LRLDEEDKLS HFRNCFYIPK    50
MRDLPSIDLS LVSEDDDAIY FLGNSLGLQP KMVRTYLEEE LDKWAKMGAY 100
GHDVGKRPWI VGDESIVSLM KDIVGAHEKE IALMNALTIN LHLLLLSFFK 150
PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMV KPREGEETLR 200
MEDILEVIEE EGDSIAVILF SGLHFYTGQL FNIPAITKAG HAKGCFVGFD 250
LAHAVGNVEL RLHDWGVDFA CWCSYKYLNS GAGGLAGAFV HEKHAHTVKP 300
ALVGWFGHDL STRFNMDNKL QLIPGANGFR ISNPPILLVC SLHASLEVFQ 350
QATMTALRRK SILLTGYLEY MLKHYHSKDN TENKGPIVNI ITPSRAEERG 400
CQLTLTFSIP KKSVFKELEK RGVVCDKREP DGIRVAPVPL YNSFHDVYKF 450
IRLLTSILDS SERS 464
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.
The sequence BAC34035.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .

Miscellaneous databases

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

Gene expression databases

ArrayExpressi Q9CXF0.
Bgeei Q9CXF0.
CleanExi MM_KYNU.
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/Cys_dSase.
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: June 11, 2014
This is version 100 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

Similar proteinsi