P34918
Gene name |
gap3 (Ava_3715) |
Protein name |
Glyceraldehyde-3-phosphate dehydrogenase 3 |
Names |
GAPDH 3, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase |
Species |
Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) |
KEGG Pathway |
ava:Ava_3715 |
EC number |
1.2.1.12: 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 P34918
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P34918-F1 | Predicted | AlphaFoldDB |
No variants for P34918
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P34918 | |||||
No associated diseases with P34918
4 regional properties for P34918
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Retroviral nucleocapsid Gag protein p24, N-terminal | 155 - 274 | IPR000721 |
| domain | Zinc finger, CCHC-type | 384 - 401 | IPR001878-1 |
| domain | Zinc finger, CCHC-type | 404 - 420 | IPR001878-2 |
| domain | Retroviral nucleocapsid Gag protein p24, C-terminal domain | 286 - 335 | IPR045345 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.12 | 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | Catalysis of the reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+. |
| 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 |
|---|---|
| gluconeogenesis | The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKIRVGINGF | GRMGRLALRA | AWGWPELEFV | HINEIKGGAV | AAAHLLKFDS | VHGRWTPEVE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AEGERVLIDS | TPLSFSEYGK | PEDVPWEDFG | VDLVLECSGK | FRTPATLDPY | FKRGVQKVIV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AAPVKEEALN | IVMGVNDYLY | EPEKHHLLTA | ASCTTNCLAP | VVKVIHEGLG | IKHGIITTIH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DNTNTQTLVD | APHKDLRRAR | ATSLSLIPTT | TGSATAIALI | YPELKGKLNG | IAVRVPLLNA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SLTDCVFEVN | RPTTVEEINA | LLKAASEQAP | LQGILGYEER | PLVSIDYKDD | PRSSIIDALS |
| 310 | 320 | 330 | |||
| TMVVDETQVK | ILAWYDNEWG | YVNRMVELAR | KVALSLK |