P0AEY3
Gene name |
mazG (b2781, JW2752) |
Protein name |
Nucleoside triphosphate pyrophosphohydrolase |
Names |
NTP-PPase |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b2781 |
EC number |
3.6.1.8: In phosphorus-containing anhydrides |
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
3 structures for P0AEY3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3CRA | X-ray | 210 A | A/B | 1-263 | PDB |
| 3CRC | X-ray | 300 A | A/B | 1-263 | PDB |
| AF-P0AEY3-F1 | Predicted | AlphaFoldDB |
No variants for P0AEY3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0AEY3 | |||||
No associated diseases with P0AEY3
2 regional properties for P0AEY3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | NTP pyrophosphohydrolase MazG, putative catalytic core | 27 - 100 | IPR004518-1 |
| domain | NTP pyrophosphohydrolase MazG, putative catalytic core | 169 - 227 | IPR004518-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.1.8 | In phosphorus-containing anhydrides |
| 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP diphosphatase activity | Catalysis of the reaction: ATP + H2O = AMP + H+ + diphosphate. |
| metal ion binding | Binding to a metal ion. |
| nucleoside triphosphate diphosphatase activity | Catalysis of the reaction: a nucleoside triphosphate + H2O = a nucleotide + H+ + diphosphate. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to starvation | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of nourishment. |
| dATP catabolic process | The chemical reactions and pathways resulting in the breakdown of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate). |
| dGTP catabolic process | The chemical reactions and pathways resulting in the breakdown of dGTP, guanosine triphosphate. |
| dTTP catabolic process | The chemical reactions and pathways resulting in the breakdown of dTTP, deoxyribosylthymine triphosphate. |
| dUTP catabolic process | The chemical reactions and pathways resulting in the breakdown of dUTP, deoxyuridine (5'-)triphosphate. |
| TTP catabolic process | The chemical reactions and pathways resulting in the breakdown of TTP, ribosylthymine triphosphate. |
| UTP catabolic process | The chemical reactions and pathways resulting in the breakdown of UTP, uridine (5'-)triphosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNQIDRLLTI | MQRLRDPENG | CPWDKEQTFA | TIAPYTLEET | YEVLDAIARE | DFDDLRGELG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLLFQVVFYA | QMAQEEGRFD | FNDICAAISD | KLERRHPHVF | ADSSAENSSE | VLARWEQIKT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EERAQKAQHS | ALDDIPRSLP | ALMRAQKIQK | RCANVGFDWT | TLGPVVDKVY | EEIDEVMYEA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RQAVVDQAKL | EEEMGDLLFA | TVNLARHLGT | KAEIALQKAN | EKFERRFREV | ERIVAARGLE |
| 250 | 260 | ||||
| MTGVDLETME | EVWQQVKRQE | IDL |