| General Information |
| MoonProt ID | 515 |
| First appeared in release | 4.0 |
| Name(s) | Glyceraldehyde-3-phosphate dehydrogenase |
| UniProt ID | A0A2P0XIG5 |
| GO terms | GO:0006006 glucose metabolic process GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor GO:0051287 NAD binding GO:0016491 oxidoreductase activity GO:0050661 NADP binding GO:0006096 glycolytic process GO:0000166 nucleotide binding GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity GO:0051287 NAD binding GO:0006096 glycolytic process |
| Organisms for which functions have been demonstrated | Periplaneta americana |
| Sequence length | 332 amino acids |
| FASTA sequence | >tr|A0A2P0XIG5|A0A2P0XIG5_PERAM Glyceraldehyde-3-phosphate dehydrogenase OS=Periplaneta americana OX=6978 PE=2 SV=1
MSKIGINGFGRIGRLVLRAALEKGAQVVAINDPFIGLDYMVYMFKYDSTHGRFKGEVSAEGDQLVVNGQKISVFAERDPKAIPWGKAGADYVVESTGVFTTIDKASAHLEGGAKKVIISAPSADAPMFVVGVNLEAYDPSLKIVSNASCTTNCLAPLAKVIHDNFEIVEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPVPNVSVVDLTVRLGKPASYDDIKAKVKEAATGPLKGILDYTEDDVVSSDFISDTHSSIFDAKAGIPLNNNFVKLISWYDNEFGYSNRVIDLIKYMQSKD |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | |
| DisProt Annotation | |
| Predicted Disorder Regions | |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) |
| References for function | 1. CAPUTTO, R., & DIXON, M. (1945). Crystallization and identity of the triose and triosephosphate dehydrogenases of muscle. Nature, 156, 630. https://doi.org/10.1038/156630c0 2. CORI, G. T., SLEIN, M. W., & CORI, C. F. (1948). Crystalline d-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. The Journal of biological chemistry, 173(2), 605–618. 3. HAGEMAN, R. H., & ARNON, D. I. (1955). The isolation of triosephosphate dehydrogenase from pea seeds. Archives of biochemistry and biophysics, 55(1), 162–168. https://doi.org/10.1016/0003-9861(55)90554-3 4. Velick, S.F. and Furfine, C. Glyceraldehyde 3-phosphate dehydrogenase.
In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes , 2nd ed. vol. 7 , Academic Press , New York , 1963 , 243-273
5. Warburg, O. and Christian, W. Isolierung und Krystallisation des Proteins des oxydierenden Gärungsferments.
Biochem. Z. 303 : 40-68 (1939). |
| E.C. number | EC:1.2.1.12 |
| Location of functional site(s) | |
| Cellular location of function | Cytoplasm |
| Comments | |
| Function 2 |
| Function description | Antibacterial and Antiviral action |
| References for function | 1. Sagar, S., & Chunduri, J. R. Identification and Characterisation of Moonlight Proteins from Insect Brain Tissue Lysate.(2020). Int. J. Life Sci. Pharma Res, 10(5), L20-30. DOI: 10.22376/ijpbs/lpr.2020.10.5.L20-30
2. Siddharth Sagar, Jayaprada Rao Chunduri and Vyomesh Javle (2020); AN ASSESSMENT OF THE INTERACTION BETWEEN INSECT BRAIN PROTEIN AND NON-STRUCTURAL PROTEIN OF CORONAVIRUS USING IN-SILICO ANALYSES Int. J. of Adv. Res. 8 (May). 436-452. DOI URL: http://dx.doi.org/10.21474/IJAR01/10945 |
| E.C. number | EC:1.2.1.59 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |