AATM_RAT
ID AATM_RAT Reviewed; 430 AA.
AC P00507; Q64551; Q9QV50;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Aspartate aminotransferase, mitochondrial;
DE Short=mAspAT;
DE EC=2.6.1.1 {ECO:0000269|PubMed:17442055};
DE EC=2.6.1.7 {ECO:0000269|PubMed:17442055};
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=Maat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3322287; DOI=10.1016/0006-291x(87)90487-6;
RA Mattingly J.R. Jr., Rodriguez-Berrocal F.J., Gordon J., Iriarte A.,
RA Martinez-Carrion M.;
RT "Molecular cloning and in vivo expression of a precursor to rat
RT mitochondrial aspartate aminotransferase.";
RL Biochem. Biophys. Res. Commun. 149:859-865(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7759512; DOI=10.1074/jbc.270.21.12629;
RA Juang H.H., Costello L.C., Franklin R.B.;
RT "Androgen modulation of multiple transcription start sites of the
RT mitochondrial aspartate aminotransferase gene in rat prostate.";
RL J. Biol. Chem. 270:12629-12634(1995).
RN [4]
RP PROTEIN SEQUENCE OF 30-430.
RC TISSUE=Liver;
RX PubMed=7470110; DOI=10.1016/0006-291x(80)90287-9;
RA Huynh Q.K., Sakakibara R., Watanabe T., Wada H.;
RT "Primary structure of mitochondrial glutamic oxaloacetic transaminase from
RT rat liver: comparison with that of the pig heart isozyme.";
RL Biochem. Biophys. Res. Commun. 97:474-479(1980).
RN [5]
RP PROTEIN SEQUENCE OF 30-430.
RC TISSUE=Liver;
RX PubMed=7309704; DOI=10.1093/oxfordjournals.jbchem.a133543;
RA Huynh Q.K., Sakakibara R., Watanabe T., Wada H.;
RT "The complete amino acid sequence of mitochondrial glutamic oxaloacetic
RT transaminase from rat liver.";
RL J. Biochem. 90:863-875(1981).
RN [6]
RP PROTEIN SEQUENCE OF 30-64.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8238519; DOI=10.1152/ajpgi.1993.265.5.g894;
RA Stump D.D., Zhou S.-L., Berk P.D.;
RT "Comparison of plasma membrane FABP and mitochondrial isoform of aspartate
RT aminotransferase from rat liver.";
RL Am. J. Physiol. 265:G894-G902(1993).
RN [7]
RP PROTEIN SEQUENCE OF 30-42, CATALYTIC ACTIVITY, AND FUNCTION.
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 [8]
RP PROTEIN SEQUENCE OF 60-68; 91-122; 126-147; 171-180; 186-200; 280-296;
RP 310-337; 356-363 AND 397-404, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 279-329.
RX PubMed=3004464; DOI=10.1016/s0006-291x(86)80492-2;
RA Horio Y., Sakakibara R., Tanaka T., Taketoshi M., Obaru K., Shimada K.,
RA Morino Y., Wada H.;
RT "Molecular cloning of rat mitochondrial glutamic oxaloacetic transaminase
RT mRNA and regulation of its expression in regenerating liver.";
RL Biochem. Biophys. Res. Commun. 134:803-811(1986).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11962739; DOI=10.14670/hh-17.353;
RA Cechetto J.D., Sadacharan S.K., Berk P.D., Gupta R.S.;
RT "Immunogold localization of mitochondrial aspartate aminotransferase in
RT mitochondria and on the cell surface in normal rat tissues.";
RL Histol. Histopathol. 17:353-364(2002).
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 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:17442055}.
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:17442055};
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:0000269|PubMed:17442055};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11962739}. Cell membrane
CC {ECO:0000269|PubMed:11962739}. Note=Located in the mitochondria of
CC liver, pancreas, spleen, heart, pituitary gland and submandibular gland
CC cells. In kidney, located in the mitochondria, on the cell surface of
CC regions with protrusions in distal tubules, on the apical cell surface
CC of protrusions along the microvilli in cortical collecting ducts, in
CC condensing vacuoles, on the cell surface at cell boundaries of
CC adjoining kidney cells and on the cell surface of endothelial cells
CC lining capillaries in the glomerulus. Also located at the cell surface
CC of endothelial cells lining arterioles and on the cell surface of
CC lymphocytes.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested: liver, pancreas,
CC kidney, heart, spleen, arterioles, and lymphocytes.
