P08495 · AK2_BACSU
- ProteinAspartokinase 2
- GenelysC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids408 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 threonine, isoleucine and methionine.
Catalytic activity
- ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Activity regulation
Lysine-sensitive. Regulated by degradation in response to starvation of cells for various nutrients. Ammonium starvation induced the fastest aspartokinase II decline, followed by amino acid starvation and glucose limitation.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
6.5 mM | ATP | |||||
10 mM | aspartate |
kcat is 952 min-1.
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 7 | Contribution to the catalysis | ||||
Sequence: K | ||||||
Binding site | 7-10 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KFGG | ||||||
Binding site | 25-30 | substrate | ||||
Sequence: RAIAEK | ||||||
Binding site | 41 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 47-49 | substrate | ||||
Sequence: TDE | ||||||
Binding site | 74 | substrate | ||||
Sequence: E | ||||||
Site | 74 | Contribution to the catalysis | ||||
Sequence: E | ||||||
Binding site | 125-126 | substrate | ||||
Sequence: LE | ||||||
Binding site | 150-153 | substrate | ||||
Sequence: RGGS | ||||||
Binding site | 153 | substrate | ||||
Sequence: S | ||||||
Binding site | 173-174 | ATP (UniProtKB | ChEBI) | ||||
Sequence: TD | ||||||
Binding site | 179-184 | ATP (UniProtKB | ChEBI) | ||||
Sequence: FTTDPR | ||||||
Binding site | 289-291 | substrate | ||||
Sequence: NVD | ||||||
Binding site | 295 | substrate | ||||
Sequence: Q | ||||||
Binding site | 354-355 | substrate | ||||
Sequence: VA | ||||||
Binding site | 368-369 | substrate | ||||
Sequence: LI | ||||||
Binding site | 375-376 | substrate | ||||
Sequence: SE |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aspartate kinase activity | |
Molecular Function | ATP binding | |
Biological Process | diaminopimelate biosynthetic process | |
Biological Process | homoserine biosynthetic process | |
Biological Process | lysine biosynthetic process via diaminopimelate | |
Biological Process | threonine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartokinase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP08495
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000002373 | 1-408 | Aspartokinase 2 | |||
Sequence: MGLIVQKFGGTSVGSVEKIQNAANRAIAEKQKGHQVVVVVSAMGKSTDELVSLAKAISDQPSKREMDMLLATGEQVTISLLSMALQEKGYDAVSYTGWQAGIRTEAIHGNARITDIDTSVLADQLEKGKIVIVAGFQGMTEDCEITTLGRGGSDTTAVALAAALKADKCDIYTDVPGVFTTDPRYVKSARKLEGISYDEMLELANLGAGVLHPRAVEFAKNYQVPLEVRSSTETEAGTLIEEESSMEQNLIVRGIAFEDQITRVTIYGLTSGLTTLSTIFTTLAKRNINVDIIIQTQAEDKTGISFSVKTEDADQTVAVLEEYKDALEFEKIETESKLAKVSIVGSGMVSNPGVAAEMFAVLAQKNILIKMVSTSEIKVSTVVSENDMVKAVESLHDAFELSKHPSAV |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 264-337 | ACT 1 | ||||
Sequence: VTIYGLTSGLTTLSTIFTTLAKRNINVDIIIQTQAEDKTGISFSVKTEDADQTVAVLEEYKDALEFEKIETESK | ||||||
Domain | 343-408 | ACT 2 | ||||
Sequence: IVGSGMVSNPGVAAEMFAVLAQKNILIKMVSTSEIKVSTVVSENDMVKAVESLHDAFELSKHPSAV |
Sequence similarities
Belongs to the aspartokinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
P08495-1
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.
- NameAlpha
- SynonymsAspartokinase 2 subunit alpha
- Length408
- Mass (Da)43,808
- Last updated2003-08-04 v2
- Checksum2E7189F938F97120
P08495-2
- NameBeta
- SynonymsAspartokinase 2 subunit beta
- Differences from canonical
- 1-245: Missing
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_018655 | 1-245 | in isoform Beta | |||
Sequence: Missing | ||||||
Sequence conflict | 166 | in Ref. 1; AAA87318 | ||||
Sequence: A → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J03294 EMBL· GenBank· DDBJ | AAA87318.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J03294 EMBL· GenBank· DDBJ | AAA87319.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z75208 EMBL· GenBank· DDBJ | CAA99580.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z75208 EMBL· GenBank· DDBJ | CAA99581.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB14807.1 EMBL· GenBank· DDBJ | Genomic DNA |