ID AATM_HUMAN Reviewed; 430 AA. AC P00505; B4DJA6; E7ERW2; Q53FL3; Q9BWA3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 27-MAR-2024, entry version 233. DE RecName: Full=Aspartate aminotransferase, mitochondrial; DE Short=mAspAT; DE EC=2.6.1.1 {ECO:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819}; 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 {ECO:0000312|HGNC:HGNC:4433}; GN Synonyms=KYAT4 {ECO:0000312|HGNC:HGNC:4433}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-346. RX PubMed=3207426; DOI=10.1016/s0006-291x(88)81017-9; RA Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B., RA Berthelot P., Hanoune J., Barouki R.; RT "Nucleotide sequence and tissue distribution of the human mitochondrial RT aspartate aminotransferase mRNA."; RL Biochem. Biophys. Res. Commun. 157:1309-1315(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-346. RC TISSUE=Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Gastric mucosa; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-428. RC TISSUE=Muscle; 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 30-430, AND VARIANT GLY-346. RX PubMed=4052435; DOI=10.1016/0167-4838(85)90172-4; RA Martini F., Angelaccio S., Barra D., Pascarella S., Maras B., Doonan S., RA Bossa F.; RT "The primary structure of mitochondrial aspartate aminotransferase from RT human heart."; RL Biochim. Biophys. Acta 832:46-51(1985). RN [7] RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION. RX PubMed=9537447; DOI=10.1002/hep.510270423; RA Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.; RT "Ethanol up-regulates fatty acid uptake and plasma membrane expression and RT export of mitochondrial aspartate aminotransferase in HepG2 cells."; RL Hepatology 27:1064-1074(1998). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90; LYS-159; LYS-234; RP LYS-296; LYS-396 AND LYS-404, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-333, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; TYR-96; SER-143 AND RP THR-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-29, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN DEE82, VARIANTS DEE82 LEU-209 RP DEL; GLY-262; GLY-337 AND VAL-366, AND CHARACTERIZATION OF VARIANTS DEE82 RP GLY-262 AND VAL-366. 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 [14] {ECO:0007744|PDB:5AX8} RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 30-430, BIOPHYSICOCHEMICAL RP PROPERTIES, AND CATALYTIC ACTIVITY. RX PubMed=26902786; DOI=10.5582/bst.2015.01150; RA Jiang X., Wang J., Chang H., Zhou Y.; RT "Recombinant expression, purification and crystallographic studies of the RT mature form of human mitochondrial aspartate aminotransferase."; RL Biosci. Trends 10:79-84(2016). 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:31422819, ECO:0000269|PubMed:9537447}. 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:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819}; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.5. {ECO:0000269|PubMed:26902786}; CC Temperature dependence: CC Optimum temperature is 47.5 degrees Celsius. CC {ECO:0000269|PubMed:26902786}; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000269|PubMed:9537447}. Cell membrane CC {ECO:0000269|PubMed:9537447}. Note=Exposure to alcohol promotes CC translocation to the cell membrane. {ECO:0000269|PubMed:9537447}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P00505-1; Sequence=Displayed; CC Name=2; CC IsoId=P00505-2; Sequence=VSP_054848; CC -!- INDUCTION: Up-regulated by long-time exposure to alcohol. CC {ECO:0000269|PubMed:9537447}. CC -!- DISEASE: Developmental and epileptic encephalopathy 82 (DEE82) CC [MIM:618721]: A form of epileptic encephalopathy, a heterogeneous group CC of severe early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. DEE82 is an autosomal recessive metabolic CC encephalopathy characterized by epilepsy from the first year of life, CC global developmental delay, hypotonia and feeding difficulties apparent CC soon after birth, and intellectual and motor disabilities. Other CC features include poor overall growth, progressive microcephaly and CC biochemical abnormalities, including increased serum lactate and CC ammonia. {ECO:0000269|PubMed:31422819}. Note=The disease is caused by CC variants affecting the gene represented in this entry. 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}. 