CC {ECO:0000269|PubMed:11962739}.
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; M18467; AAB54275.1; -; mRNA.
DR EMBL; BC061792; AAH61792.1; -; mRNA.
DR EMBL; U21158; AAC13868.1; -; Genomic_DNA.
DR EMBL; M12709; AAA41267.1; -; mRNA.
DR PIR; A28005; XNRTDM.
DR PIR; I55427; I55427.
DR RefSeq; NP_037309.1; NM_013177.2.
DR AlphaFoldDB; P00507; -.
DR SMR; P00507; -.
DR BioGRID; 247750; 3.
DR IntAct; P00507; 5.
DR MINT; P00507; -.
DR STRING; 10116.ENSRNOP00000015956; -.
DR ChEMBL; CHEMBL2351; -.
DR CarbonylDB; P00507; -.
DR iPTMnet; P00507; -.
DR PhosphoSitePlus; P00507; -.
DR jPOST; P00507; -.
DR PaxDb; P00507; -.
DR PRIDE; P00507; -.
DR GeneID; 25721; -.
DR KEGG; rno:25721; -.
DR UCSC; RGD:2722; rat.
DR CTD; 2806; -.
DR RGD; 2722; Got2.
DR VEuPathDB; HostDB:ENSRNOG00000011782; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P00507; -.
DR OMA; VGACTIV; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P00507; -.
DR TreeFam; TF300641; -.
DR BioCyc; MetaCyc:MON-15069; -.
DR BRENDA; 2.6.1.1; 5301.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR Reactome; R-RNO-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; P00507; -.
DR PRO; PR:P00507; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000011782; Expressed in heart and 19 other tissues.
DR Genevisible; P00507; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR GO; GO:0031406; F:carboxylic acid binding; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IMP:RGD.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:RGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006532; P:aspartate biosynthetic process; ISO:RGD.
DR GO; GO:0006533; P:aspartate catabolic process; ISO:RGD.
DR GO; GO:0006531; P:aspartate metabolic process; IMP:RGD.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:RGD.
DR GO; GO:0043648; P:dicarboxylic acid metabolic process; IDA:RGD.
DR GO; GO:0015908; P:fatty acid transport; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:RGD.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; ISO:RGD.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
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 Acetylation; Aminotransferase; Cell membrane; Direct protein sequencing;
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:17442055,
FT ECO:0000269|PubMed:7309704, ECO:0000269|PubMed:7470110,
FT ECO:0000269|PubMed:8238519"
FT CHAIN 30..430
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000001218"
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:0000250|UniProtKB:P00505"
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:0000250|UniProtKB:P00505"
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:0000250|UniProtKB:P00505"
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:0000250|UniProtKB:P00505"
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:0000250|UniProtKB:P00505"
FT MOD_RES 159
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
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:0000250|UniProtKB:P00505"
FT MOD_RES 279
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
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:0000250|UniProtKB:P00505"
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 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:0000250|UniProtKB:P00505"
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:0000250|UniProtKB:P00505"
FT MOD_RES 404
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT CONFLICT 30
FT /note="S -> R (in Ref. 3; AAC13868)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="W -> G (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..169
FT /note="PIF -> EIA (in Ref. 4; AA sequence and 5; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Q -> E (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="V -> Y (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="D -> N (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..339
FT /note="KQ -> QG (in Ref. 4; AA sequence and 5; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="I -> G (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="L -> I (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="V -> I (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47314 MW; EDC8B862A20DB736 CRC64;
MALLHSGRVL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
NLGVGAYRDD NGKPYVLPSV RKAEAQIAGK NLDKEYLPIG GLADFCKASA ELALGENSEV
LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR
YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEMA AVVKKKNLFA
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE
AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS
NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY
LAHAIHQVTK
