You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Toxin, Toxin Target Database.
NameKynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Synonyms
  • 2-aminoadipate aminotransferase
  • 2-aminoadipate transaminase
  • AadAT
  • Alpha-aminoadipate aminotransferase
  • KAT/AadAT
  • KAT2
  • Kynurenine aminotransferase II
  • Kynurenine--oxoglutarate aminotransferase II
  • Kynurenine--oxoglutarate transaminase 2
  • Kynurenine--oxoglutarate transaminase II
Gene NameAADAT
OrganismHuman
Amino acid sequence
>lcl|BSEQ0001450|Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
Number of residues425
Molecular Weight47351.17
Theoretical pI6.96
GO Classification
Functions
  • protein homodimerization activity
  • kynurenine-oxoglutarate transaminase activity
  • 2-aminoadipate transaminase activity
  • pyridoxal phosphate binding
Processes
  • cellular nitrogen compound metabolic process
  • small molecule metabolic process
  • L-lysine catabolic process to acetyl-CoA via saccharopine
  • lysine catabolic process
  • 2-oxoglutarate metabolic process
  • glutamate metabolic process
  • tryptophan catabolic process
  • tryptophan catabolic process to kynurenine
  • biosynthetic process
  • kynurenine metabolic process
  • L-kynurenine metabolic process
Components
  • mitochondrial matrix
General FunctionPyridoxal phosphate binding
Specific FunctionTransaminase 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).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID6165634
UniProtKB IDQ8N5Z0
UniProtKB Entry NameAADAT_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0016189|Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (AADAT)
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGAGTGAGAAACGGGCTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTG
GCTGGTGGCTTACCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAA
AATGGAAAGACCATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCG
AGTGCTGGAATTCCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAAT
CCTCCTACCATCCATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGC
AGCCAACAAGGTCTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTC
CTAGATGAACCTGCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATT
ATTAATGTTGCCAGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCC
AGATGGAAACCAGAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACT
GTTCCAAATGGCAACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATC
TATGAGCTTGCAAGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTC
CAGTTTAACAAGTTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATC
AGAGCTGACTCTTTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGT
CCAAAACCCTTAATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGC
ACTTTTAACCAGCTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATG
GCTCATGTAGACAGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCT
GCAGACAAGTGGTTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTA
TGGATTAAAGTTAAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAG
ATGGGGGTATTAATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCT
TACTTGAGAGCATCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTA
TTAGCACAACTTATAAAAGAATCTTTATGA
GenBank Gene IDAF097994
GeneCard IDNot Available
GenAtlas IDAADAT
HGNC IDHGNC:17929
Chromosome Location4
Locus4q33
References
  1. Goh DL, Patel A, Thomas GH, Salomons GS, Schor DS, Jakobs C, Geraghty MT: Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT). Mol Genet Metab. 2002 Jul;76(3):172-80. 12126930
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  4. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  5. Han Q, Cai T, Tagle DA, Robinson H, Li J: Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II. Biosci Rep. 2008 Aug;28(4):205-15. doi: 10.1042/BSR20080085. 18620547
  6. Han Q, Robinson H, Li J: Crystal structure of human kynurenine aminotransferase II. J Biol Chem. 2008 Feb 8;283(6):3567-73. Epub 2007 Dec 5. 18056995
  7. Rossi F, Garavaglia S, Montalbano V, Walsh MA, Rizzi M: Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia. J Biol Chem. 2008 Feb 8;283(6):3559-66. Epub 2007 Dec 5. 18056996