P00504 · AATC_CHICK

  • Protein
    Aspartate aminotransferase, cytoplasmic
  • Gene
    GOT1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site38L-aspartate (UniProtKB | ChEBI)
Binding site140L-aspartate (UniProtKB | ChEBI)
Binding site194L-aspartate (UniProtKB | ChEBI)
Binding site386L-aspartate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionL-aspartate:2-oxoglutarate aminotransferase activity
Molecular FunctionL-cysteine transaminase activity
Molecular Functionphosphatidylserine decarboxylase activity
Molecular Functionpyridoxal phosphate binding
Biological Process2-oxoglutarate metabolic process
Biological Processaspartate biosynthetic process
Biological Processaspartate catabolic process
Biological Processaspartate metabolic process
Biological Processcellular response to insulin stimulus
Biological Processfatty acid homeostasis
Biological Processgluconeogenesis
Biological Processglutamate catabolic process to 2-oxoglutarate
Biological Processglutamate catabolic process to aspartate
Biological Processglutamate metabolic process
Biological Processglycerol biosynthetic process
Biological ProcessNotch signaling pathway
Biological Processoxaloacetate metabolic process
Biological Processresponse to glucocorticoid

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate aminotransferase, cytoplasmic
  • EC number
  • Short names
    cAspAT
  • Alternative names
    • Cysteine aminotransferase, cytoplasmic
    • Cysteine transaminase, cytoplasmic (cCAT)
    • Glutamate oxaloacetate transaminase 1
    • Transaminase A

Gene names

    • Name
      GOT1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus

Accessions

  • Primary accession
    P00504

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001238842-412Aspartate aminotransferase, cytoplasmic
Modified residue258N6-(pyridoxal phosphate)lysine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    412
  • Mass (Da)
    45,935
  • Last updated
    2007-01-23 v3
  • Checksum
    C55BEE72669078E1
MAASIFAAVPRAPPVAVFKLTADFREDGDSRKVNLGVGAYRTDEGQPWVLPVVRKVEQLIAGDGSLNHEYLPILGLPEFRANASRIALGDDSPAIAQKRVGSVQGLGGTGALRIGAEFLRRWYNGNNNTATPVYVSSPTWENHNSVFMDAGFKDIRTYRYWDAAKRGLDLQGLLDDMEKAPEFSIFILHACAHNPTGTDPTPDEWKQIAAVMKRRCLFPFFDSAYQGFASGSLDKDAWAVRYFVSEGFELFCAQSFSKNFGLYNERVGNLSVVGKDEDNVQRVLSQMEKIVRTTWSNPPSQGARIVATTLTSPQLFAEWKDNVKTMADRVLLMRSELRSRLESLGTPGTWNHITDQIGMFSFTGLNPKQVEYMIKEKHIYLMASGRINMCGLTTKNLDYVAKSIHEAVTKIQ

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict63in Ref. 2; AA sequence and 3; AA sequence
Sequence conflict121in Ref. 2; AA sequence and 3; AA sequence
Sequence conflict140in Ref. 3; AA sequence
Sequence conflict175in Ref. 2; AA sequence and 3; AA sequence
Sequence conflict232-234in Ref. 2; AA sequence and 3; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X15636
EMBL· GenBank· DDBJ
CAA33646.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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