Hmdb loader
Identification
HMDB Protein ID HMDBP00378
Secondary Accession Numbers
  • 5615
  • HMDBP03657
Name Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
Synonyms
  1. 2-aminoadipate aminotransferase
  2. 2-aminoadipate transaminase
  3. AadAT
  4. Alpha-aminoadipate aminotransferase
  5. KAT/AadAT
  6. Kynurenine aminotransferase II
  7. Kynurenine--oxoglutarate aminotransferase II
  8. Kynurenine--oxoglutarate transaminase II
  9. Kynurenine--oxoglutarate transaminase 2
Gene Name AADAT
Protein Type Enzyme
Biological Properties
General Function Involved in transferase activity, transferring nitrogenous groups
Specific 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).
Pathways
  • 2-aminoadipic 2-oxoadipic aciduria
  • 2-Oxocarboxylic acid metabolism
  • Glutaric Aciduria Type I
  • Hyperlysinemia I, Familial
  • Hyperlysinemia II or Saccharopinuria
  • L-lysine degradation via saccharopine pathway
  • Lysine biosynthesis
  • Lysine degradation
  • Lysine degradation
  • Pyridoxine dependency with seizures
  • Saccharopinuria/Hyperlysinemia II
  • Tryptophan metabolism
  • Tryptophan metabolism
Reactions
L-Kynurenine + Oxoglutaric acid → 4-(2-Aminophenyl)-2,4-dioxobutanoic acid + L-Glutamic acid details
Aminoadipic acid + Oxoglutaric acid → Oxoadipic acid + L-Glutamic acid details
L-3-Hydroxykynurenine + Oxoglutaric acid → 4-(2-Amino-3-hydroxyphenyl)-2,4-dioxobutanoic acid + L-Glutamic acid details
GO Classification
Biological Process
tryptophan catabolic process
2-oxoglutarate metabolic process
biosynthetic process
glutamate metabolic process
L-lysine catabolic process to acetyl-CoA via saccharopine
lysine catabolic process
tryptophan catabolic process to kynurenine
Cellular Component
mitochondrial matrix
Function
binding
catalytic activity
transferase activity
transferase activity, transferring nitrogenous groups
cofactor binding
pyridoxal phosphate binding
Molecular Function
2-aminoadipate transaminase activity
kynurenine-oxoglutarate transaminase activity
pyridoxal phosphate binding
Process
metabolic process
biosynthetic process
Cellular Location
  1. Mitochondrion (Potential)
Gene Properties
Chromosome Location 4
Locus 4q33
SNPs AADAT
Gene Sequence
>1278 bp
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
Protein Properties
Number of Residues 425
Molecular Weight 47351.17
Theoretical pI 6.954
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q8N5Z0
UniProtKB/Swiss-Prot Entry Name AADAT_HUMAN
PDB IDs
GenBank Gene ID AF097994
GeneCard ID AADAT
GenAtlas ID AADAT
HGNC ID HGNC:17929
References
General References
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  2. 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. [PubMed:15489334 ]
  3. 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. [PubMed:12126930 ]
  4. 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. [PubMed:18620547 ]
  5. 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. [PubMed:18056995 ]
  6. 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. [PubMed:18056996 ]