ID   AADAT_MOUSE             Reviewed;         425 AA.
AC   Q9WVM8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-SEP-2026, entry version 159.
DE   RecName: Full=Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial {ECO:0000305};
DE            Short=KAT/AadAT;
DE   AltName: Full=2-aminoadipate aminotransferase;
DE   AltName: Full=2-aminoadipate transaminase;
DE            EC=2.6.1.39 {ECO:0000250|UniProtKB:Q8N5Z0};
DE   AltName: Full=Alpha-aminoadipate aminotransferase;
DE            Short=AadAT;
DE   AltName: Full=Glycine transaminase AADAT {ECO:0000250|UniProtKB:Q8N5Z0};
DE            EC=2.6.1.4 {ECO:0000250|UniProtKB:Q8N5Z0};
DE   AltName: Full=Kynurenine aminotransferase II;
DE   AltName: Full=Kynurenine--glyoxylate transaminase AADAT {ECO:0000250|UniProtKB:Q8N5Z0};
DE            EC=2.6.1.63 {ECO:0000250|UniProtKB:Q8N5Z0};
DE   AltName: Full=Kynurenine--oxoglutarate aminotransferase II;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase 2;
DE            EC=2.6.1.7 {ECO:0000250|UniProtKB:Q8N5Z0};
DE   AltName: Full=Kynurenine--oxoglutarate transaminase II;
DE   AltName: Full=Methionine--glyoxylate transaminase AADAT {ECO:0000250|UniProtKB:Q8N5Z0};
DE            EC=2.6.1.73 {ECO:0000250|UniProtKB:Q8N5Z0};
DE   Flags: Precursor;
GN   Name=Aadat {ECO:0000312|MGI:MGI:1345167}; Synonyms=Kat2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=10441733; DOI=10.1007/s003359901102;
RA   Yu P., Mosbrook D.M., Tagle D.A.;
RT   "Genomic organization and expression analysis of mouse kynurenine
RT   aminotransferase II, a possible factor in the pathophysiology of
RT   Huntington's disease.";
RL   Mamm. Genome 10:845-852(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-263; LYS-339 AND
RP   LYS-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-179; LYS-263; LYS-339;
RP   LYS-351; LYS-367 AND LYS-422, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Transaminase with broad substrate specificity. Has
CC       transaminase activity towards aminoadipate, kynurenine, methionine and
CC       glutamate. Shows activity also towards tryptophan, aspartate and
CC       hydroxykynurenine. Accepts a variety of oxo-acids as amino-group
CC       acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid,
CC       phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use
CC       glyoxylate as amino-group acceptor (in vitro) (By similarity).
CC       {ECO:0000250|UniProtKB:Q8N5Z0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate +
CC         H2O; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-
CC         glutamate; Xref=Rhea:RHEA:12601, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57499, ChEBI:CHEBI:58672; EC=2.6.1.39;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + 2-oxoglutarate = glyoxylate + L-glutamate;
CC         Xref=Rhea:RHEA:14089, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.4;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-kynurenine + glyoxylate = kynurenate + glycine + H2O;
CC         Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-L-kynurenine + glyoxylate = xanthurenate + glycine +
CC         H2O; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:58125, ChEBI:CHEBI:71201; EC=2.6.1.63;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxohexanoate + L-kynurenine = L-2-aminohexanoate +
CC         kynurenate + H2O; Xref=Rhea:RHEA:66060, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:35177, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC         ChEBI:CHEBI:58455; Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66061;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phenylpyruvate + L-kynurenine = kynurenate + L-phenylalanine
CC         + H2O; Xref=Rhea:RHEA:66092, ChEBI:CHEBI:15377, ChEBI:CHEBI:18005,
CC         ChEBI:CHEBI:57959, ChEBI:CHEBI:58095, ChEBI:CHEBI:58454;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66093;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-methylsulfanyl-2-oxobutanoate + L-kynurenine = kynurenate +
CC         L-methionine + H2O; Xref=Rhea:RHEA:69096, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16723, ChEBI:CHEBI:57844, ChEBI:CHEBI:57959,
