A3MWK6
Gene name |
Pcal_1606 |
Protein name |
NADP(+)-dependent glutamate dehydrogenase |
Names |
NADP-GDH |
Species |
Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1) |
KEGG Pathway |
pcl:Pcal_1606 |
EC number |
1.4.1.4: 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 A3MWK6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A3MWK6-F1 | Predicted | AlphaFoldDB |
No variants for A3MWK6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A3MWK6 | |||||
No associated diseases with A3MWK6
3 regional properties for A3MWK6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal | 182 - 419 | IPR006096 |
| domain | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain | 35 - 163 | IPR006097 |
| domain | NAD(P) binding domain of glutamate dehydrogenase | 181 - 413 | IPR033922 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.4.1.4 | 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 |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| glutamate dehydrogenase (NADP+) activity | Catalysis of the reaction: L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+. |
| NADP+ binding | Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. |
| NADPH binding | Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 2-oxoglutarate metabolic process | The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism. |
| glutamate metabolic process | The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSQNGQFLEY | TLQVIRRGVE | MGGFPEDFYK | LLSRPKRIIQ | VSIPVKMDNG | SYEVFEGYRV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QHNDALGPFK | GGIRFHPEVT | LADDIALAML | MTLKNSLAGL | PYGGAKGAVR | VDPRRLSRRE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LEELARGYAR | AVAPLIGEQL | DIPAPDVGTD | SQVMAWMVDE | YSKLAGRNAP | AVFTSKPPEL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| WGNPVREYST | GFGVAVAARE | VAKRLWGGIE | GKTVAVHGAG | NTGAWAAYWL | EKMGAKVVAI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SDTRGTVVNK | AGIPGEQILK | VYMEKKRDKS | ATVLALEGEK | IADSNASLYQ | DVDILVPAAI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ENVVREDNVG | LVRARLVVEG | ANGPTTPGAE | RRLYERGVVV | VPDILANAGG | VIMSYLEWVE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NLQWLFWDEE | ETRRRLEAIM | SNNVARVYAR | WEKEKSWTMR | DAAVVTALER | IYNAMKTRGW |
| I |