Q8FYE2 (ARGJ_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 59.
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 |
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| Organism | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 413 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 acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate By similarity. HAMAP MF_01106 |
| Catalytic activity | N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP 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 MF_01106 Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01106 |
| Subunit structure | Heterotetramer of two alpha and two beta chains By similarity. |
| Subcellular location | Cytoplasm Probable HAMAP MF_01106. |
| Miscellaneous | Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP MF_01106 |
| Sequence similarities | Belongs to the ArgJ family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Acyltransferase Transferase |
| PTM | Autocatalytic cleavage |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC glutamate N-acetyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 194 | 194 | Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity | PRO_0000002139 | |||||
| Chain | 195 – 413 | 219 | Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity | PRO_0000002140 | |||||
Sites | |||||||||
| Site | 194 – 195 | 2 | Cleavage; by autolysis By similarity | ||||||
Sequences
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References
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014291 Genomic DNA. Translation: AAN30833.1. CP002997 Genomic DNA. Translation: AEM19250.1. |
| RefSeq | NP_698918.1. NC_004310.3. |
3D structure databases | |
| ProteinModelPortal | Q8FYE2. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T05.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1167641. |
| GenomeReviews | Gene locus BR1941 in contig AE014291_GR. |
| KEGG | bms:BR1941. |
| PATRIC | 17792301. VBIBruSui107850_1975. |
| TIGR | BR1941. |
Phylogenomic databases | |
| HOGENOM | HBG284202. |
| OMA | FPKLATR. |
| PhylomeDB | Q8FYE2. |
| ProtClustDB | PRK05388. |
Enzyme and pathway databases | |
| BioCyc | BSUI204722:BR_1941-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01106. ArgJ. [Tree] |
| InterPro | IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view] |
| KO | K00620. |
| PANTHER | PTHR23100. ArgJ. 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_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8FYE2 Secondary accession number(s): G0K884 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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