AATM_MOUSE
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 03-AUG-2022, entry version 196.
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, Pancreas,
RC 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; 23.
DR IntAct; P05202; 5.
DR MINT; P05202; -.
DR STRING; 10090.ENSMUSP00000034097; -.
DR ChEMBL; CHEMBL3647; -.
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; P05202; -.
DR PeptideAtlas; P05202; -.
DR PRIDE; P05202; -.
DR ProteomicsDB; 285701; -.
DR TopDownProteomics; P05202; -.
DR Antibodypedia; 15396; 646 antibodies from 40 providers.
DR DNASU; 14719; -.
DR Ensembl; ENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672.
DR GeneID; 14719; -.
DR KEGG; mmu:14719; -.
DR UCSC; uc009mzi.1; mouse.
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; 1104596at2759; -.
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 75 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 134 other tissues.
DR Genevisible; P05202; MM.
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; IEA:UniProtKB-SubCell.
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: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:0006520; P:cellular amino acid metabolic process; ISO:MGI.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
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
