ID   AATM_MOUSE              Reviewed;         430 AA.
AC   P05202; O09188; Q3TIP6; Q3UD91; Q5HZH5;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   27-MAR-2024, entry version 205.
DE   RecName: Full=Aspartate aminotransferase, mitochondrial;
DE            Short=mAspAT;
DE            EC=2.6.1.1 {ECO:0000250|UniProtKB:P00507};
DE            EC=2.6.1.7 {ECO:0000250|UniProtKB:P00507};
DE   AltName: Full=Fatty acid-binding protein;
DE            Short=FABP-1;
DE   AltName: Full=Glutamate oxaloacetate transaminase 2;
DE   AltName: Full=Kynurenine aminotransferase 4;
DE   AltName: Full=Kynurenine aminotransferase IV;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase 4;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase IV;
DE   AltName: Full=Plasma membrane-associated fatty acid-binding protein;
DE            Short=FABPpm;
DE   AltName: Full=Transaminase A;
DE   Flags: Precursor;
GN   Name=Got2; Synonyms=Got-2;
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].
RX   PubMed=3782150; DOI=10.1016/s0021-9258(19)75987-0;
RA   Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y.;
RT   "Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase
RT   isoenzymes.";
RL   J. Biol. Chem. 261:16976-16983(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/He; TISSUE=Liver;
RX   PubMed=2828632; DOI=10.1016/0022-2836(87)90454-2;
RA   Tsuzuki T., Obaru K., Setoyama C., Shimada K.;
RT   "Structural organization of the mouse mitochondrial aspartate
RT   aminotransferase gene.";
RL   J. Mol. Biol. 198:21-31(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=FVB/NJ; TISSUE=Liver;
RX   PubMed=10642497; DOI=10.1042/bj3450423;
RA   Bradbury M.W., Berk P.D.;
RT   "Mitochondrial aspartate aminotransferase: direction of a single protein
RT   with two distinct functions to two subcellular sites does not require
RT   alternative splicing of the mRNA.";
RL   Biochem. J. 345:423-427(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow macrophage, Cecum, Dendritic cell, and Melanocyte;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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   [6]
RP   PROTEIN SEQUENCE OF 60-81; 91-122; 126-139; 171-180; 186-200; 280-296;
RP   310-345; 356-363 AND 397-404, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7878064; DOI=10.3181/00379727-208-43854;
RA   Zhou S.-L., Stump D., Kiang C.L., Isola L.M., Berk P.D.;
RT   "Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-
RT   L1 adipocytes mediates saturable fatty acid uptake.";
RL   Proc. Soc. Exp. Biol. Med. 208:263-270(1995).
RN   [8]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA   Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA   Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT   disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [9]
RP   CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=17442055; DOI=10.1111/j.1471-4159.2007.04556.x;
RA   Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R.;
RT   "Mitochondrial aspartate aminotransferase: a third kynurenate-producing
RT   enzyme in the mammalian brain.";
RL   J. Neurochem. 102:103-111(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-159 AND LYS-404,
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-107; LYS-122;
RP   LYS-159; LYS-185; LYS-227; LYS-296; LYS-309; LYS-338; LYS-363; LYS-396 AND
RP   LYS-404, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and 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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-73; LYS-82; LYS-90;
RP   LYS-107; LYS-122; LYS-159; LYS-185; LYS-234; LYS-279; LYS-296; LYS-302;
RP   LYS-309; LYS-338; LYS-345; LYS-363; LYS-364; LYS-387; LYS-396 AND LYS-404,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [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).
RN   [13]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-313, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [14]
RP   MUTAGENESIS OF LEU-209 AND ARG-337.
RX   PubMed=31422819; DOI=10.1016/j.ajhg.2019.07.015;
RA   van Karnebeek C.D.M., Ramos R.J., Wen X.Y., Tarailo-Graovac M.,
RA   Gleeson J.G., Skrypnyk C., Brand-Arzamendi K., Karbassi F., Issa M.Y.,
RA   van der Lee R., Droegemoeller B.I., Koster J., Rousseau J., Campeau P.M.,
RA   Wang Y., Cao F., Li M., Ruiter J., Ciapaite J., Kluijtmans L.A.J.,
RA   Willemsen M.A.A.P., Jans J.J., Ross C.J., Wintjes L.T., Rodenburg R.J.,
RA   Huigen M.C.D.G., Jia Z., Waterham H.R., Wasserman W.W., Wanders R.J.A.,
RA   Verhoeven-Duif N.M., Zaki M.S., Wevers R.A.;
RT   "Bi-allelic GOT2 mutations cause a treatable malate-aspartate shuttle-
RT   related encephalopathy.";
RL   Am. J. Hum. Genet. 105:534-548(2019).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 30-430 IN COMPLEX WITH SYNTHETIC
RP   INHIBITOR, AND SUBUNIT.
