ID AATM_HORSE Reviewed; 401 AA. AC P08907; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 02-SEP-2026, entry version 146. 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; GN Name=GOT2; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP PROTEIN SEQUENCE. RX PubMed=3104605; DOI=10.1007/bf02100642; RA Doonan S., Martini F., Angelaccio S., Pascarella S., Barra D., Bossa F.; RT "The complete amino acid sequences of cytosolic and mitochondrial aspartate RT aminotransferases from horse heart, and inferences on evolution of the RT isoenzymes."; RL J. Mol. Evol. 23:328-335(1986). RN [2] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=6641173; DOI=10.1016/0305-0491(83)90280-8; RA Martini F., Angelaccio S., Barra D., Doonan S., Bossa F.; RT "Primary structure of aspartate aminotransferase from horse heart and RT comparison with that of other homotopic and heterotopic isoenzymes."; RL Comp. Biochem. Physiol. 76B:483-487(1983). 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:0000250|UniProtKB:P00505}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; 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=L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate + CC H2O; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, 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 -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane CC {ECO:0000250}. 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 PIR; B26341; B26341. DR AlphaFoldDB; P08907; -. DR SMR; P08907; -. DR STRING; 9796.ENSECAP00000014550; -. DR PaxDb; 9796-ENSECAP00000014550; -. DR PeptideAtlas; P08907; -. DR InParanoid; P08907; -. DR Proteomes; UP000002281; Unplaced. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate transaminase activity; ISS:UniProtKB. DR GO; GO:0016212; F:L-kynurenine:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB. DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB. DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB. DR GO; GO:0006533; P:L-aspartate catabolic process; IBA:GO_Central. DR CDD; cd00609; AAT_like; 1. DR FunFam; 3.40.640.10:FF:000026; Aspartate aminotransferase; 1. DR FunFam; 3.90.1150.10:FF:000001; Aspartate aminotransferase; 1. DR FunFam; 3.90.1150.10:FF:000160; Similar to aspartate aminotransferase; 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_large. 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 NCBIfam; NF006719; PRK09257.1; 1. 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. 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 Transport. FT CHAIN 1..401 FT /note="Aspartate aminotransferase, mitochondrial" FT /id="PRO_0000123885" FT BINDING 36 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 133 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 378 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 19 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 30 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 44 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 44 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 53 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 61 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 61 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 67 FT /note="3'-nitrotyrosine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 67 FT /note="Phosphotyrosine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 78 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 78 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 93 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 93 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 130 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 130 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 156 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 156 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 198 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 205 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 250 FT /note="N6-(pyridoxal phosphate)lysine; alternate" FT MOD_RES 250 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 267 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 267 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 273 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 280 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 280 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P12344" FT MOD_RES 284 FT /note="Asymmetric dimethylarginine" 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:P05202" FT MOD_RES 316 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 334 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 334 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 335 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 358 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 367 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 367 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" FT MOD_RES 375 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00505" FT MOD_RES 375 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05202" SQ SEQUENCE 401 AA; 44567 MW; 8562D82170A40487 CRC64; SSWWAHVEMG PPDPILGVTE AYKRDTNSKK MNLGVGAYRD DNGKPYVLPS VRKAEAQIAA KNLDKEYLPI GGLAEFCKAS AELALGENSE ALKSGRYVTV QSISGTGALR IGANFLQRFF KFSRDVFLPK PSWGNHTPIF RDAGLQLHAY RYYDPKTCGF DVTGALEDIS KIPQQSIILL HACAHNPTGV DPRPEQWKEI ATLVKKNNLF AFFDMAYQGF ASGDGNKDAW AVRYFIEQGI NVCLCQSYAK NMGLYGERVG AFTMVCKDAD EAKRVESQLK ILIRPLYSNP PLNGARIAST ILTSPDLRKQ WLQEVKGMAD RIISMRTQLV SNLKKEGSSH SWQHIADQIG MFCFTGLKPE QVERLTKEFS IYMTKDGRIS VAGVTSGNVG YLAHAIHQVT K //