A0AA35SMB1 · A0AA35SMB1_GEOBA
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids307 (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.
Catalytic activity
- L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H+
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 | 21 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Site | 22 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | |||
Binding site | 56 | substrate | |||
Binding site | 82 | substrate | |||
Site | 92-93 | Cleavage; by autolysis | |||
Active site | 93 | Nucleophile | |||
Binding site | 93 | substrate | |||
Binding site | 179 | substrate | |||
Binding site | 302 | substrate | |||
Binding site | 307 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | glutamate N-acetyltransferase activity | |
Molecular Function | L-glutamate N-acetyltransferase activity | |
Biological Process | L-arginine biosynthetic process | |
Biological Process | ornithine biosynthetic process |
Keywords
- Molecular function
- Biological process
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
- Taxonomic lineageEukaryota > Metazoa > Porifera > Demospongiae > Heteroscleromorpha > Tetractinellida > Astrophorina > Geodiidae > Geodia
Accessions
- Primary accessionA0AA35SMB1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5041495703 | 1-92 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | ||
Chain | PRO_5041495704 | 93-307 | 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
Interaction
Subunit
Heterodimer of an alpha and a beta chain.
Structure
Sequence
- Sequence statusComplete
- Length307
- Mass (Da)32,265
- Last updated2024-01-24 v1
- MD5 Checksum89E2DFE2CCFF7887C09D66B1B65BA8CB
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AA35SLD4 | A0AA35SLD4_GEOBA | GBAR_LOCUS17736 | 397 | ||
A0AA35SKQ5 | A0AA35SKQ5_GEOBA | GBAR_LOCUS17736 | 368 | ||
A0AA35SJH3 | A0AA35SJH3_GEOBA | GBAR_LOCUS17736 | 375 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CASHTH010002526 EMBL· GenBank· DDBJ | CAI8031236.1 EMBL· GenBank· DDBJ | Genomic DNA |