Q04728 · ARGJ_YEAST
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- GeneARG7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids441 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 + N2-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Activity regulation
Inhibited by ornithine.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
8.4 mM | glutamate | |||||
2.8 mM | N-acetylornithine |
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 | 136 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 137 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 177 | substrate | ||||
Sequence: T | ||||||
Binding site | 204 | substrate | ||||
Sequence: K | ||||||
Site | 214-215 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 215 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 215 | substrate | ||||
Sequence: T | ||||||
Binding site | 301 | substrate | ||||
Sequence: E | ||||||
Binding site | 436 | substrate | ||||
Sequence: N | ||||||
Binding site | 441 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | acetyl-CoA:L-glutamate N-acetyltransferase activity | |
Molecular Function | glutamate N-acetyltransferase activity | |
Molecular Function | methione N-acyltransferase 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
- Alternative names
- 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
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ04728
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 215 | Blocks autocatalytic processing of the precursor protein. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-8 | Mitochondrion | ||||
Sequence: MRISSTLL | ||||||
Chain | PRO_0000002283 | 9-214 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: QRSKQLIDKYALYVPKTGSFPKGFEVGYTASGVKKNGSLDLGVILNTNKSRPSTAAAVFTTNKFKAAPVLTSKKVLETARGKNINAIVVNSGCANSVTGDLGMKDAQVMIDLVNDKIGQKNSTLVMSTGVIGQRLQMDKISTGINKIFGEEKFGSDFNSWLNVAKSICTTDTFPKLVTSRFKLPSGTEYTLTGMAKGAGMICPNMA | ||||||
Chain | PRO_0000002284 | 215-441 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TLLGFIVTDLPIESKALQKMLTFATTRSFNCISVDGDMSTNDTICMLANGAIDTKEINEDSKDFEQVKLQVTEFAQRLAQLVVRDGEGSTKFVTVNVKNALHFEDAKIIAESISNSMLVKTALYGQDANWGRILCAIGYAKLNDLKSLDVNKINVSFIATDNSEPRELKLVANGVPQLEIDETRASEILALNDLEVSVDLGTGDQAAQFWTCDLSHEYVTINGDYRS |
Post-translational modification
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length441
- Mass (Da)47,849
- Last updated1997-11-01 v1
- Checksum7AC03B7A72E3CE46
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U90438 EMBL· GenBank· DDBJ | AAB49897.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z48952 EMBL· GenBank· DDBJ | CAA88787.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49703 EMBL· GenBank· DDBJ | CAA89772.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA09960.1 EMBL· GenBank· DDBJ | Genomic DNA |