Reviewed,
UniProtKB/Swiss-Prot Q9JW21 (ARGA_NEIMA)
Last modified
November 3, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Amino-acid acetyltransferase EC=2.3.1.1 Alternative name(s): N-acetylglutamate synthase Short name=AGS Short name=NAGS | ||||
| Gene names |
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| Organism | Neisseria meningitidis serogroup A [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 65699 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 436 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01105 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01105 |
| Subcellular location | Cytoplasm Probable. |
| Miscellaneous | In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (argJ), argA fulfills an anaplerotic role. HAMAP MF_01105 |
| Sequence similarities | Belongs to the acetyltransferase family. ArgA subfamily. Contains 1 N-acetyltransferase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | amino-acid N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 436 | 436 | Amino-acid acetyltransferase HAMAP MF_01105 | PRO_0000186794 | ||||
Regions | ||||||||
| Domain | 287 – 436 | 150 | N-acetyltransferase | |||||
Sequences
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References
| [1] | "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491." Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S. Barrell B.G.Nature 404:502-506(2000) [PubMed: 10761919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Z2491 / Serogroup A / Serotype 4A. |
Cross-references
Sequence databases | |
|---|---|
| AL157959 Genomic DNA. Translation: CAM07850.1. | |
| PIR | A81977. |
| RefSeq | YP_002342056.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 906573. |
| GenomeReviews | Gene locus NMA0580 in contig AL157959_GR. |
| KEGG | nma:NMA0580. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9JW21. |
| OMA | DLIRPLE. |
Enzyme and pathway databases | |
| BioCyc | NMEN122587:NMA0580-MON. |
| BRENDA | 2.3.1.1. 292829. |
Family and domain databases | |
| HAMAP | MF_01105. [Tree] |
| InterPro | IPR016181. Acyl_CoA_acyltransferase. IPR001048. Asp/Glu/Uridylate_kinase. IPR000182. GCN5-rel_AcTrfase. IPR010167. NH2A_AcTrfase_ArgA. [Graphical view] |
| Gene3D | G3DSA:3.40.1160.10. Aa_kinase. 1 hit. G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. |
| Pfam | PF00696. AA_kinase. 1 hit. PF00583. Acetyltransf_1. 1 hit. [Graphical view] |
| PIRSF | PIRSF000423. ArgA. 1 hit. |
| TIGRFAMs | TIGR01890. N-Ac-Glu-synth. 1 hit. |
| PROSITE | PS51186. GNAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGA_NEIMA | ||||||||
| Accession | Primary (citable) accession number: Q9JW21 Secondary accession number(s): A1IQ24 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


