P15723
Gene name |
dgt |
Protein name |
Deoxyguanosinetriphosphate triphosphohydrolase |
Names |
dGTP triphosphohydrolase, dGTPase |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b0160 |
EC number |
3.1.5.1: Triphosphoric monoester hydrolases |
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
11 structures for P15723
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4X9E | X-ray | 310 A | A/B/C/D/E/F | 1-505 | PDB |
| 4XDS | X-ray | 335 A | A/B/C/D/E/F | 1-505 | PDB |
| 6OI7 | X-ray | 290 A | A/B/C/D/E/F | 1-505 | PDB |
| 6OIV | X-ray | 306 A | A/B/C/D/E/F | 1-505 | PDB |
| 6OIW | X-ray | 335 A | A/B/C/D/E/F | 1-505 | PDB |
| 6OIX | X-ray | 315 A | A/B/C/D/E/F | 1-505 | PDB |
| 6OIY | X-ray | 329 A | A/B/C/D/E/F | 1-505 | PDB |
| 7U65 | EM | 280 A | A/B/C/D/E/F | 1-505 | PDB |
| 7U66 | EM | 310 A | A/B/C/D/E/F | 1-505 | PDB |
| 7U67 | EM | 250 A | A/B/C/D/E/F | 1-505 | PDB |
| AF-P15723-F1 | Predicted | AlphaFoldDB |
No variants for P15723
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P15723 | |||||
No associated diseases with P15723
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.5.1 | Triphosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| cobalt ion binding | Binding to a cobalt ion (Co). |
| dGTPase activity | Catalysis of the reaction: dGTP + H(2)O = 2'-deoxyguanosine + 2 H(+) + triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| identical protein binding | Binding to an identical protein or proteins. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| single-stranded DNA binding | Binding to single-stranded DNA. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| dGTP catabolic process | The chemical reactions and pathways resulting in the breakdown of dGTP, guanosine triphosphate. |
| nucleobase-containing small molecule interconversion | The chemical reactions and pathways by which a nucleobase, nucleoside or nucleotide small molecule is synthesized from another nucleobase, nucleoside or nucleotide small molecule. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5ZJL9 | SAMHD1 | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 | Gallus gallus (Chicken) | PR |
| Q9Y3Z3 | SAMHD1 | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 | Homo sapiens (Human) | PR |
| Q60710 | Samhd1 | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAQIDFRKKI | NWHRRYRSPQ | GVKTEHEILR | IFESDRGRII | NSPAIRRLQQ | KTQVFPLERN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AAVRTRLTHS | MEVQQVGRYI | AKEILSRLKE | LKLLEAYGLD | ELTGPFESIV | EMSCLMHDIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NPPFGHFGEA | AINDWFRQRL | HPEDAESQPL | TDDRCSVAAL | RLRDGEEPLN | ELRRKIRQDL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CHFEGNAQGI | RLVHTLMRMN | LTWAQVGGIL | KYTRPAWWRG | ETPETHHYLM | KKPGYYLSEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AYIARLRKEL | NLALYSRFPL | TWIMEAADDI | SYCVADLEDA | VEKRIFTVEQ | LYHHLHEAWG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QHEKGSLFSL | VVENAWEKSR | SNSLSRSTED | QFFMYLRVNT | LNKLVPYAAQ | RFIDNLPAIF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AGTFNHALLE | DASECSDLLK | LYKNVAVKHV | FSHPDVERLE | LQGYRVISGL | LEIYRPLLSL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SLSDFTELVE | KERVKRFPIE | SRLFHKLSTR | HRLAYVEAVS | KLPSDSPEFP | LWEYYYRCRL |
| 490 | 500 | ||||
| LQDYISGMTD | LYAWDEYRRL | MAVEQ |