| General Information |
| MoonProt ID | 574 |
| First appeared in release | 4.0 |
| Name(s) | Triosephosphate isomerase - tpiA |
| UniProt ID | B1ICZ4 |
| GO terms | GO:0004807 triose-phosphate isomerase activity, GO:0016853 isomerase activity, GO:0006094 gluconeogenesis, GO:0006096 glycolytic process, GO:0019563 glycerol catabolic process, GO:0046166 glyceraldehyde-3-phosphate biosynthetic process, GO:0005737 cytoplasm, GO:0005829 cytosol |
| Organisms for which functions have been demonstrated | Streptococcus pneumoniae (strain Hungary19A-6) a commensal bacterium that infects humans |
| Sequence length | 252.0 |
| FASTA sequence | >sp|B1ICZ4|TPIS_STRPI Triosephosphate isomerase OS=Streptococcus pneumoniae (strain Hungary19A-6) OX=487214 GN=tpiA PE=3 SV=1
MSRKPFIAGNWKMNKNPEEAKAFVEAVASKLPSSDLVEAGIAAPALDLTTVLAVAKGSNL
KVAAQNCYFENAGAFTGETSPQVLKEIGTDYVVIGHSERRDYFHETDEDINKKAKAIFAN
GMLPIICCGESLETYEAGKAAEFVGAQVSAALAGLTAEQVAASVIAYEPIWAIGTGKSAS
QDDAQKMCKVVRDVVAADFGQEVADKVRVQYGGSVKPENVASYMACPDVDGALVGGASLE
AESFLALLDFVK |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | homodimer |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | not in DisProt |
| Predicted Disorder Regions | no disorder found |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme, triose phosphate isomerase |
| References for function | Hirayama, S., Domon, H., Hiyoshi, T., Isono, T., Tamura, H., Sasagawa, K., Takizawa, F., & Terao, Y. (2022). Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation. FEBS open bio, 12(6), 1206–1219. https://doi.org/10.1002/2211-5463.13396 |
| E.C. number | EC:5.3.1.1 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | binds plasminogen, binds host complement inhibitors Factor H, FHL-1, CFHR1 |
| References for function | Hirayama, S., Domon, H., Hiyoshi, T., Isono, T., Tamura, H., Sasagawa, K., Takizawa, F., & Terao, Y. (2022). Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation. FEBS open bio, 12(6), 1206–1219. https://doi.org/10.1002/2211-5463.13396 |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | cell surface |
| Comments | |