P90521
Gene name |
top2mt (topA, DDB_G0279737) |
Protein name |
ATP-dependent 6-phosphofructokinase |
Names |
ATP-PFK, Phosphofructokinase, Phosphohexokinase |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0274111 |
EC number |
2.7.1.11: Phosphotransferases with an alcohol group as acceptor |
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 P90521
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P90521-F1 | Predicted | AlphaFoldDB |
No variants for P90521
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P90521 | |||||
No associated diseases with P90521
4 regional properties for P90521
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphofructokinase domain | 54 - 356 | IPR000023-1 |
| domain | Phosphofructokinase domain | 439 - 720 | IPR000023-2 |
| conserved_site | Phosphofructokinase, conserved site | 326 - 344 | IPR015912-1 |
| conserved_site | Phosphofructokinase, conserved site | 692 - 710 | IPR015912-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.11 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 6-phosphofructokinase complex | A protein complex that possesses 6-phosphofructokinase activity; homodimeric, homooctameric, and allosteric homotetrameric forms are known. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| 6-phosphofructokinase activity | Catalysis of the reaction: ATP + D-fructose-6-phosphate = ADP + D-fructose 1,6-bisphosphate. |
| AMP binding | Binding to AMP, adenosine monophosphate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| fructose-6-phosphate binding | Binding to fructose 6-phosphate. |
| identical protein binding | Binding to an identical protein or proteins. |
| metal ion binding | Binding to a metal ion. |
| monosaccharide binding | Binding to a monosaccharide. Monosaccharides are the simplest carbohydrates; they are polyhydroxy aldehydes H[CH(OH)]nC(=O)H or polyhydroxy ketones HnC(=O) |
| tubulin binding | Binding to monomeric or multimeric forms of tubulin, including microtubules. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| canonical glycolysis | The glycolytic process that begins with the conversion of glucose to glucose-6-phosphate by glucokinase activity. Glycolytic processes are the chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP. |
| fructose 1,6-bisphosphate metabolic process | The chemical reactions and pathways involving fructose 1,6-bisphosphate, also known as FBP. The D enantiomer is a metabolic intermediate in glycolysis and gluconeogenesis. |
| fructose 6-phosphate metabolic process | The chemical reactions and pathways involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism. |
| glucose catabolic process | The chemical reactions and pathways resulting in the breakdown of glucose, the aldohexose gluco-hexose. |
| negative regulation of microtubule polymerization | Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTTSKIIND | GEGEDVKGNK | NINKKSLIDE | NRLDEKKDLL | SDKVESKTHC | SVKRMAVLTS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GGDSSGMNPA | IRAFARQVML | KGAKVFAVRE | GYNGLVNDSI | VPLNWGSVAG | IISRGGTIIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TARSAEFRTR | EGRKRAVFNL | VKNRIDNLLV | IGGDGSLTGA | NLLRTEWCSL | LEELVKDGKL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TLDVMEHFPI | LSIAGIVGSI | DNDMCGTDLT | VGADTATKRI | LEAIDSILST | AVSHQRSFVI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EVMGRNCGWL | ALASGVATGA | DYILIPESPP | DDGWEQTMAD | NLERGRLSGR | RCSLVIVSEG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AIDRQGKPIT | SAYVRQFLED | KGHDARITIL | GHVQRGGTPT | FLDRYIATRM | GIEAANYFYD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| STIEQLKQPV | LIGMSGMDTI | RSPLMECVQK | TQSIASLIKE | RRFNEVVDVR | GGMFKEFYEI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FIACSNLHRR | KVESKGMGVL | ILHSGGPSPG | MNPCVRAFTR | LGIDHGYTMY | GCFNGFGGLA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LGEIEQLHWM | TVNGWSVMGG | AELGTNRSIP | NDSNIEAIIA | TLERFKINAI | LMFGGFNGYL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GIAKLYEYRE | KYQQLKRISI | IGAPGTIANN | VPGTNISIGS | DTSLNNTLDA | LDKIKQSAVA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SRRLFVVEVM | GAHCGYLAAM | SSLTSGAERS | YIMERGITLN | TLTKDLEMFV | ERFKREHRIG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LIIKSELASN | TYSTHFIYSL | FKEEGKHLFD | VRESILGHLQ | QGGTPSAIDR | IFSTRLMNHY |
| 730 | 740 | 750 | 760 | 770 | 780 |
| YQFLENDLKE | HGHLQMNGCI | GFIDGGIHYT | PMQEMIEEMS | DKFRRPRSQW | WMDLVETSQN |
| 790 | 800 | 810 | 820 | 830 | |
| ISVFPLDDPS | STNFEGCNSN | LSEQDRPIKK | SDISSPTSYS | QKTFDPNVNP | QFTL |