CC         ChEBI:CHEBI:58454; Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69097;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxo-3-sulfanylpropanoate + L-kynurenine = kynurenate + L-
CC         cysteine + H2O; Xref=Rhea:RHEA:69104, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:57678, ChEBI:CHEBI:57959,
CC         ChEBI:CHEBI:58454; Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69105;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=indole-3-pyruvate + L-kynurenine = kynurenate + L-tryptophan +
CC         H2O; Xref=Rhea:RHEA:66052, ChEBI:CHEBI:15377, ChEBI:CHEBI:17640,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66053;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxopentanoate + L-kynurenine = L-2-aminopentanoate +
CC         kynurenate + H2O; Xref=Rhea:RHEA:66076, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28644, ChEBI:CHEBI:57959, ChEBI:CHEBI:58441,
CC         ChEBI:CHEBI:58454; Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66077;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-methyl-2-oxopentanoate + L-kynurenine = kynurenate + L-
CC         leucine + H2O; Xref=Rhea:RHEA:66068, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:57427, ChEBI:CHEBI:57959,
CC         ChEBI:CHEBI:58454; Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66069;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + L-methionine = 4-methylsulfanyl-2-oxobutanoate +
CC         glycine; Xref=Rhea:RHEA:22884, ChEBI:CHEBI:16723, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57844; EC=2.6.1.73;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-2-aminoadipate + glyoxylate = 2-oxoadipate + glycine;
CC         Xref=Rhea:RHEA:69112, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57499, ChEBI:CHEBI:58672;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69113;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine + glyoxylate = 3-(4-hydroxyphenyl)pyruvate +
CC         glycine; Xref=Rhea:RHEA:69116, ChEBI:CHEBI:36242, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:58315;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + L-phenylalanine = 3-phenylpyruvate + glycine;
CC         Xref=Rhea:RHEA:69120, ChEBI:CHEBI:18005, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:58095;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan + glyoxylate = indole-3-pyruvate + glycine;
CC         Xref=Rhea:RHEA:69124, ChEBI:CHEBI:17640, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57912;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine + glyoxylate = 4-methyl-2-oxopentanoate + glycine;
CC         Xref=Rhea:RHEA:69128, ChEBI:CHEBI:17865, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57427;
CC         Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxobutanoate + L-kynurenine = (2S)-2-aminobutanoate +
CC         kynurenate + H2O; Xref=Rhea:RHEA:66044, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC         ChEBI:CHEBI:74359; Evidence={ECO:0000250|UniProtKB:Q64602};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66045;
CC         Evidence={ECO:0000250|UniProtKB:Q64602};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoadipate + L-kynurenine = L-2-aminoadipate + kynurenate +
CC         H2O; Xref=Rhea:RHEA:70047, ChEBI:CHEBI:15377, ChEBI:CHEBI:57499,
CC         ChEBI:CHEBI:57959, ChEBI:CHEBI:58454, ChEBI:CHEBI:58672;
CC         Evidence={ECO:0000250|UniProtKB:Q64602};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70048;
CC         Evidence={ECO:0000250|UniProtKB:Q64602};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 4/6.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in kidney and to a lesser amount
CC       in liver and brain. {ECO:0000269|PubMed:10441733}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AF072376; AAD39680.1; -; mRNA.
DR   EMBL; AK075578; BAC35833.1; -; mRNA.
DR   EMBL; BC012637; AAH12637.1; -; mRNA.
DR   CCDS; CCDS22320.1; -.
DR   RefSeq; NP_035964.1; NM_011834.2.
DR   AlphaFoldDB; Q9WVM8; -.
DR   SMR; Q9WVM8; -.
DR   FunCoup; Q9WVM8; 691.
DR   STRING; 10090.ENSMUSP00000078436; -.
DR   iPTMnet; Q9WVM8; -.
DR   PhosphoSitePlus; Q9WVM8; -.
DR   SwissPalm; Q9WVM8; -.
DR   jPOST; Q9WVM8; -.
DR   PaxDb; 10090-ENSMUSP00000078436; -.
