Q2U7R8 · ARGJ_ASPOR
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids456 (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 | 145 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 146 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 184 | substrate | ||||
Sequence: T | ||||||
Binding site | 213 | substrate | ||||
Sequence: K | ||||||
Site | 223-224 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 224 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 224 | substrate | ||||
Sequence: T | ||||||
Binding site | 311 | substrate | ||||
Sequence: E | ||||||
Binding site | 451 | substrate | ||||
Sequence: N | ||||||
Binding site | 456 | substrate | ||||
Sequence: T |
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
Protein family/group 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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionQ2U7R8
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000398022 | 1-223 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MAAFARMVKGQVRSYSAPVDMAIPASKRKFIPSSGSYPKGFVVSGTHVGVKASNTKFPDLALISSETPCSAAAVFTTNKFQAAPVQVSRDIIKTRQGQGIRSVVINSGCANAVTGKGGLEDAVSMGKKVDECDGLNEPSTLVMSTGVIGQRLPISKILKKVPVAHANLSSTHDAWLTTARAICTTDTFPKLLSRTFTLPSSPGRTYSLAGMTKGAGMIHPNMA | ||||||
Chain | PRO_0000398023 | 224-456 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TLLGVLCTDAPIEPSALQSLLKHSVNRSFNSISVDGDTSTNDTIAILANGAAGGAPISSSSSDDYAAMQDILTSFAQSLSQLVVRDGEGATKFVTVRVQNSPDYESGRLIASTIARSPLVKTALYGKDANWGRILCAIGYTQGVAPGTVVPEHTSVSFKPVDGSPVLNLLVNGEPEQVDEERASVILQEEDLEIVVDLGGGEKGEQGLGGEEAVYWFCDFSHEYVTINGDYRT |
Post-translational modification
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length456
- Mass (Da)47,996
- Last updated2006-01-24 v1
- Checksum15F1B26AEC6077F4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000053 EMBL· GenBank· DDBJ | BAE62397.1 EMBL· GenBank· DDBJ | Genomic DNA |