RX   PubMed=19826765; DOI=10.1007/s00018-009-0166-4;
RA   Han Q., Cai T., Tagle D.A., Li J.;
RT   "Structure, expression, and function of kynurenine aminotransferases in
RT   human and rodent brains.";
RL   Cell. Mol. Life Sci. 67:353-368(2010).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 30-430 IN COMPLEX WITH
RP   L-KYNURENINE; OXALOACETATE AND PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY,
RP   FUNCTION, SUBUNIT, AND COFACTOR.
RX   PubMed=20977429; DOI=10.1042/bsr20100117;
RA   Han Q., Robinson H., Cai T., Tagle D.A., Li J.;
RT   "Biochemical and structural characterization of mouse mitochondrial
RT   aspartate aminotransferase, a newly identified kynurenine aminotransferase-
RT   IV.";
RL   Biosci. Rep. 31:323-332(2011).
CC   -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC       metabolite L-kynurenine to form kynurenic acid (KA). As a member of the
CC       malate-aspartate shuttle, it has a key role in the intracellular NAD(H)
CC       redox balance. Is important for metabolite exchange between
CC       mitochondria and cytosol, and for amino acid metabolism. Facilitates
CC       cellular uptake of long-chain free fatty acids.
CC       {ECO:0000269|PubMed:20977429, ECO:0000269|PubMed:7878064}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P00507};
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:P00507};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:20977429};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19826765,
CC       ECO:0000269|PubMed:20977429}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane
CC       {ECO:0000269|PubMed:7878064}.
CC   -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC       {ECO:0000269|PubMed:17442055}.
CC   -!- PTM: Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver
CC       mitochondria from fasted mice but not from fed mice.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; J02622; AAA37264.1; -; mRNA.
DR   EMBL; X06917; CAA30015.1; -; Genomic_DNA.
DR   EMBL; X06918; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06919; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06920; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06921; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06922; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06923; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06924; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06925; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06926; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; M37259; AAA37265.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M37250; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37251; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37252; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37253; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37254; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37255; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37256; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37258; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; U82470; AAB91426.1; -; mRNA.
DR   EMBL; AK136556; BAE23042.1; -; mRNA.
DR   EMBL; AK147953; BAE28248.1; -; mRNA.
DR   EMBL; AK149886; BAE29146.1; -; mRNA.
DR   EMBL; AK149926; BAE29171.1; -; mRNA.
DR   EMBL; AK150194; BAE29370.1; -; mRNA.
DR   EMBL; AK152921; BAE31596.1; -; mRNA.
DR   EMBL; AK155075; BAE33029.1; -; mRNA.
DR   EMBL; AK167767; BAE39800.1; -; mRNA.
DR   EMBL; BC089015; AAH89015.1; -; mRNA.
DR   EMBL; BC089341; AAH89341.1; -; mRNA.
DR   CCDS; CCDS22568.1; -.
DR   PIR; S01174; S01174.
DR   RefSeq; NP_034455.1; NM_010325.2.
DR   PDB; 3HLM; X-ray; 2.50 A; A/B/C/D=30-430.
DR   PDB; 3PD6; X-ray; 2.40 A; A/B/C/D=30-430.
DR   PDB; 3PDB; X-ray; 2.40 A; A/B/C/D=30-430.
DR   PDBsum; 3HLM; -.
DR   PDBsum; 3PD6; -.
DR   PDBsum; 3PDB; -.
DR   AlphaFoldDB; P05202; -.
DR   SMR; P05202; -.
DR   BioGRID; 200000; 26.
DR   IntAct; P05202; 5.
DR   MINT; P05202; -.
DR   STRING; 10090.ENSMUSP00000034097; -.
DR   ChEMBL; CHEMBL3647; -.
DR   GlyGen; P05202; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P05202; -.
DR   PhosphoSitePlus; P05202; -.
DR   SwissPalm; P05202; -.
DR   CPTAC; non-CPTAC-3628; -.
DR   EPD; P05202; -.
DR   jPOST; P05202; -.
DR   MaxQB; P05202; -.
DR   PaxDb; 10090-ENSMUSP00000034097; -.
DR   PeptideAtlas; P05202; -.
DR   ProteomicsDB; 285701; -.
DR   Pumba; P05202; -.
DR   TopDownProteomics; P05202; -.
DR   Antibodypedia; 15396; 698 antibodies from 40 providers.
DR   DNASU; 14719; -.
DR   Ensembl; ENSMUST00000034097.8; ENSMUSP00000034097.8; ENSMUSG00000031672.9.
