P52991
Gene name |
thrB |
Protein name |
Homoserine kinase |
Names |
HK, HSK |
Species |
Lactococcus lactis subsp cremoris (Streptococcus cremoris) |
KEGG Pathway |
|
EC number |
2.7.1.39: Phosphotransferases with an alcohol group as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P52991
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P52991-F1 | Predicted | AlphaFoldDB |
No variants for P52991
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P52991 | |||||
No associated diseases with P52991
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.39 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| homoserine kinase activity | Catalysis of the reaction: L-homoserine + ATP = O-phospho-L-homoserine + ADP + 2 H(+). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| phosphorylation | The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. |
| threonine biosynthetic process | The chemical reactions and pathways resulting in the formation of threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKIIVPATSA | NLGAGFDSIG | IAVNLYLTVE | VLGESRDWKI | DHDLGENIPT | DERNLLLTTL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SAVLEDKNVA | LSAKFHLKMT | SEVPLARGLG | SSSSVIIAGI | ELANQLAKLN | LTSDEKLKLA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CEIEGHPDNV | APALLGNLVI | ASTVAGKTSH | IVADFPSCAL | LAFVPDYELK | TVESRKVLPN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELTYKEAVAA | SSIANVLTAS | LLTNNLEVAG | QMMEADRFHE | SYRASLIPEL | QLLREIGHEF |
| 250 | 260 | 270 | 280 | 290 | |
| GAYGTYLSGA | GPTVMLLVPD | DKLTLLTEKI | MEKNLTGHLY | PLKIDNKGLQ | VEESVF |