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2.A.23.1.14
Sodium:glutamate cotransporter (symporter), Glt, of 430 aas and probably 9 TMSs in a 3 + 3 + 3 TMS arrangement.  Several 3-d structures are known (Jensen et al. 2013). The binding and transport of L- and D-aspartate have been studied, revealing that both the L- and D-aspartate bound GltTk structures with only minor rearrangements in the structure of the binding site (Arkhipova et al. 2019). A conserved methionine residue plays a role in the ion symport process, apparently by influencing the specific kinetics in the binding reaction, which, while influential for the turnover rate, does not fundamentally explain the ion-coupling mechanism (Zhou et al. 2021). The 3-d structure is available (PDB # 6XWO).  It has a covalent trimeric transporter structure with an interconnecting rigid scafford domain (trimerization domain) on the inside. This seems to be a unique structure for a transporter (Colucci et al. 2023). The structure of the P208R mutant is also known (Colucci et al. 2023).

Accession Number:Q5JID0
Protein Name:Proton/glutamate symporter, SDF family
Length:430
Molecular Weight:45546.00
Species:Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) [69014]
Number of TMSs:9
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate anion, sodium(1+), hydron, L-aspartate(1-), glutamate(2-)

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FASTA formatted sequence
1:	MGKSLLRRYL DYPVLWKILW GLVLGAVFGL IAGHFGYAGA VKTYIKPFGD LFVRLLKMLV 
61:	MPIVLASLVV GAASISPARL GRVGVKIVVY YLATSAMAVF FGLIVGRLFN VGANVNLGSG 
121:	TGKAIEAQPP SLVQTLLNIV PTNPFASLAK GEVLPVIFFA IILGIAITYL MNRNEERVRK 
181:	SAETLLRVFD GLAEAMYLIV GGVMQYAPIG VFALIAYVMA EQGVRVVGPL AKVVGAVYTG 
241:	LFLQIVITYF ILLKVFGIDP IKFIRKAKDA MITAFVTRSS SGTLPVTMRV AEEEMGVDKG 
301:	IFSFTLPLGA TINMDGTALY QGVTVLFVAN AIGHPLTLGQ QLVVVLTAVL ASIGTAGVPG 
361:	AGAIMLAMVL QSVGLDLTPG SPVALAYAMI LGIDAILDMG RTMVNVTGDL AGTVIVAKTE 
421:	KELDESKWIS