Sodium-dependent glucose transporter 1, also called Major facilitator superfamily domain-containing protein 4B
Sodium-dependent glucose transporter 1 (NaGLT1) is also called major facilitator superfamily domain-containing protein 4B (MFSD4B). NaGLT1 is a primary fructose transporter in rat renal brush-border membranes. It also facilitates sodium-independent urea uptake in assays performed on Xenopus oocytes. NaGLT1/MFSD4B belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Feature 1:putative chemical substrate binding pocket [chemical binding site]
Evidence:
Comment:based on the structures of MFS transporters with bound substrates, substrate analogs, and/or inhibitors
Comment:since MFS proteins facilitate the transport of many different substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides, the residues involved in substrate binding may not be strictly conserved among superfamily members
Comment:the substrate binding site or translocation pore has access to both sides of the membrane in an alternating fashion through a conformational change of the MFS transporter
Jiyao W et al.(2023). "The conserved domain database in 2023.",