Reviewed, UniProtKB/Swiss-Prot Q9WVM8 (AADAT_MOUSE)

Names and origin

Protein names

Recommended name:
    Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Alternative name(s):
    KAT/AadAT
    EC=2.6.1.7
    Kynurenine aminotransferase II
    Kynurenine--oxoglutarate aminotransferase II
    Kynurenine--oxoglutarate transaminase II
    2-aminoadipate transaminase
    EC=2.6.1.39
    2-aminoadipate aminotransferase
    Alpha-aminoadipate aminotransferase
      Short name=AadAT

Gene names

Name:	Aadat
Synonyms:	Kat2

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	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Shows activity also towards tryptophan, aspartate and hydroxykinurenine.
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion Potential.
Tissue specificity	Expressed mainly in kidney and to a lesser amount in liver and brain.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	2-aminoadipate transaminase activity Inferred from electronic annotation. Source: EC kynurenine-oxoglutarate transaminase 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
	Transit peptide	1 – 29	29	Mitochondrion Potential
	Chain	30 – 425	396	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial		PRO_0000020603
Amino acid modifications
	Modified residue	263	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WVM8-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E3A6711CFE96D77E	FASTA	425	47,598
	10 20 30 40 50 60 MNYSRFLTAT SLARKPSPIR TTADILSKAP KTLISLAPGS PNPSMFPFKS AAFTVENGST 70 80 90 100 110 120 IRFEDDLIKR ALQYSPSYGI PELLSWLKQF QVKLHNPPTV NYPPNQGQMD LCITSGCQDG 130 140 150 160 170 180 LCKAFEMLIN PGDTILVNEP LFPGTLYAMK PLGCNIINVP SDEHGIIPEG LKKILSQWKP 190 200 210 220 230 240 EDSKDPTKKT PKFLYTVPNG NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFSK 250 260 270 280 290 300 PWEPTFLSMD VDGRVIRADT FSKTVSSGLR VGFMTGPKTL IQNIVLHTQV SSVHACTLSQ 310 320 330 340 350 360 LMILQLLHQW GEEGFLAHID RTIDFYKNQR DSILAAADKW LRGLAEWHVP KAGMFLWIKV 370 380 390 400 410 420 KGISDTKQLI EEKAIEREVL LVPGNGFFID GSAPTSFFRA SFSLATPAQM DTAFQRLAQL IKESL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization and expression analysis of mouse kynurenine aminotransferase II, a possible factor in the pathophysiology of Huntington's disease." Yu P., Mosbrook D.M., Tagle D.A. Mamm. Genome 10:845-852(1999) [PubMed: 10441733] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/SvJ.
[2]	"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: Kidney.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF072376 mRNA. Translation: AAD39680.1. AK075578 mRNA. Translation: BAC35833.1. BC012637 mRNA. Translation: AAH12637.1.
IPI	IPI00762346.
RefSeq	NP_035964.1.
UniGene	Mm.35020
3D structure databases
SMR	Q9WVM8. Positions 1-425.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9WVM8.
Proteomic databases
PRIDE	Q9WVM8.
Genome annotation databases
Ensembl	ENSMUST00000079472; ENSMUSP00000078436; ENSMUSG00000057228; Mus musculus. [Genome view]
GeneID	23923.
KEGG	mmu:23923.
UCSC	uc009lte.1. mouse.
Organism-specific databases
CTD	23923.
MGI	MGI:1345167. Aadat.
Phylogenomic databases
HOVERGEN	Q9WVM8.
OrthoDB	EOG9C8BC9.
PhylomeDB	Q9WVM8.
Enzyme and pathway databases
BRENDA	2.6.1.39. 244. 2.6.1.7. 244.
Gene expression databases
ArrayExpress	Q9WVM8.
Bgee	Q9WVM8.
CleanEx	MM_AADAT.
Genevestigator	Q9WVM8.
GermOnline	ENSMUSG00000057228. Mus musculus.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	303709.
SOURCE	Search...

Entry information

Entry name

AADAT_MOUSE

Accession

Primary (citable) accession number: Q9WVM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	November 1, 1999
Last modified:	January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)