P00504 · AATC_CHICK
- ProteinAspartate aminotransferase, cytoplasmic
- GeneGOT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids412 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H2S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain.
Miscellaneous
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Catalytic activity
- 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetateThis reaction proceeds in the forward direction.
- (2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L-glutamateThis reaction proceeds in the backward direction.
- 2-oxoglutarate + 3-sulfino-L-alanine = 3-sulfinopyruvate + L-glutamateThis reaction proceeds in the backward direction.
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | L-aspartate:2-oxoglutarate aminotransferase activity | |
Molecular Function | L-cysteine transaminase activity | |
Molecular Function | phosphatidylserine decarboxylase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | 2-oxoglutarate metabolic process | |
Biological Process | aspartate biosynthetic process | |
Biological Process | aspartate catabolic process | |
Biological Process | aspartate metabolic process | |
Biological Process | cellular response to insulin stimulus | |
Biological Process | fatty acid homeostasis | |
Biological Process | gluconeogenesis | |
Biological Process | glutamate catabolic process to 2-oxoglutarate | |
Biological Process | glutamate catabolic process to aspartate | |
Biological Process | glutamate metabolic process | |
Biological Process | glycerol biosynthetic process | |
Biological Process | Notch signaling pathway | |
Biological Process | oxaloacetate metabolic process | |
Biological Process | response to glucocorticoid |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate aminotransferase, cytoplasmic
- EC number
- Short namescAspAT
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionP00504
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000123884 | 2-412 | Aspartate aminotransferase, cytoplasmic | |||
Sequence: AASIFAAVPRAPPVAVFKLTADFREDGDSRKVNLGVGAYRTDEGQPWVLPVVRKVEQLIAGDGSLNHEYLPILGLPEFRANASRIALGDDSPAIAQKRVGSVQGLGGTGALRIGAEFLRRWYNGNNNTATPVYVSSPTWENHNSVFMDAGFKDIRTYRYWDAAKRGLDLQGLLDDMEKAPEFSIFILHACAHNPTGTDPTPDEWKQIAAVMKRRCLFPFFDSAYQGFASGSLDKDAWAVRYFVSEGFELFCAQSFSKNFGLYNERVGNLSVVGKDEDNVQRVLSQMEKIVRTTWSNPPSQGARIVATTLTSPQLFAEWKDNVKTMADRVLLMRSELRSRLESLGTPGTWNHITDQIGMFSFTGLNPKQVEYMIKEKHIYLMASGRINMCGLTTKNLDYVAKSIHEAVTKIQ | ||||||
Modified residue | 258 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length412
- Mass (Da)45,935
- Last updated2007-01-23 v3
- ChecksumC55BEE72669078E1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 63 | in Ref. 2; AA sequence and 3; AA sequence | ||||
Sequence: D → N | ||||||
Sequence conflict | 121 | in Ref. 2; AA sequence and 3; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 140 | in Ref. 3; AA sequence | ||||
Sequence: W → S | ||||||
Sequence conflict | 175 | in Ref. 2; AA sequence and 3; AA sequence | ||||
Sequence: D → S | ||||||
Sequence conflict | 232-234 | in Ref. 2; AA sequence and 3; AA sequence | ||||
Sequence: SLD → NLE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15636 EMBL· GenBank· DDBJ | CAA33646.1 EMBL· GenBank· DDBJ | mRNA |