Q8FY59 (AROK_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 65.
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: Shikimate kinase Short name=SK EC=2.7.1.71 | ||||
| Gene names |
| ||||
| 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 | 200 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate By similarity. HAMAP-Rule MF_00109 |
| Catalytic activity | ATP + shikimate = ADP + shikimate 3-phosphate. HAMAP-Rule MF_00109 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Pathway | Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. HAMAP-Rule MF_00109 |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the shikimate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP chorismate biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP shikimate kinase 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 – 200 | 200 | Shikimate kinase HAMAP-Rule MF_00109 | PRO_0000237856 | |||||
Regions | |||||||||
| Nucleotide binding | 33 – 38 | 6 | ATP By similarity | ||||||
Sites | |||||||||
| Metal binding | 37 | 1 | Magnesium By similarity | ||||||
| Binding site | 55 | 1 | Substrate By similarity | ||||||
| Binding site | 79 | 1 | Substrate By similarity | ||||||
| Binding site | 101 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 139 | 1 | ATP By similarity | ||||||
| Binding site | 158 | 1 | Substrate By similarity | ||||||
Sequences
| ||||||||||||||||||
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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014291 Genomic DNA. Translation: AAN30919.1. CP002997 Genomic DNA. Translation: AEM19336.1. |
| RefSeq | NP_699004.1. NC_004310.3. YP_005616828.1. NC_017251.1. |
3D structure databases | |
| ProteinModelPortal | Q8FY59. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 204722.BR2029. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN30919; AAN30919; BR2029. AEM19336; AEM19336; BS1330_I2023. |
| GeneID | 1167731. 12137811. |
| KEGG | bms:BR2029. bsi:BS1330_I2023. |
| PATRIC | 17792485. VBIBruSui107850_2064. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0703. |
| HOGENOM | HOG000032568. |
| KO | K00891. |
| OMA | ADIPWIF. |
| ProtClustDB | PRK13946. |
Enzyme and pathway databases | |
| UniPathway | UPA00053; UER00088. |
Family and domain databases | |
| HAMAP | MF_00109. Shikimate_kinase. |
| InterPro | IPR000623. Shikimate_kinase. [Graphical view] |
| Pfam | PF01202. SKI. 1 hit. [Graphical view] |
| PRINTS | PR01100. SHIKIMTKNASE. |
| PROSITE | PS01128. SHIKIMATE_KINASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AROK_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8FY59 Secondary accession number(s): G0K8P9 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with
