Q5HNR8
Gene name |
relA (SERP1196) |
Protein name |
GTP pyrophosphokinase |
Names |
(p)ppGpp synthase, ATP:GTP 3'-pyrophosphotransferase, ppGpp synthase I |
Species |
Staphylococcus epidermidis (strain ATCC 35984 / RP62A) |
KEGG Pathway |
ser:SERP1196 |
EC number |
2.7.6.5: Diphosphotransferases |
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 Q5HNR8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5HNR8-F1 | Predicted | AlphaFoldDB |
No variants for Q5HNR8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5HNR8 | |||||
No associated diseases with Q5HNR8
7 regional properties for Q5HNR8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ACT domain | 649 - 729 | IPR002912 |
| domain | HD/PDEase domain | 46 - 171 | IPR003607 |
| domain | TGS | 393 - 454 | IPR004095 |
| domain | HD domain | 50 - 149 | IPR006674 |
| domain | RelA/SpoT | 220 - 350 | IPR007685 |
| domain | RelA/SpoT, TGS domain | 396 - 454 | IPR033655 |
| domain | RelA/SpoT, AH and RIS domains | 468 - 632 | IPR045600 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.6.5 | Diphosphotransferases |
| 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. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTP diphosphokinase activity | Catalysis of the reaction: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. |
| kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
2 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. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNNEYPYSAD | EVLYKAKSYL | STSEYEYVLK | SYHIAYEAHK | GQFRKNGLPY | IMHPIQVAGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTEMRLDGPT | IVAGFLHDVI | EDTSYTFEDV | KDMFNEEIAR | IVDGVTKLKK | VKYRSKEEQQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AENHRKLFIA | IAKDVRVILV | KLADRLHNMR | TLKAMPREKQ | VRISKETLEI | YAPLAHRLGI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NTIKWELEDT | ALRYIDSVQY | FRIVNLMKKK | RSEREAYITN | AINKIKNEMT | KMNLSGEING |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RPKHIYSIYR | KMIKQKKQFD | QIFDLLAIRI | IVNSINDCYA | TLGLVHTLWK | PMPGRFKDYI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AMPKQNMYQS | LHTTVVGPNG | DPLEIQIRTH | EMHEIAEHGV | AAHWAYKEGK | TVNQKTQDFQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NKLNWLKELA | ETDHTSADAQ | EFMESLKYDL | QSDKVYAFTP | ASDVIELPYG | AVPIDFAYAI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HSEVGNKMIG | AKVNGKIVPI | DYVLQTGDII | EIRTSKHSYG | PSRDWLKIVK | SSSAKSKIKS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FFKKQDRSSN | IEKGKFMVEA | EIKEQGFRVE | DILTEKNLEV | VNEKYHFAND | EDLYAAVGFG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GVTSIQIVNK | LTERQRILDK | QKALNEAQEV | TKSVPIKKDI | TTDSGVYVEG | LENVLIKLSK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| CCNPIPGDDI | VGYITKGHGI | KVHRTDCPNI | KNETDRLISV | EWVKSKDSTQ | QYQVDLEVTA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YDRNGLLNEV | LQAVNSTAGS | LIKVSGRSDI | DKNAVINISV | MVKNVNDVYR | VVEKIKQLGD |
| VYTVSRVWN |