DR   GeneID; 14719; -.
DR   KEGG; mmu:14719; -.
DR   UCSC; uc009mzi.1; mouse.
DR   AGR; MGI:95792; -.
DR   CTD; 2806; -.
DR   MGI; MGI:95792; Got2.
DR   VEuPathDB; HostDB:ENSMUSG00000031672; -.
DR   eggNOG; KOG1411; Eukaryota.
DR   GeneTree; ENSGT00950000183082; -.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   InParanoid; P05202; -.
DR   OMA; VGACTIV; -.
DR   OrthoDB; 1123851at2759; -.
DR   PhylomeDB; P05202; -.
DR   TreeFam; TF300641; -.
DR   BRENDA; 2.6.1.7; 3474.
DR   Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-MMU-70263; Gluconeogenesis.
DR   Reactome; R-MMU-8963693; Aspartate and asparagine metabolism.
DR   Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR   BioGRID-ORCS; 14719; 8 hits in 80 CRISPR screens.
DR   ChiTaRS; Got2; mouse.
DR   EvolutionaryTrace; P05202; -.
DR   PRO; PR:P05202; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P05202; Protein.
DR   Bgee; ENSMUSG00000031672; Expressed in hindlimb stylopod muscle and 137 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0030315; C:T-tubule; ISO:MGI.
DR   GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR   GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:MGI.
DR   GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006520; P:amino acid metabolic process; ISO:MGI.
DR   GO; GO:0006532; P:aspartate biosynthetic process; IDA:MGI.
DR   GO; GO:0006533; P:aspartate catabolic process; ISO:MGI.
DR   GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR   GO; GO:0043648; P:dicarboxylic acid metabolic process; ISO:MGI.
DR   GO; GO:0015908; P:fatty acid transport; IEA:Ensembl.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:MGI.
DR   GO; GO:0019550; P:glutamate catabolic process to aspartate; IDA:MGI.
DR   GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IDA:MGI.
DR   GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   Genevisible; P05202; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Aminotransferase; Cell membrane;
KW   Direct protein sequencing; Lipid transport; Membrane; Methylation;
KW   Mitochondrion; Nitration; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide; Transport.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT   CHAIN           30..430
FT                   /note="Aspartate aminotransferase, mitochondrial"
FT                   /id="PRO_0000001216"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT   BINDING         407
FT                   /ligand="substrate"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         59
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753,
FT                   ECO:0007744|PubMed:23806337"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         82
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         90
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         90
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         96
FT                   /note="3'-nitrotyrosine; alternate"
FT                   /evidence="ECO:0007744|PubMed:16800626"
FT   MOD_RES         96
FT                   /note="Phosphotyrosine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         107
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         107
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         122
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         122
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         159
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753,
FT                   ECO:0007744|PubMed:23806337"
FT   MOD_RES         159
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         185
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         185
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         227
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         234
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         296
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         296
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         302
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         309
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         309
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         313
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         338
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         338
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         345
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         363
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         363
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         364
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         387
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         396
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         396
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         404
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753,
FT                   ECO:0007744|PubMed:23806337"
FT   MOD_RES         404
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MUTAGEN         209
FT                   /note="Missing: Heterozygous mice are viable and healthy.
FT                   Results in early lethality at homozygosity."
FT                   /evidence="ECO:0000269|PubMed:31422819"
FT   MUTAGEN         337
FT                   /note="R->G: Heterozygous mice are viable and healthy.
FT                   Results in early lethality at homozygosity."
FT                   /evidence="ECO:0000269|PubMed:31422819"
FT   CONFLICT        68
FT                   /note="R -> G (in Ref. 4; BAE39800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="Q -> E (in Ref. 3; AAB91426)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="R -> G (in Ref. 4; BAE39800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="Q -> K (in Ref. 4; BAE39800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="L -> I (in Ref. 4; BAE39800)"
FT                   /evidence="ECO:0000305"
FT   TURN            32..35
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           43..53
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           78..89
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           119..123
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           133..148
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           165..172
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          175..180
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           191..199
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           223..235
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          239..245
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   TURN            247..251
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           254..257
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           259..266
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   TURN            278..280
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           284..286
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          288..294
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           298..316
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           322..332
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           334..364
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           373..376
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          379..383
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           388..398
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   STRAND          406..409
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:3PD6"
FT   HELIX           418..429
FT                   /evidence="ECO:0007829|PDB:3PD6"
SQ   SEQUENCE   430 AA;  47411 MW;  D590524CA7FFB885 CRC64;
     MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
     NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENNEV
     LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR
     YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA
     FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE
     AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS
     NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY
     LAHAIHQVTK
//