AADAT_MOUSE
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 03-AUG-2022, entry version 141.
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=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC 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=2-oxoglutarate + L-2-aminoadipate = 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=2-oxoglutarate + glycine = 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=glyoxylate + L-kynurenine = glycine + H2O + kynurenate;
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 = glycine + H2O +
CC xanthurenate; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58125,
CC ChEBI:CHEBI:71201; EC=2.6.1.63;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxohexanoate + L-kynurenine = H2O + kynurenate + L-2-
CC aminohexanoate; 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 = H2O + kynurenate + L-
CC phenylalanine; Xref=Rhea:RHEA:66092, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:57959, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58454; 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 = H2O +
CC kynurenate + L-methionine; 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 = H2O + kynurenate +
CC L-cysteine; 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 = H2O + kynurenate + L-
CC tryptophan; Xref=Rhea:RHEA:66052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:57912, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; 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 = H2O + kynurenate + L-2-
CC aminopentanoate; 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 = H2O + kynurenate +
CC L-leucine; 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=glyoxylate + L-2-aminoadipate = 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=glyoxylate + L-tyrosine = 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=glyoxylate + L-tryptophan = glycine + indole-3-pyruvate;
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=glyoxylate + L-leucine = 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 + H2O +
CC kynurenate; 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 = H2O + kynurenate + L-2-
CC aminoadipate; Xref=Rhea:RHEA:70047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57499, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC ChEBI:CHEBI:58672; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 STRING; 10090.ENSMUSP00000078436; -.
DR iPTMnet; Q9WVM8; -.
DR PhosphoSitePlus; Q9WVM8; -.
DR jPOST; Q9WVM8; -.
DR MaxQB; Q9WVM8; -.
DR PaxDb; Q9WVM8; -.
DR PRIDE; Q9WVM8; -.
DR ProteomicsDB; 285893; -.
DR Antibodypedia; 17143; 331 antibodies from 35 providers.
DR DNASU; 23923; -.
DR Ensembl; ENSMUST00000079472; ENSMUSP00000078436; ENSMUSG00000057228.
DR GeneID; 23923; -.
DR KEGG; mmu:23923; -.
DR UCSC; uc009lte.1; mouse.
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; MRLNFTY; -.
DR OrthoDB; 1241781at2759; -.
DR PhylomeDB; Q9WVM8; -.
DR TreeFam; TF328598; -.
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 72 CRISPR screens.
DR ChiTaRS; Aadat; mouse.
DR PRO; PR:Q9WVM8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9WVM8; protein.
DR Bgee; ENSMUSG00000057228; Expressed in right kidney and 67 other tissues.
DR ExpressionAtlas; Q9WVM8; baseline and differential.
DR Genevisible; Q9WVM8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; ISS:UniProtKB.
DR GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
DR GO; GO:0050094; F:methionine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 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
