B8BVB6 · ARGJ_THAPS
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids488 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Miscellaneous
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
Catalytic activity
- N2-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N2-acetyl-L-ornithine (cyclic): step 1/1.
Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 1/4.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 189 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 190 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 227 | substrate | |||
Binding site | 250 | substrate | |||
Site | 260-261 | Cleavage; by autolysis | |||
Active site | 261 | Nucleophile | |||
Binding site | 261 | substrate | |||
Binding site | 340 | substrate | |||
Binding site | 483 | substrate | |||
Binding site | 488 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | glutamate N-acetyltransferase activity | |
Molecular Function | L-glutamate N-acetyltransferase activity | |
Biological Process | arginine biosynthetic process | |
Biological Process | ornithine biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- Cleaved into 2 chains
Including 2 domains:
- Recommended nameGlutamate N-acetyltransferase
- EC number
- Short namesGAT
- Alternative names
- Recommended nameAmino-acid acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Stramenopiles > Ochrophyta > Bacillariophyta > Coscinodiscophyceae > Thalassiosirophycidae > Thalassiosirales > Thalassiosiraceae > Thalassiosira
Accessions
- Primary accessionB8BVB6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000397998 | 1-260 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_0000397999 | 261-488 | Arginine biosynthesis bifunctional protein ArgJ beta chain | ||
Post-translational modification
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Keywords
- PTM
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length488
- Mass (Da)50,928
- Last updated2009-03-03 v1
- ChecksumAF8197EF2F0D72DA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM000639 EMBL· GenBank· DDBJ | EED95434.1 EMBL· GenBank· DDBJ | Genomic DNA |