P96426 (ARGJ_RHOFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Arginine biosynthesis bifunctional protein ArgJ Cleaved into the following 2 chains: | ||||
| Gene names |
| ||||
| Organism | Rhodococcus fascians | ||||
| Taxonomic identifier | 1828 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus![]() |
Protein attributes
| Sequence length | 403 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate By similarity. HAMAP-Rule MF_01106 |
| Catalytic activity | N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP-Rule MF_01106 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP-Rule MF_01106 |
| Pathway | Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. HAMAP-Rule MF_01106 Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP-Rule MF_01106 |
| Subunit structure | Heterotetramer of two alpha and two beta chains By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP-Rule MF_01106 |
| Sequence similarities | Belongs to the ArgJ family. |
| Sequence caution | The sequence CAC43342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Acyltransferase Transferase |
| PTM | Autocatalytic cleavage |
| Technical term | Multifunctional enzyme |
| 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 | acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP glutamate N-acetyltransferase activityInferred 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 – 193 | 193 | Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity | PRO_0000002227 | |||||
| Chain | 194 – 403 | 210 | Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity | PRO_0000002228 | |||||
Sites | |||||||||
| Active site | 194 | 1 | Nucleophile By similarity | ||||||
| Binding site | 161 | 1 | Substrate By similarity | ||||||
| Binding site | 183 | 1 | Substrate By similarity | ||||||
| Binding site | 194 | 1 | Substrate By similarity | ||||||
| Binding site | 273 | 1 | Substrate By similarity | ||||||
| Binding site | 398 | 1 | Substrate By similarity | ||||||
| Binding site | 403 | 1 | Substrate By similarity | ||||||
| Site | 125 | 1 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity | ||||||
| Site | 126 | 1 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole By similarity | ||||||
| Site | 193 – 194 | 2 | Cleavage; by autolysis By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Leafy gall formation is controlled by fasR, an AraC-type regulatory gene in Rhodococcus fascians." Temmerman W., Vereecke D., Dreesen R., Van Montagu M., Holsters M., Goethals K. J. Bacteriol. 182:5832-5840(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: D188. |
| [2] | "The att locus of Rhodococcus fascians strain D188 is essential for full virulence on tobacco through the production of an autoregulatory compound." Maes T., Vereecke D., Ritsema T., Cornelis K., Thu H.N., Van Montagu M., Holsters M., Goethals K. Mol. Microbiol. 42:13-28(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: D188. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y09820 Genomic DNA. Translation: CAA70949.1. AJ311775 Genomic DNA. Translation: CAC43342.1. Different initiation. |
3D structure databases | |
| ProteinModelPortal | P96426. |
| SMR | P96426. Positions 22-400. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T05.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00068; UER00106. UPA00068; UER00111. |
Family and domain databases | |
| Gene3D | 3.60.70.12. 1 hit. |
| HAMAP | MF_01106. ArgJ. |
| InterPro | IPR002813. Arg_biosynth_ArgJ. IPR016117. ArgJ-like_dom. [Graphical view] |
| PANTHER | PTHR23100. PTHR23100. 1 hit. |
| Pfam | PF01960. ArgJ. 1 hit. [Graphical view] |
| ProDom | PD004193. Arg_biosynth_ArgJ. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SUPFAM | SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit. |
| TIGRFAMs | TIGR00120. ArgJ. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ARGJ_RHOFA | ||||||||
| Accession | Primary (citable) accession number: P96426 Secondary accession number(s): Q93JQ2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