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; M22632; AAA35568.1; -; mRNA. DR EMBL; AK295993; BAG58768.1; -; mRNA. DR EMBL; AK223271; BAD96991.1; -; mRNA. DR EMBL; AC012183; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000525; AAH00525.1; -; mRNA. DR CCDS; CCDS10801.1; -. [P00505-1] DR CCDS; CCDS67045.1; -. [P00505-2] DR PIR; A31873; XNHUDM. DR RefSeq; NP_001273149.1; NM_001286220.1. [P00505-2] DR RefSeq; NP_002071.2; NM_002080.3. [P00505-1] DR PDB; 5AX8; X-ray; 2.99 A; A/B/C/D=30-430. DR PDBsum; 5AX8; -. DR AlphaFoldDB; P00505; -. DR SMR; P00505; -. DR BioGRID; 109068; 99. DR IntAct; P00505; 26. DR MINT; P00505; -. DR STRING; 9606.ENSP00000245206; -. DR BindingDB; P00505; -. DR ChEMBL; CHEMBL4524033; -. DR DrugBank; DB02783; 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate. DR DrugBank; DB00128; Aspartic acid. DR DrugBank; DB00151; Cysteine. DR DrugBank; DB00142; Glutamic acid. DR DrugBank; DB00114; Pyridoxal phosphate. DR DrugCentral; P00505; -. DR TCDB; 9.A.70.1.1; the aspartate amino transferase (aat) family. DR GlyGen; P00505; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P00505; -. DR MetOSite; P00505; -. DR PhosphoSitePlus; P00505; -. DR SwissPalm; P00505; -. DR BioMuta; GOT2; -. DR DMDM; 308153643; -. DR CPTAC; CPTAC-518; -. DR CPTAC; CPTAC-519; -. DR EPD; P00505; -. DR jPOST; P00505; -. DR MassIVE; P00505; -. DR MaxQB; P00505; -. DR PaxDb; 9606-ENSP00000245206; -. DR PeptideAtlas; P00505; -. DR ProteomicsDB; 17864; -. DR ProteomicsDB; 51258; -. [P00505-1] DR Pumba; P00505; -. DR TopDownProteomics; P00505-1; -. [P00505-1] DR Antibodypedia; 15396; 698 antibodies from 40 providers. DR DNASU; 2806; -. DR Ensembl; ENST00000245206.10; ENSP00000245206.5; ENSG00000125166.13. [P00505-1] DR Ensembl; ENST00000434819.2; ENSP00000394100.2; ENSG00000125166.13. [P00505-2] DR GeneID; 2806; -. DR KEGG; hsa:2806; -. DR MANE-Select; ENST00000245206.10; ENSP00000245206.5; NM_002080.4; NP_002071.2. DR UCSC; uc002eof.2; human. [P00505-1] DR AGR; HGNC:4433; -. DR CTD; 2806; -. DR DisGeNET; 2806; -. DR GeneCards; GOT2; -. DR HGNC; HGNC:4433; GOT2. DR HPA; ENSG00000125166; Group enriched (choroid plexus, heart muscle, liver, skeletal muscle, tongue). DR MalaCards; GOT2; -. DR MIM; 138150; gene. DR MIM; 618721; phenotype. DR neXtProt; NX_P00505; -. DR OpenTargets; ENSG00000125166; -. DR PharmGKB; PA28818; -. DR VEuPathDB; HostDB:ENSG00000125166; -. DR eggNOG; KOG1411; Eukaryota. DR GeneTree; ENSGT00950000183082; -. DR HOGENOM; CLU_032440_1_2_1; -. DR InParanoid; P00505; -. DR OMA; VGACTIV; -. DR OrthoDB; 1123851at2759; -. DR PhylomeDB; P00505; -. DR TreeFam; TF300641; -. DR BioCyc; MetaCyc:HS04858-MONOMER; -. DR BRENDA; 2.6.1.1; 2681. DR PathwayCommons; P00505; -. DR Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine. DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation. DR Reactome; R-HSA-70263; Gluconeogenesis. DR Reactome; R-HSA-8963693; Aspartate and asparagine metabolism. DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism. DR SignaLink; P00505; -. DR SIGNOR; P00505; -. DR BioGRID-ORCS; 2806; 155 hits in 1161 CRISPR screens. DR ChiTaRS; GOT2; human. DR GeneWiki; GOT2; -. DR GenomeRNAi; 2806; -. DR Pharos; P00505; Tbio. DR PRO; PR:P00505; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P00505; Protein. DR Bgee; ENSG00000125166; Expressed in hindlimb stylopod muscle and 205 other cell types or tissues. DR ExpressionAtlas; P00505; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB. DR GO; GO:0019470; P:4-hydroxyproline catabolic process; TAS:BHF-UCL. DR GO; GO:0006532; P:aspartate biosynthetic process; IEA:Ensembl. DR GO; GO:0006533; P:aspartate catabolic process; IDA:UniProtKB. DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB. DR GO; GO:0015908; P:fatty acid transport; IEP:UniProtKB. DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl. DR GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl. DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB. 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:SF39; 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 UCD-2DPAGE; P00505; -. DR Genevisible; P00505; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase; KW Cell membrane; Direct protein sequencing; Disease variant; Epilepsy; KW Lipid transport; Membrane; Methylation; Mitochondrion; Nitration; KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase; KW Transit peptide; Transport. FT TRANSIT 1..29 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:4052435, FT ECO:0007744|PubMed:25944712" FT CHAIN 30..430 FT /note="Aspartate aminotransferase, mitochondrial" FT /id="PRO_0000001215" 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 /evidence="ECO:0000250" FT BINDING 407 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 48 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 59 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 73 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 73 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 82 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 90 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 90 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 96 FT /note="3'-nitrotyrosine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 96 FT /note="Phosphotyrosine; alternate" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 107 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 107 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 122 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 122 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 159 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 