Oxalate:formate antiporter (OFA) and similar proteins of the Major Facilitator Superfamily of transporters; This subfamily is composed of Oxalobacter formigenes oxalate:formate antiporter (OFA or OxlT) and similar proteins. O. formigenes, a commensal found in the gut of animals and humans, plays an important role in clearing dietary oxalate from the intestinal tract, which is carried out by OFA/OxlT, an anion transporter that facilitates the exchange of divalent oxalate with monovalent formate, the product of oxalate decarboxylation. This exchange generates an electrochemical proton gradient and is the source of energy for ATP synthesis in this cell. The OFA-like subfamily belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968930  94 LGFTIGSFVLSATTLPLGILMDRFGPRPVRLVGSACFTASCTLMALASRdvealSPLIFLALSlnGFGGI 163
Cdd:cd17353   42 LAFTLTIVFLAISAPFAGRLVDRGGPRKAILIGGILFGLGFILSAFAIS-----LPLLFLGYG--VLGGI 104

Oxalate:formate antiporter (OFA) and similar proteins of the Major Facilitator Superfamily of transporters; This subfamily is composed of Oxalobacter formigenes oxalate:formate antiporter (OFA or OxlT) and similar proteins. O. formigenes, a commensal found in the gut of animals and humans, plays an important role in clearing dietary oxalate from the intestinal tract, which is carried out by OFA/OxlT, an anion transporter that facilitates the exchange of divalent oxalate with monovalent formate, the product of oxalate decarboxylation. This exchange generates an electrochemical proton gradient and is the source of energy for ATP synthesis in this cell. The OFA-like subfamily belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968930  94 LGFTIGSFVLSATTLPLGILMDRFGPRPVRLVGSACFTASCTLMALASRdvealSPLIFLALSlnGFGGI 163
Cdd:cd17353   42 LAFTLTIVFLAISAPFAGRLVDRGGPRKAILIGGILFGLGFILSAFAIS-----LPLLFLGYG--VLGGI 104

Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968930  96 FTIGSFVLSATTLPLGILMDRFGPRPVRLVGSACFTASCTLMALASrdvealSPLIFLALS-LNGFGGICLTFTSLTLIY 174
Cdd:COG2814   51 VTAYLLGAALGAPLAGRLADRFGRRRVLLLGLLLFALGSLLCALAP------SLWLLLAARfLQGLGAGALFPAALALIA 124

                         90       100
                 ....*....|....*....|
gi 767968930 175 DA------GVAFVVIMFTWS 188
Cdd:COG2814  125 DLvpperrGRALGLLGAGLG 144

MFS-type transporter YcxA and similar proteins of the Major Facilitator Superfamily of transporters; This group is composed of uncharacterized bacterial MFS-type transporters including Bacillus subtilis YcxA and YbfB. YcxA has been shown to facilitate the export of surfactin in B. subtilis. The YcxA-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968930  94 LGFTIGsFVLSATTLPL-GILMDRFGPRPVRLVGSACFTASCTLMALASRDVE--ALSPLIFLALSLNGFGGICLTFTSL 170
Cdd:cd17355   42 LAFTVG-LLAFGLAQPFvGRLLDRFGPRRVMLLGLLLLAAGLVLLALATSLWQlyLLWGLLGGGGAGTLAAVAFATVAAW 120

                         90       100
                 ....*....|....*....|....*.
gi 767968930 171 TLIYDAGVAFvVIMFTWSGLACLIFL 196
Cdd:cd17355  121 WFERRRGLAL-GILTAGGGLGSLVFL 145

Sugar phosphate permease [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968930  89 DEMLNLGFTIGSFVLSATTLPLGILMDRFGPRPVRLVGSACFTASCTLMALASrdvealSPLIFLAL-SLNGFG 161
Cdd:COG2271   44 AAQLGLLASAFFLGYALGQIPAGLLADRFGRRRVLAIGLLLWGLATLLFGFAT------SFWQLLLLrFLLGLG 111

Fucose permease [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968930  91 MLNLGFTIGSFVLSattLPLGILMDRFGPRPVRLVGSACFTASCTLMALASRdvealSPLIFLALSLNGFGG 162
Cdd:COG0738   47 LLLFAFFLGYLLAS---LPAGRLIDRFGYKRGLLLGLLLMALGLLLFALAPS-----YPLLLLALFLLGLGL 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968930  91 MLNLGFTIGSFVLSATTLPLGILMDRFGPRPVRLVGSACFTASCTLMALAsrdveALSPLIFLALSLNGFGGICLTFTSL 170
Cdd:cd06174   32 QLGLLFALFSLGYALLQPLAGLLADRFGRRPVLLLGLLLFALGALLFAFA-----PSFWLLLLGRFLLGLGSGLIDPAVL 106

                 ....*
gi 767968930 171 TLIYD 175
Cdd:cd06174  107 ALIAD 111