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2.A.7.9.5
The plastidic phosphate/triosephosphate transporter, TPT (Linka et al., 2008). TPT catalyses the strict 1:1 exchange of triose-phosphate, 3-phosphoglycerate and inorganic phosphate across the chloroplast envelope Lee et al. 2017 reported crystal structures of TPT bound to two different substrates, 3-phosphoglycerate and inorganic phosphate, in occluded conformations. The structures reveal that TPT adopts a 10-transmembrane drug/metabolite transporter fold. Both substrates are bound within the same central pocket, where conserved lysine, arginine and tyrosine residues recognize the shared phosphate group. A structural comparison with the outward-open conformation of the bacterial drug/metabolite transporter suggests a rocker-switch motion of helix bundles, and molecular dynamics simulations support a model in which this rocker-switch motion is tightly coupled to substrate binding to ensure strict 1:1 exchange. The results reveal the mechanism of sugar phosphate/phosphate exchange by TPT. TPTexports  Calvin cycle intermediates from chloroplasts and plays fundamental roles in nearly all photosynthetic eukaryotes (Lee et al. 2017).

Accession Number:B5AJT1
Protein Name:Putative hexose phosphate translocator
Length:410
Molecular Weight:45451.00
Species:Galdieria sulphuraria (Red alga) [130081]
Number of TMSs:8
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate phosphate, Triose-phosphate

Cross database links:

Pfam: PF03151   

Gene Ontology

GO:0016021 C:integral to membrane

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MIEAAFVPLS CSLFSKQHRW TVVSRNKNKN SISSHMEGSK KLLGTPRFTL SRSQFLNVSY 
61:	LRTKYNNVAS SSKGEKDIIR AAVDKSESGG SPQKSSVGVS PTLVHTLKVG FYFFLWYFFN 
121:	FIFNIANKRT LNMWKYPWVL STIQLGVGAL YCTFLWVLGL RTKPNVSKKL IKALIWPSLG 
181:	HTLGHAATCM SFSLVAISFT HVVKSAEPVF GAVGSALVLG EFFHPLTYLT LVPIVSGVAL 
241:	SAATELTFTW TGFITAMISN VAFVTRNITS KFTMVDFKNE KTLIAQNTYA LITIISFFME 
301:	LPFALLMEGF PPLVSAIAGV SKAKLFGSIM FCSLFYHLYN EVSYLCLDNV SPVSFSIGNT 
361:	IKRVIIIFGS ILVFRTPVTR LNFIGSTIAI IGTMLYSLAK AKLPSKREKQ