DR   ProteomicsDB; 285893; -.
DR   Antibodypedia; 17143; 329 antibodies from 35 providers.
DR   DNASU; 23923; -.
DR   Ensembl; ENSMUST00000079472.4; ENSMUSP00000078436.3; ENSMUSG00000057228.7.
DR   GeneID; 23923; -.
DR   KEGG; mmu:23923; -.
DR   UCSC; uc009lte.1; mouse.
DR   AGR; MGI:1345167; -.
DR   CTD; 51166; -.
DR   MGI; MGI:1345167; Aadat.
DR   VEuPathDB; HostDB:ENSMUSG00000057228; -.
DR   eggNOG; KOG0634; Eukaryota.
DR   GeneTree; ENSGT00390000004594; -.
DR   HOGENOM; CLU_017584_0_6_1; -.
DR   InParanoid; Q9WVM8; -.
DR   OMA; FMPGEPF; -.
DR   PhylomeDB; Q9WVM8; -.
DR   BRENDA; 2.6.1.39; 3474.
DR   BRENDA; 2.6.1.7; 3474.
DR   Reactome; R-MMU-71064; Lysine catabolism.
DR   Reactome; R-MMU-71240; Tryptophan catabolism.
DR   UniPathway; UPA00868; UER00838.
DR   BioGRID-ORCS; 23923; 3 hits in 77 CRISPR screens.
DR   PRO; PR:Q9WVM8; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9WVM8; protein.
DR   Bgee; ENSMUSG00000057228; Expressed in right kidney and 69 other cell types or tissues.
DR   ExpressionAtlas; Q9WVM8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0047313; F:aromatic-amino-acid:glyoxylate transaminase activity; IEA:RHEA.
DR   GO; GO:0047958; F:glycine:2-oxoglutarate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0047536; F:L-2-aminoadipate:2-oxoglutarate transaminase activity; IDA:MGI.
DR   GO; GO:0016212; F:L-kynurenine:2-oxoglutarate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0047315; F:L-kynurenine:glyoxylate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0050094; F:L-methionine:glyoxylate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:GO_Central.
DR   GO; GO:1901606; P:alpha-amino acid catabolic process; IGI:MGI.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0009063; P:amino acid catabolic process; IGI:MGI.
DR   GO; GO:0006536; P:glutamate metabolic process; ISO:GO_Central.
DR   GO; GO:0019477; P:L-lysine catabolic process; IGI:MGI.
DR   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000071; Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial; 1.
DR   FunFam; 3.90.1150.10:FF:000166; Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR050859; Class-I_PLP-dep_aminotransf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF19; KYNURENINE_ALPHA-AMINOADIPATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aminotransferase; Mitochondrion; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..425
FT                   /note="Kynurenine/alpha-aminoadipate aminotransferase,
FT                   mitochondrial"
FT                   /id="PRO_0000020603"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         172
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         263
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         263
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         339
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         339
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         351
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         367
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         367
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         422
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
SQ   SEQUENCE   425 AA;  47598 MW;  E3A6711CFE96D77E CRC64;
     MNYSRFLTAT SLARKPSPIR TTADILSKAP KTLISLAPGS PNPSMFPFKS AAFTVENGST
     IRFEDDLIKR ALQYSPSYGI PELLSWLKQF QVKLHNPPTV NYPPNQGQMD LCITSGCQDG
     LCKAFEMLIN PGDTILVNEP LFPGTLYAMK PLGCNIINVP SDEHGIIPEG LKKILSQWKP
     EDSKDPTKKT PKFLYTVPNG NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFSK
     PWEPTFLSMD VDGRVIRADT FSKTVSSGLR VGFMTGPKTL IQNIVLHTQV SSVHACTLSQ
     LMILQLLHQW GEEGFLAHID RTIDFYKNQR DSILAAADKW LRGLAEWHVP KAGMFLWIKV
     KGISDTKQLI EEKAIEREVL LVPGNGFFID GSAPTSFFRA SFSLATPAQM DTAFQRLAQL
     IKESL
//