major facilitator superfamily (MFS) transporter facilitates the transport across cytoplasmic or internal membranes of one or more from a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
86-566
2.37e-110
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.
The actual alignment was detected with superfamily member pfam13000:
Pssm-ID: 475125 [Multi-domain] Cd Length: 543 Bit Score: 340.49 E-value: 2.37e-110
Acetyl-coenzyme A transporter 1; The mouse Acatn is a 61 kDa hydrophobic protein with six to ...
86-566
2.37e-110
Acetyl-coenzyme A transporter 1; The mouse Acatn is a 61 kDa hydrophobic protein with six to 10 transmembrane domains. It appears to promote 9-O-acetylation in gangliosides.
Pssm-ID: 372424 [Multi-domain] Cd Length: 543 Bit Score: 340.49 E-value: 2.37e-110
Major facilitator superfamily domain containing 3 protein; Major facilitator superfamily ...
86-494
1.45e-34
Major facilitator superfamily domain containing 3 protein; Major facilitator superfamily domain containing 3 protein (MFSD3) is a predicted acetyl-CoA transporter. As an atypical putative membrane-bound solute carrier (SLC), MFSD3 is most likely to be functionally active in the plasma membrane and not in any intracellular organelles. MFSD3 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 341038 [Multi-domain] Cd Length: 386 Bit Score: 134.66 E-value: 1.45e-34
Acetyl-coenzyme A transporter 1; The mouse Acatn is a 61 kDa hydrophobic protein with six to ...
86-566
2.37e-110
Acetyl-coenzyme A transporter 1; The mouse Acatn is a 61 kDa hydrophobic protein with six to 10 transmembrane domains. It appears to promote 9-O-acetylation in gangliosides.
Pssm-ID: 372424 [Multi-domain] Cd Length: 543 Bit Score: 340.49 E-value: 2.37e-110
Major facilitator superfamily domain containing 3 protein; Major facilitator superfamily ...
86-494
1.45e-34
Major facilitator superfamily domain containing 3 protein; Major facilitator superfamily domain containing 3 protein (MFSD3) is a predicted acetyl-CoA transporter. As an atypical putative membrane-bound solute carrier (SLC), MFSD3 is most likely to be functionally active in the plasma membrane and not in any intracellular organelles. MFSD3 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 341038 [Multi-domain] Cd Length: 386 Bit Score: 134.66 E-value: 1.45e-34
AmpG and similar transporters of the Major Facilitator Superfamily; AmpG acts as an inner ...
86-481
4.37e-17
AmpG and similar transporters of the Major Facilitator Superfamily; AmpG acts as an inner membrane permease in the beta-lactamase induction system and in peptidoglycan recycling. It transports meuropeptide from the periplasm into the cytosol in gram-negative bacteria, which is essential for the induction of the ampC encoding beta-lactamase. The AmpG family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 341039 [Multi-domain] Cd Length: 387 Bit Score: 83.42 E-value: 4.37e-17
siderophore transporter, RhtX/FptX family; RhtX from Sinorhizobium meliloti 2011 and FptX from ...
86-502
9.47e-16
siderophore transporter, RhtX/FptX family; RhtX from Sinorhizobium meliloti 2011 and FptX from Pseudomonas aeruginosa appear to be single polypeptide transporters, from the major facilitator family (see pfam07690) for import of siderophores as a means to import iron. This function was suggested by proximity to siderophore biosynthesis genes and then confirmed by study of knockout and heterologous expression phenotypes. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131765 Cd Length: 390 Bit Score: 79.17 E-value: 9.47e-16
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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