A0A1X6PF32 · A0A1X6PF32_PORUM
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids223 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
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 binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 29 | substrate | ||||
Sequence: T | ||||||
Binding site | 55 | substrate | ||||
Sequence: K | ||||||
Site | 65-66 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 66 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 66 | substrate | ||||
Sequence: T | ||||||
Binding site | 153 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
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
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 > Rhodophyta > Bangiophyceae > Bangiales > Bangiaceae > Porphyra
Accessions
- Primary accessionA0A1X6PF32
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023441983 | 1-65 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MGKYVAAVPALVAAASADGGDAAARAILTTDLVEKTAAVRGTVGGRRVTVGGMAKGSGMIHPNMA | ||||||
Chain | PRO_5023441982 | 66-223 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TMLGFVTTDADVAPGVWAALVTAAADASFNAITVDGDTSTNDTLVGLASGAAGNARVTDAASADGVALAAALTAVCVRLAKAIARDGEGATVLVEVGVTGAASDAAARAVARAVAGSSLTKAAVFGRDPNWGRIAAAAGRAGVPFEQGALGVALGGCP |
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
- Length223
- Mass (Da)21,330
- Last updated2017-07-05 v1
- ChecksumCFD12E9A58D38527
Keywords
- Technical term