P51776
Gene name |
|
Protein name |
Pyruvate, phosphate dikinase |
Names |
Pyruvate, orthophosphate dikinase |
Species |
Giardia intestinalis (Giardia lamblia) |
KEGG Pathway |
|
EC number |
2.7.9.1: Phosphotransferases with paired acceptors |
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 P51776
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P51776-F1 | Predicted | AlphaFoldDB |
No variants for P51776
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P51776 | |||||
No associated diseases with P51776
6 regional properties for P51776
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PEP-utilising enzyme, C-terminal | 529 - 874 | IPR000121 |
| domain | Pyruvate phosphate dikinase, AMP/ATP-binding | 68 - 297 | IPR002192-1 |
| domain | Pyruvate phosphate dikinase, AMP/ATP-binding | 313 - 367 | IPR002192-2 |
| domain | PEP-utilising enzyme, mobile domain | 431 - 512 | IPR008279 |
| active_site | PEP-utilising enzyme, active site | 459 - 470 | IPR018274 |
| conserved_site | PEP-utilising enzyme, conserved site | 769 - 787 | IPR023151 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.9.1 | Phosphotransferases with paired acceptors |
| 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. |
| kinase activity | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. |
| metal ion binding | Binding to a metal ion. |
| pyruvate, phosphate dikinase activity | Catalysis of the reaction: ATP + phosphate + pyruvate = AMP + diphosphate + 2 H(+) + phosphoenolpyruvate. |
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. |
| pyruvate metabolic process | The chemical reactions and pathways involving pyruvate, 2-oxopropanoate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTRRVYFFG | ETPENQPANS | ELCRKVLGGK | GISLAAMIKL | GMPVPLGFTI | TCQTCVEYQK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TASWPKGLKE | EVASNLKLLE | EKMGKTFGDN | TNPLLVSVRS | GAAVSMPGMM | DTILNLGLND |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ESVKGLAAVT | GNARFAYDSY | RRFMQMFGDV | CLGIDHDKFE | HALDAVKTRY | GRKTDPELTA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DELEEVCEAY | RKICVAATGK | TFPQCPHEQL | ELAINAVFKS | WTNPRAQAYR | TLNKLDHNMG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TAVNVQSMVF | GNTGDDSGTG | VGFTRCPKTG | EKFSYLYGEF | LQNAQGEDVV | AGIRTPVNLK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EMPTINASWK | ACYDELSLIY | AKLEGYYNDM | VDLEFTVENG | KLWMLQARAG | KRTGFAMVRI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AIDMCKEGML | TEEEALLRID | ANKINEFLFK | RFDPSVKPVV | LGKGIPASPG | AAVGVICFCP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MRTCELAEQG | KKVILTRIET | SPEDILGMDR | AVGILTARGG | QTSHAAVVAR | GMGKCCVAGA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DCCQINYATK | TLVIGDRKFK | EGDFISINGT | TGEIYNGAVQ | TIEPGITDDL | QTIMDWSDKY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RVLKIRTNAD | TPHDAAVARK | FGAEGIGLCR | TEHMFFAADR | IMAMREMILS | DDEGARRTAL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NKLLPFQRED | FIGIFKAMDG | KGVNIRLLDP | PLHEFLPHTR | DLQKKLAEDM | NKKHRHIHER |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VEDLHEVNPM | LGFRGVRLGI | VYPEISEMQV | RAILEAACIV | SREGVTVKPE | IMIPVLFSEN |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EMEIMHALVN | RVAASVFKEH | GTTVDYEVGT | MIELPRACVM | ADKIAQTAQY | FSFGTNDLTQ |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TTFGISRDDA | GKFIPKYIDR | GIFKVDPFVT | LDQQGVGALM | KMAIEGGRST | RTDMKIGICG |
| 850 | 860 | 870 | 880 | ||
| EQTDPASILF | LHKIGLNYVS | CSPYRVPVAR | VAAAIAAIKA | RTNQ |