Q9KNM2
Gene name |
spoT (VC_2710) |
Protein name |
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase |
Names |
Penta-phosphate guanosine-3'-pyrophosphohydrolase, (ppGpp)ase |
Species |
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
KEGG Pathway |
vch:VC_2710 |
EC number |
3.1.7.2: Diphosphoric 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
1 structures for Q9KNM2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9KNM2-F1 | Predicted | AlphaFoldDB |
No variants for Q9KNM2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9KNM2 | |||||
No associated diseases with Q9KNM2
7 regional properties for Q9KNM2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ACT domain | 626 - 705 | IPR002912 |
| domain | HD/PDEase domain | 41 - 166 | IPR003607 |
| domain | TGS | 387 - 448 | IPR004095 |
| domain | HD domain | 45 - 144 | IPR006674 |
| domain | RelA/SpoT | 214 - 345 | IPR007685 |
| domain | RelA/SpoT, TGS domain | 390 - 447 | IPR033655 |
| domain | RelA/SpoT, AH and RIS domains | 461 - 544 | IPR045600 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.7.2 | Diphosphoric 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 |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP diphosphokinase activity | Catalysis of the reaction: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. |
| guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity | Catalysis of the reaction: guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| guanosine tetraphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of guanine tetraphosphate (5'-ppGpp-3'), a derivative of guanine riboside with four phosphates. |
| guanosine tetraphosphate metabolic process | The chemical reactions and pathways involving guanine tetraphosphate (5'-ppGpp-3'), a derivative of guanine riboside with four phosphates. |
| response to starvation | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nourishment. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MYLFDSLKDV | AQEYLTEPQI | EALRQSYVVA | RDAHEGQTRS | SGEPYIIHPV | AVARILAEMR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDLETLQAAL | LHDVIEDCDV | TKEDLDAHFG | SSVAELVDGV | SKLDKLKFRD | RKEAQAENFR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KMVLAMVQDI | RVILIKLADR | TPNMRTLGAL | RPDKKRRIAR | ETLEIYAPLA | HRLGIHNIKT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELEELGFEAL | YPNRYRVLKE | VVKAARGNRK | EMIQRIHSEI | EGRLQEVGLP | ARVVGREKNL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FSIYNKMKTK | EQRFHTIMDI | YAFRIVVDTA | DTCYRVLGQV | HSLYKPRPAR | MKDYIAVPKA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NGYQSLHTSM | VGPHGVPVEV | QIRTEDMDQM | ADKGVAAHWS | YKANSERGGT | TAQIKAQRWM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QSLLELQQSA | GNSFEFIENV | KSDLFPDEIY | VFTPKGRIVE | LPMGATAVDF | AYAVHTDIGN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TCVGARVDRT | PYPLSQSLKS | GQTVEIISAP | GARPNAAWLN | YVVTSRARTK | IRQVLKTMRR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EDSITLGRRL | LNHALGEHSV | NEIAPENISK | VLSDLKIASM | DDLLAAIGLG | ELMSIVIARR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LLGNADELTE | PSKSGGNKNK | LPIRGAEGIL | LTFANCCHPI | PDDHIIAHVS | PGRGLVVHRE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| TCPNVRGYQK | EPDKYMAVEW | TKDYDQEFIT | ELKVDMHNRQ | GALAELTNVI | SKTGSNIHGL |
| 670 | 680 | 690 | 700 | ||
| STEERDGRLY | TVTVLLTTKD | RVHLAGIMRK | IRTMPHALKV | RRRKN |