159 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 185 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 185 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 227 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 234 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" 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:0000250|UniProtKB:P05202" FT MOD_RES 296 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 296 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 302 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 309 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 309 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P12344" FT MOD_RES 313 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 333 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 338 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 338 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 345 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 363 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 363 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 364 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 387 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 396 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 396 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 404 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 404 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT VAR_SEQ 83..125 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054848" FT VARIANT 2 FT /note="A -> S (in dbSNP:rs11558171)" FT /id="VAR_055494" FT VARIANT 188 FT /note="G -> S (in dbSNP:rs11076256)" FT /id="VAR_031710" FT VARIANT 209 FT /note="Missing (in DEE82; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31422819" FT /id="VAR_083488" FT VARIANT 262 FT /note="R -> G (in DEE82; decreased glutamate oxaloacetate FT transferase activity; dbSNP:rs752927520)" FT /evidence="ECO:0000269|PubMed:31422819" FT /id="VAR_083489" FT VARIANT 337 FT /note="R -> G (in DEE82; uncertain significance; FT dbSNP:rs1247507359)" FT /evidence="ECO:0000269|PubMed:31422819" FT /id="VAR_083490" FT VARIANT 346 FT /note="V -> G (in dbSNP:rs30842)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:3207426, ECO:0000269|PubMed:4052435" FT /id="VAR_031711" FT VARIANT 366 FT /note="G -> V (in DEE82; uncertain significance; decreased FT glutamate oxaloacetate transferase activity; FT dbSNP:rs1597696047)" FT /evidence="ECO:0000269|PubMed:31422819" FT /id="VAR_083491" FT VARIANT 428 FT /note="V -> A (in dbSNP:rs17849335)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031712" FT CONFLICT 110..111 FT /note="AE -> EA (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="D -> N (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 258 FT /note="A -> T (in Ref. 3; BAD96991)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="E -> Q (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 43..53 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 78..88 FT /evidence="ECO:0007829|PDB:5AX8" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 103..114 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 119..123 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 126..132 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 133..148 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 153..159 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 165..172 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:5AX8" FT TURN 184..187 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 191..198 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 206..213 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 223..236 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 239..246 FT /evidence="ECO:0007829|PDB:5AX8" FT TURN 247..251 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 254..257 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 259..266 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 272..276 FT /evidence="ECO:0007829|PDB:5AX8" FT TURN 278..280 FT /evidence="ECO:0007829|PDB:5AX8" FT TURN 284..287 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 298..315 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 321..332 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 334..364 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 372..376 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 379..383 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 388..398 FT /evidence="ECO:0007829|PDB:5AX8" FT STRAND 406..409 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 410..412 FT /evidence="ECO:0007829|PDB:5AX8" FT HELIX 415..428 FT /evidence="ECO:0007829|PDB:5AX8" SQ SEQUENCE 430 AA; 47518 MW; F559567ABF2DB346 CRC64; MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP TWGNHTPIFR DAGMQLQGYR YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKVMADR IIGMRTQLVS NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI YMTKDGRISV AGVTSSNVGY LAHAIHQVTK //