| General Information |
| MoonProt ID | 581 |
| First appeared in release | 4.0 |
| Name(s) | Glyceraldehyde-3-phosphate dehydrogenase - gap |
| UniProt ID | B0B879 |
| GO terms | GO:0000166 nucleotide binding, GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity, GO:0016491 oxidoreductase activity, GO:0016620 oxidoreductase activity acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor, GO:0050661 NADP binding, GO:0051287 NAD binding, GO:0006006 glucose metabolic process, GO:0006096 glycolytic process, GO:0005737 cytoplasm |
| Organisms for which functions have been demonstrated | Chlamydia trachomatis, obligate intracellular bacteria of eukaryotic cells |
| Sequence length | 334 |
| FASTA sequence | >sp|B0B879|G3P_CHLT2 Glyceraldehyde-3-phosphate dehydrogenase OS=Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu) OX=471472 GN=gap PE=3 SV=1
MRIVINGFGRIGRLVLRQILKRNSPIEVVAINDLVAGDLLTYLFKYDSTHGSFAPQATFS
DGCLVMGERKIRFLAEKDVQKLPWKDLDVDVVVESTGLFVNRDDAAKHLDSGAKRVLITA
PAKGDVPTFVMGVNHQQFDPADVIISNASCTTNCLAPLAKVLLDNFGIEEGLMTTVHAAT
ATQSVVDGPSRKDWRGGRGAFQNIIPASTGAAKAVGLCLPELKGKLTGMAFRVPVADVSV
VDLTVKLSSATTYEAICEAVKHAANTSMKNIMYYTEEAVVSSDFIGCEYSSIFDAQAGVA
LNDRFFKLVAWYDNEIGYATRIVDLLEYVQENSK |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | not in DisProt |
| Predicted Disorder Regions | N-terminus AA 1, 2, 188-191, 332-334 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme, glyceraldehyde 3-phosphate dehydrogenase, catalyzes the reversible oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphate coupled with reduction of NAD+ to NADH |
| References for function | Schormann, N., Campos, J., Motamed, R., Hayden, K. L., Gould, J. R., Green, T. J., Senkovich, O., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2020). Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding. Protein science : a publication of the Protein Society, 29(12), 2446–2458. https://doi.org/10.1002/pro.3975 |
| E.C. number | EC:1.2.1.12 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | binds to plasminogen |
| References for function | Schormann, N., Campos, J., Motamed, R., Hayden, K. L., Gould, J. R., Green, T. J., Senkovich, O., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2020). Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding. Protein science : a publication of the Protein Society, 29(12), 2446–2458. https://doi.org/10.1002/pro.3975 |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | cell surface |
| Comments | |