| Primary Identifier | IPR004696 | Type | Family |
| Short Name | Tpt_PEP_transl |
| description | Functionally characterised members of the 6-8 TMS Triose-phosphate Transporter (TPT) family are derived from the inner envelopemembranes of chloroplasts and non-green plastids of plants. Under normal physiological conditions, chloroplast TPTs mediate a strict antiport of substrates, frequently exchanging an organic three carbon compound phosphate ester for inorganic phosphate (Pi) [, ].Normally, a triose-phosphate, 3-phosphoglycerate, or another phosphorylated C3compound made in the chloroplast during photosynthesis, exits the organelle into thecytoplasm of the plant cell in exchange for Pi. However, experiments with reconstituted translocator in artificial membranes indicate that transport can also occur by a channel-like uniport mechanism with up to 10-fold higher transport rates. Channel opening may be induced by a membrane potential of large magnitude and/or by high substrate concentrations. Non-green plastid and chloroplast carriers, such as those from maize endosperm and root membranes, mediate transport of C3 compounds phosphorylated at carbon atom 2, particularly phosphoenolpyruvate, in exchange for Pi. These are the phosphoenolpyruvate:Pi antiporters (PPT). Glucose-6-P has also been shown to be a substrate of some plastid translocators (GPT). The three types of proteins (TPT, PPT and GPT) are divergent in sequence as well as substrate specificity, but their substrate specificities overlap.TPT paralogues are also present in Saccharomyces cerevisiae, which are functionally uncharacterised. |
