P48826
Gene name |
gsdA (g6pdh) |
Protein name |
Glucose-6-phosphate 1-dehydrogenase |
Names |
G6PD |
Species |
Aspergillus niger |
KEGG Pathway |
|
EC number |
1.1.1.49: With NAD(+) or NADP(+) 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 P48826
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P48826-F1 | Predicted | AlphaFoldDB |
No variants for P48826
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P48826 | |||||
No associated diseases with P48826
19 regional properties for P48826
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | LDLR class B repeat | 359 - 399 | IPR000033-1 |
| repeat | LDLR class B repeat | 697 - 736 | IPR000033-2 |
| repeat | LDLR class B repeat | 738 - 780 | IPR000033-3 |
| repeat | LDLR class B repeat | 781 - 819 | IPR000033-4 |
| domain | Protein kinase domain | 1945 - 2222 | IPR000719 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 1948 - 2215 | IPR001245 |
| conserved_site | Tyrosine-protein kinase, receptor class II, conserved site | 2108 - 2116 | IPR002011 |
| domain | Fibronectin type III | 99 - 196 | IPR003961-1 |
| domain | Fibronectin type III | 195 - 285 | IPR003961-2 |
| domain | Fibronectin type III | 557 - 671 | IPR003961-3 |
| domain | Fibronectin type III | 948 - 1028 | IPR003961-4 |
| domain | Fibronectin type III | 1041 - 1150 | IPR003961-5 |
| domain | Fibronectin type III | 1469 - 1539 | IPR003961-6 |
| domain | Fibronectin type III | 1557 - 1656 | IPR003961-7 |
| domain | Fibronectin type III | 1658 - 1751 | IPR003961-8 |
| domain | Fibronectin type III | 1753 - 1842 | IPR003961-9 |
| active_site | Tyrosine-protein kinase, active site | 2075 - 2087 | IPR008266 |
| binding_site | Protein kinase, ATP binding site | 1951 - 1980 | IPR017441 |
| domain | Tyrosine-protein kinase, catalytic domain | 1945 - 2215 | IPR020635 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.49 | With NAD(+) or NADP(+) as acceptor |
| 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 |
|---|---|
| glucose-6-phosphate dehydrogenase activity | Catalysis of the reaction: D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glucose metabolic process | The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides. |
| pentose-phosphate shunt | The metabolic process in which glucose-6-phosphate is oxidized to form carbon dioxide (CO2) and ribulose 5-phosphate, coupled to reduction of NADP+ to NADPH; ribulose 5-P then enters a series of reactions that can yield biosynthetic precursors (ribose-5-phosphate and erythrose-4-phosphate) and glycolytic intermediates (fructose-6-phosphate and glyceraldehyde-3-phosphate). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASTIARTEE | RQNAGTMELK | DDTVIIVLGA | SGDLAKKKTF | PALFGLYRNK | FLPKGIKIVG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YARTNMDHEE | YLRRVRSYIK | TPTKEIEEQL | DSFCQFCTYI | SGQYDKDDSF | INLNKHLEEI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EKGQKEQNRI | YYMALPPSVF | TTVSDQLKRN | CYPKNGVARI | IVEKPFGKDL | QSSRDLQKAL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EPNWKEEEIF | RIDHYLGKEM | VKNILIMRFG | NEFFNATWNR | HHIDNVQITF | KEPFGTEGRG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GYFDEFGIIR | DVMQNHLLQV | LTLLAMERPI | SFSAEDIRDE | KVRVLRAMDA | IEPKNVIIGQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YGKSLDGSKP | AYKEDETVPQ | DSRCPTFCAM | VAYIKNERWD | GVPFIMKAGK | ALNEQKTEIR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IQFRDVTSGI | FKDIPRNELV | IRVQPNESVY | IKMNSKLPGL | SMQTVVTELD | LTYRRRFSDL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KIPEAYESLI | LDALKGDHSN | FVRDDELDAS | WRIFTPLLHY | LDDNKEIIPM | EYPYGSRGPA |
| 490 | 500 | ||||
| VLDDFTASFG | YKFSDAAGYQ | WPLTSTPNRL |