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Q9WVM8 (AADAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. 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:
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Short name=KAT/AadAT
Alternative name(s):
2-aminoadipate aminotransferase
2-aminoadipate transaminase
EC=2.6.1.39
Alpha-aminoadipate aminotransferase
Short name=AadAT
Kynurenine aminotransferase II
Kynurenine--oxoglutarate aminotransferase II
Kynurenine--oxoglutarate transaminase 2
EC=2.6.1.7
Kynurenine--oxoglutarate transaminase II
Gene names
Name:Aadat
Synonyms:Kat2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) By similarity.

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. Ref.1

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Potential
Chain30 – 425396Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
PRO_0000020603

Sites

Binding site201Substrate By similarity
Binding site741Substrate By similarity
Binding site2021Substrate By similarity
Binding site3991Substrate By similarity

Amino acid modifications

Modified residue2631N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WVM8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E3A6711CFE96D77E

FASTA42547,598
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
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. 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: 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] [Europe PMC] [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.
IPIIPI00762346.
RefSeqNP_035964.1. NM_011834.2.
UniGeneMm.35020.

3D structure databases

ProteinModelPortalQ9WVM8.
SMRQ9WVM8. Positions 1-425.
ModBaseSearch...

PTM databases

PhosphoSiteQ9WVM8.

Proteomic databases

PaxDbQ9WVM8.
PRIDEQ9WVM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079472; ENSMUSP00000078436; ENSMUSG00000057228.
GeneID23923.
KEGGmmu:23923.
UCSCuc009lte.1. mouse.

Organism-specific databases

CTD51166.
MGIMGI:1345167. Aadat.

Phylogenomic databases

eggNOGCOG1167.
GeneTreeENSGT00390000004594.
HOGENOMHOG000223057.
HOVERGENHBG050429.
KOK00825.
OMAPFQSASI.
OrthoDBEOG480HWQ.

Enzyme and pathway databases

UniPathwayUPA00868; UER00838.

Gene expression databases

BgeeQ9WVM8.
CleanExMM_AADAT.
GenevestigatorQ9WVM8.
GermOnlineENSMUSG00000057228. Mus musculus.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAADAT. mouse.
NextBio303709.
SOURCESearch...

Entry information

Entry nameAADAT_MOUSE
AccessionPrimary (citable) accession number: Q9WVM8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1999
Last modified: April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families