A7GSF3 (A7GSF3_BACCN) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 38.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Arginine biosynthesis bifunctional protein ArgJ HAMAP MF_01106 | ||||
| Gene names |
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| Organism | Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP] EMBL ABS23061.1 | ||||
| Taxonomic identifier | 315749 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 407 AA. |
| Sequence status | Complete. |
| 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 | Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106 N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + 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. HAMAP MF_01106 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01106. |
| Miscellaneous | Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway By similarity. HAMAP MF_01106 |
| Sequence similarities | Belongs to the ArgJ family. HAMAP MF_01106 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis HAMAP MF_01106 |
| Cellular component | Cytoplasm HAMAP MF_01106 |
| Molecular function | Acyltransferase HAMAP MF_01106 EMBL ABS23061.1 Transferase |
| PTM | Autocatalytic cleavage HAMAP MF_01106 |
| Technical term | Complete proteome Multifunctional enzyme HAMAP MF_01106 |
| 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Site | 193 – 194 | 2 | Cleavage; by autolysis By similarity HAMAP MF_01106 | ||||||
Sequences
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References
| [1] | "Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000764 Genomic DNA. Translation: ABS23061.1. |
| RefSeq | YP_001376056.1. NC_009674.1. |
3D structure databases | |
| ProteinModelPortal | A7GSF3. |
| SMR | A7GSF3. Positions 5-405. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7GSF3. |
Protein family/group databases | |
| MEROPS | T05.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000039062; EBBACP00000038113; EBBACG00000039053. |
| GeneID | 5343639. |
| GenomeReviews | Gene locus Bcer98_2828 in contig CP000764_GR. |
| KEGG | bcy:Bcer98_2828. |
| PATRIC | 18934270. VBIBacCyt128034_2979. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1364. |
| GeneTree | EBGT00050000002382. |
| HOGENOM | HBG284202. |
| OMA | GRDPNWG. |
| ProtClustDB | PRK05388. |
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 | A7GSF3_BACCN | ||||||||
| Accession | Primary (citable) accession number: A7GSF3 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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