P61488 (AK_THET2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 64.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Aspartokinase EC=2.7.2.4 Alternative name(s): Aspartate kinase Short name=ASK | ||||||
| Gene names |
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| Organism | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 262724 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › ![]() |
Protein attributes
| Sequence length | 405 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine. Ref.1 |
| Catalytic activity | ATP + L-aspartate = ADP + 4-phospho-L-aspartate. |
| Pathway | Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. |
| Subunit structure | Tetramer consisting of 2 isoforms Alpha (catalytic and regulation) and of a homodimer of 2 isoforms Beta (regulation) By similarity. |
| Disruption phenotype | Cells lacking this gene show auxotrophy for methionine and threonine. Ref.1 |
| Sequence similarities | Belongs to the aspartokinase family. Contains 2 ACT domains. |
| Sequence caution | The sequence AAS80514.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis |
| Coding sequence diversity | Alternative initiation |
| Domain | Repeat |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW lysine biosynthetic process via diaminopimelateInferred from electronic annotation. Source: UniProtKB-UniPathway threonine biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid bindingInferred from electronic annotation. Source: InterPro aspartate kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Alpha (identifier: P61488-1) Also known as: Aspartokinase subunit alpha; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Beta (identifier: P61488-2) Also known as: Aspartokinase subunit beta; The sequence of this isoform differs from the canonical sequence as follows: 1-244: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 405 | 405 | Aspartokinase | PRO_0000002387 | |||||
Regions | |||||||||
| Domain | 262 – 335 | 74 | ACT 1 | ||||||
| Domain | 343 – 404 | 62 | ACT 2 | ||||||
| Region | 7 – 10 | 4 | ATP binding By similarity | ||||||
| Region | 25 – 30 | 6 | Substrate binding By similarity | ||||||
| Region | 47 – 49 | 3 | Substrate binding By similarity | ||||||
| Region | 125 – 126 | 2 | Substrate binding By similarity | ||||||
| Region | 150 – 153 | 4 | Substrate binding By similarity | ||||||
| Region | 173 – 174 | 2 | ATP binding By similarity | ||||||
| Region | 179 – 184 | 6 | ATP binding By similarity | ||||||
| Region | 288 – 290 | 3 | Substrate binding By similarity | ||||||
| Region | 355 – 356 | 2 | Substrate binding By similarity | ||||||
| Region | 369 – 370 | 2 | Substrate binding By similarity | ||||||
| Region | 376 – 377 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 41 | 1 | ATP By similarity | ||||||
| Binding site | 74 | 1 | Substrate By similarity | ||||||
| Binding site | 153 | 1 | Substrate By similarity | ||||||
| Binding site | 209 | 1 | ATP By similarity | ||||||
| Binding site | 270 | 1 | Substrate By similarity | ||||||
| Binding site | 294 | 1 | Substrate By similarity | ||||||
| Site | 7 | 1 | Contribution to the catalysis By similarity | ||||||
| Site | 74 | 1 | Contribution to the catalysis By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 244 | 244 | Missing in isoform Beta. | VSP_018664 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid." Kobashi N., Nishiyama M., Tanokura M. J. Bacteriol. 181:1713-1718(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE. |
| [2] | "The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB27 / ATCC BAA-163 / DSM 7039. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB013131 Genomic DNA. Translation: BAA25848.1. AB013131 Genomic DNA. Translation: BAA25849.1. AE017221 Genomic DNA. Translation: AAS80514.1. Different initiation. |
| RefSeq | YP_004141.1. NC_005835.1. |
3D structure databases | |
| ProteinModelPortal | P61488. |
| SMR | P61488. Positions 249-401. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 262724.TTC0166. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAS80514; AAS80514; TT_C0166. |
| GeneID | 2775578. |
| KEGG | tth:TTC0166. |
| PATRIC | 23950725. VBITheThe54392_0167. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0527. |
| KO | K00928. |
| OMA | SVDMIIQ. |
| ProtClustDB | PRK06635. |
Enzyme and pathway databases | |
| BioCyc | TTHE262724:GCAT-170-MONOMER. |
| UniPathway | UPA00034; UER00015. UPA00050; UER00461. UPA00051; UER00462. |
Family and domain databases | |
| Gene3D | 3.40.1160.10. 1 hit. |
| InterPro | IPR002912. ACT_dom. IPR001048. Asp/Glu/Uridylate_kinase. IPR005260. Asp_kin_monofn. IPR001341. Asp_kinase_dom. IPR018042. Aspartate_kinase_CS. [Graphical view] |
| Pfam | PF00696. AA_kinase. 1 hit. PF01842. ACT. 1 hit. [Graphical view] |
| PIRSF | PIRSF000726. Asp_kin. 1 hit. |
| SUPFAM | SSF53633. Aa_kinase. 1 hit. |
| TIGRFAMs | TIGR00656. asp_kin_monofn. 1 hit. TIGR00657. asp_kinases. 1 hit. |
| PROSITE | PS00324. ASPARTOKINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AK_THET2 | ||||||||
| Accession | Primary (citable) accession number: P61488 Secondary accession number(s): P77991, P97151 | ||||||||
| Entry history |
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| 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
