HAMAP rule MF_01105
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01105 |
| Accession | MF_01105 |
| Dates | 28-FEB-2005 (Created)
05-NOV-2024 (Last updated, Version 31) |
| Name | N_acetyl_glu_synth |
| Scope(s) |
Bacteria Pseudomonadota |
| Template(s) | P0A6C5; [ Recover all ] |
| Triggered by |
HAMAP; MF_01105 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ARGA |
| Protein name | RecName: Full=Amino-acid acetyltransferase; EC=2.3.1.1; AltName: Full=N-acetylglutamate synthase; Short=AGS; Short=NAGS; |
| Gene name | Name=argA; |
Comments
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| CATALYTIC ACTIVITY | Reaction=L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+); Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1; |
| PATHWAY | Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 1/4. |
| case <OC:Enterobacterales> | |
| SUBUNIT | Homohexamer. |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| case not <OC:Enterobacterales> and not <OC:Pseudomonadaceae> and not <OC:Vibrionaceae> | |
| MISCELLANEOUS | In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA fulfills an anaplerotic role. |
| end case | |
| SIMILARITY | Belongs to the acetyltransferase family. ArgA subfamily. |
Keywords
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Gene Ontology
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| GO:0004042; Molecular function:L-glutamate N-acetyltransferase activity |
| GO:0006526; Biological process:L-arginine biosynthetic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF00696; AA_kinase; 1; |
| Pfam | PF00583; Acetyltransf_1; 1; |
| PIRSF | PIRSF000423; ArgA; 1; |
| NCBIfam | TIGR01890; N-Ac-Glu-synth; 1; |
| PROSITE | PS51186; GNAT; 1; |
Features
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Additional information
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| Size range | 432-451 amino acids |
| Related rules |
None |
| Fusion | Nter: MF_00006 (argH) Cter: None |
| Comments | Moritella sp. argA is fusioned in its N-terminal part to argH. The NAT domain is not shown here - it is much smaller than other acetylglutamate synthases. |