A9A6M9
Gene name |
gap |
Protein name |
Glyceraldehyde-3-phosphate dehydrogenase |
Names |
GAPDH, NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase |
Species |
Methanococcus maripaludis (strain C6 / ATCC BAA-1332) |
KEGG Pathway |
mmx:MmarC6_0626 |
EC number |
1.2.1.59: 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 A9A6M9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A9A6M9-F1 | Predicted | AlphaFoldDB |
No variants for A9A6M9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A9A6M9 | |||||
No associated diseases with A9A6M9
No regional properties for A9A6M9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A9A6M9 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.59 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4-hydroxy-tetrahydrodipicolinate reductase | Catalysis of the reaction: (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+. |
| glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | Catalysis of the reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+. |
| glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity | Catalysis of the reaction: phosphate + NADP+ + glyceraldehyde-3-phosphate = NADPH + 3-phospho-D-glyceroyl-phosphate. |
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| 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 |
|---|---|
| glycolytic process | The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. |
| lysine biosynthetic process via diaminopimelate | The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVNVLINGYG | SIGKRVADAV | AKQDDMKVIG | VTKTKPDFEA | RMAVEKGYKL | FAAIPERKHL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FEEAGIPVEG | TLDDIIEDAD | IVVDGAPKKI | GKANLENVYK | KHGVKAIIQG | GEKAGDAQDS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FNSLWSYNRC | YGKDYIRLVS | CNTTGLCRSM | YAINSVADIL | KARIVLIRRA | ADPNDVKTGP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VNAIVPNPVS | VPSHHGPDVV | SVIPELDGKI | MTSAVIVPTT | LMHMHSIMVE | TSGTNRDEII |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DALAKTPRIL | TLKASEGFDS | TAKIIEYARD | LGRSRYDLNE | IAVWEESVNV | VDNEVYMMQA |
| 310 | 320 | 330 | |||
| IHQESDVIPE | NVDCIRAMLE | MESDNLKSIE | KTNKAMGLIK |