Reviewed, UniProtKB/Swiss-Prot Q9CXF0 (KYNU_MOUSE)

Names and origin

Protein names

Recommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase

Gene names

Name:

Kynu

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	L-kynurenine + H2O = anthranilate + L-alanine. L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
PTM	Acetylation
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro tryptophan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	kynureninase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 464	464	Kynureninase		PRO_0000218658
Regions
	Region	165 – 168	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	137	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	138	1	Pyridoxal phosphate By similarity
	Binding site	250	1	Pyridoxal phosphate By similarity
	Binding site	253	1	Pyridoxal phosphate By similarity
	Binding site	275	1	Pyridoxal phosphate By similarity
	Binding site	305	1	Pyridoxal phosphate By similarity
	Binding site	333	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	276	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CXF0-1 [UniParc]. Last modified December 16, 2008. Version 3. Checksum: FF51BE81F935E79E	FASTA	464	52,325
	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

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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK014484 mRNA. Translation: BAB29386.2. Different initiation. AK050024 mRNA. Translation: BAC34035.1. Different initiation.
IPI	IPI00187259.
RefSeq	NP_081828.1.
UniGene	Mm.105278
3D structure databases
SMR	Q9CXF0. Positions 7-461.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9CXF0.
Proteomic databases
PRIDE	Q9CXF0.
Genome annotation databases
Ensembl	ENSMUST00000028223; ENSMUSP00000028223; ENSMUSG00000026866; Mus musculus. [Genome view]
GeneID	70789.
KEGG	mmu:70789.
NMPDR	fig|10090.3.peg.5940.
UCSC	uc008jot.1. mouse.
Organism-specific databases
CTD	70789.
MGI	MGI:1918039. Kynu.
Phylogenomic databases
HOGENOM	Q9CXF0.
HOVERGEN	Q9CXF0.
OMA	WQPLSGW.
Enzyme and pathway databases
BRENDA	3.7.1.3. 244.
Gene expression databases
ArrayExpress	Q9CXF0.
Bgee	Q9CXF0.
CleanEx	MM_KYNU.
Genevestigator	Q9CXF0.
GermOnline	ENSMUSG00000026866. Mus musculus.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR14084. Kynureninase. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	332254.
SOURCE	Search...

Entry information

Entry name

KYNU_MOUSE

Accession

Primary (citable) accession number: Q9CXF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	December 16, 2008
Last modified:	November 3, 2009
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)