| IED ID | IndEnz0002014503 |
| Enzyme Type ID | protease014503 |
| Protein Name |
Aspartate aminotransferase, mitochondrial mAspAT EC 2.6.1.1 EC 2.6.1.7 Fatty acid-binding protein FABP-1 Glutamate oxaloacetate transaminase 2 Kynurenine aminotransferase 4 Kynurenine aminotransferase IV Kynurenine--oxoglutarate transaminase 4 Kynurenine--oxoglutarate transaminase IV Plasma membrane-associated fatty acid-binding protein FABPpm Transaminase A |
| Gene Name | GOT2 |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MALLHSGRVLSGVASAFHPGLAAAASARASSWWAHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRYVTVQTISGTGALRIGANFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLHSYRYYDPKTCGFDFTGALEDISKIPAQSVILLHACAHNPTGVDPRPEQWKEMATLVKKNNLFAFFDMAYQGFASGDGNKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPMYSNPPVNGARIASTILTSPDLRQQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHIVDQIGMFCFTGIKPEQVERLTKEFSIYMTKDGRISVAGVTSGNVGYLAHAIHQVTK |
| Enzyme Length | 430 |
| Uniprot Accession Number | P00506 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 65; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250; BINDING 162; /note=Substrate; /evidence=ECO:0000250; BINDING 215; /note=Substrate; /evidence=ECO:0000250; BINDING 407; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P00507}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000250|UniProtKB:P00507}; |
| DNA Binding | |
| EC Number | 2.6.1.1; 2.6.1.7 |
| Enzyme Function | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids. {ECO:0000250|UniProtKB:P00505}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (4); Chain (1); Modified residue (36); Sequence conflict (4); Transit peptide (1) |
| Keywords | Acetylation;Aminotransferase;Cell membrane;Direct protein sequencing;Lipid transport;Membrane;Methylation;Mitochondrion;Nitration;Phosphoprotein;Pyridoxal phosphate;Reference proteome;Transferase;Transit peptide;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane {ECO:0000250}. |
| Modified Residue | MOD_RES 48; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 59; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 73; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 73; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 82; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 90; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 90; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 96; /note=3'-nitrotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 96; /note=Phosphotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 107; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 107; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 122; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 122; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 159; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 159; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 185; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 185; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 227; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 234; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 279; /note=N6-(pyridoxal phosphate)lysine; alternate; MOD_RES 279; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 296; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 296; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 302; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 309; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 309; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P12344; MOD_RES 313; /note=Asymmetric dimethylarginine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 345; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 363; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 363; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 364; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 387; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 396; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 396; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202; MOD_RES 404; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P00505; MOD_RES 404; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05202 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,436 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21824; RHEA:65560 |
| Cross Reference Brenda |