ID HXT1_PLAF7 Reviewed; 504 AA. AC Q7KWJ5; DT 29-MAY-2024, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 29-MAY-2024, entry version 141. DE RecName: Full=Hexose transporter 1 {ECO:0000303|PubMed:10066789}; DE Short=PfHT1 {ECO:0000303|PubMed:10066789, ECO:0000303|PubMed:10954735, ECO:0000303|PubMed:32860739}; GN Name=HT1 {ECO:0000305}; GN ORFNames=PF3D7_0204700 {ECO:0000312|EMBL:CZT98059.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450}; RN [1] {ECO:0000312|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450}; RX PubMed=9804551; DOI=10.1126/science.282.5391.1126; RA Gardner M.J., Tettelin H., Carucci D.J., Cummings L.M., Aravind L., RA Koonin E.V., Shallom S.J., Mason T., Yu K., Fujii C., Pederson J., Shen K., RA Jing J., Aston C., Lai Z., Schwartz D.C., Pertea M., Salzberg S.L., RA Zhou L., Sutton G.G., Clayton R., White O., Smith H.O., Fraser C.M., RA Adams M.D., Venter J.C., Hoffman S.L.; RT "Chromosome 2 sequence of the human malaria parasite Plasmodium RT falciparum."; RL Science 282:1126-1132(1998). RN [2] {ECO:0000312|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450}; RX PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S., RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium falciparum."; RL Nature 419:498-511(2002). RN [3] {ECO:0000305} RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RC STRAIN=3D7 {ECO:0000303|PubMed:10066789}; RX PubMed=10066789; DOI=10.1074/jbc.274.11.7272; RA Woodrow C.J., Penny J.I., Krishna S.; RT "Intraerythrocytic Plasmodium falciparum expresses a high affinity RT facilitative hexose transporter."; RL J. Biol. Chem. 274:7272-7277(1999). RN [4] {ECO:0000305} RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF GLN-169. RC STRAIN=3D7 {ECO:0000303|PubMed:10954735}; RX PubMed=10954735; DOI=10.1073/pnas.170153097; RA Woodrow C.J., Burchmore R.J., Krishna S.; RT "Hexose permeation pathways in Plasmodium falciparum-infected RT erythrocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9931-9936(2000). RN [5] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12238947; DOI=10.1042/bj20021189; RA Joet T., Holterman L., Stedman T.T., Kocken C.H., Van Der Wel A., RA Thomas A.W., Krishna S.; RT "Comparative characterization of hexose transporters of Plasmodium RT knowlesi, Plasmodium yoelii and Toxoplasma gondii highlights functional RT differences within the apicomplexan family."; RL Biochem. J. 368:923-929(2002). RN [6] {ECO:0000305} RP MUTAGENESIS OF 302-SER--LEU-304; SER-302 AND LEU-304. RX PubMed=12042321; DOI=10.1074/jbc.m204337200; RA Manning S.K., Woodrow C., Zuniga F.A., Iserovich P., Fischbarg J., RA Louw A.I., Krishna S.; RT "Mutational analysis of the hexose transporter of Plasmodium falciparum and RT development of a three-dimensional model."; RL J. Biol. Chem. 277:30942-30949(2002). RN [7] {ECO:0000305} RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF RP GLN-169. RX PubMed=12792024; DOI=10.1073/pnas.1330865100; RA Joet T., Eckstein-Ludwig U., Morin C., Krishna S.; RT "Validation of the hexose transporter of Plasmodium falciparum as a novel RT drug target."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7476-7479(2003). RN [8] {ECO:0007744|PDB:6M20, ECO:0007744|PDB:6M2L} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH BETA-D-GLUCOSE, RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, DISULFIDE BONDS, AND MUTAGENESIS OF LYS-51 AND ASP-447. RX PubMed=32860739; DOI=10.1016/j.cell.2020.08.015; RA Jiang X., Yuan Y., Huang J., Zhang S., Luo S., Wang N., Pu D., Zhao N., RA Tang Q., Hirata K., Yang X., Jiao Y., Sakata-Kato T., Wu J.W., Yan C., RA Kato N., Yin H., Yan N.; RT "Structural Basis for Blocking Sugar Uptake into the Malaria Parasite RT Plasmodium falciparum."; RL Cell 183:258-268.e12(2020). RN [9] {ECO:0007744|PDB:6RW3} RP X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 20-504 IN COMPLEX WITH RP ALPHA-D-GLUCOSE, FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ASN-48; LYS-51; RP HIS-168; GLN-169; GLN-305; GLN-306; ILE-310; ASN-311; VAL-314; SER-315; RP ASN-316; SER-317; ASN-318; GLU-319; ASN-341; PHE-403; ALA-404; TRP-412; RP ASN-435; TRP-436 AND ALA-439. RX PubMed=31996846; DOI=10.1038/s41586-020-1963-z; RA Qureshi A.A., Suades A., Matsuoka R., Brock J., McComas S.E., Nji E., RA Orellana L., Claesson M., Delemotte L., Drew D.; RT "The molecular basis for sugar import in malaria parasites."; RL Nature 578:321-325(2020). CC -!- FUNCTION: Sodium-independent facilitative hexose transporter CC (PubMed:10066789). Can transport D-glucose and D-fructose CC (PubMed:10066789, PubMed:10954735, PubMed:12238947, PubMed:12792024, CC PubMed:31996846, PubMed:32860739). Can transport D-mannose, D- CC galactose, D-xylose and D-glucosamine (PubMed:31996846). CC {ECO:0000269|PubMed:10066789, ECO:0000269|PubMed:10954735, CC ECO:0000269|PubMed:12238947, ECO:0000269|PubMed:12792024, CC ECO:0000269|PubMed:31996846, ECO:0000269|PubMed:32860739}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:10066789, CC ECO:0000269|PubMed:10954735, ECO:0000269|PubMed:12238947, CC ECO:0000269|PubMed:12792024, ECO:0000269|PubMed:31996846, CC ECO:0000269|PubMed:32860739}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60377; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372, CC ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:10954735, CC ECO:0000269|PubMed:12792024, ECO:0000269|PubMed:31996846}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60373; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915, CC ChEBI:CHEBI:4139; Evidence={ECO:0000269|PubMed:31996846}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34917; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-mannose(out) = D-mannose(in); Xref=Rhea:RHEA:78391, CC ChEBI:CHEBI:4208; Evidence={ECO:0000269|PubMed:31996846}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78392; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucosamine(out) = D-glucosamine(in); Xref=Rhea:RHEA:78423, CC ChEBI:CHEBI:58723; Evidence={ECO:0000269|PubMed:31996846}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78424; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-xylose(out) = D-xylose(in); Xref=Rhea:RHEA:78427, CC ChEBI:CHEBI:53455; Evidence={ECO:0000269|PubMed:31996846}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78428; CC Evidence={ECO:0000305}; CC -!- ACTIVITY REGULATION: Inhibited by cytochalasin B (PubMed:10066789, CC PubMed:31996846). Inhibited by compound 3361 (3-O-((undec-10-en)-1-yl)- CC D-glucose) (PubMed:12792024, PubMed:31996846, PubMed:32860739). CC Inhibited by compound HTI-1 (PubMed:32860739). CC {ECO:0000269|PubMed:10066789, ECO:0000269|PubMed:12792024, CC ECO:0000269|PubMed:31996846, ECO:0000269|PubMed:32860739}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.48 mM for D-glucose {ECO:0000269|PubMed:10066789}; CC KM=1.0 mM for D-glucose {ECO:0000269|PubMed:10954735}; CC KM=11.0 mM for D-fructose {ECO:0000269|PubMed:10954735}; CC KM=1.59 mM for D-glucose {ECO:0000269|PubMed:32860739}; CC KM=0.8 mM for D-glucose {ECO:0000269|PubMed:31996846}; CC KM=1.48 mM for D-mannose {ECO:0000269|PubMed:31996846}; CC KM=9.54 mM for D-galactose {ECO:0000269|PubMed:31996846}; CC KM=9.55 mM for D-fructose {ECO:0000269|PubMed:31996846}; CC KM=14.69 mM for D-glucosamine {ECO:0000269|PubMed:31996846}; CC Vmax=2.5 umol/min/mg enzyme for D-glucose CC {ECO:0000269|PubMed:32860739}; CC Vmax=21.11 umol/min/mg enzyme for D-glucose CC {ECO:0000269|PubMed:31996846}; CC Vmax=13.04 umol/min/mg enzyme for D-mannose CC {ECO:0000269|PubMed:31996846}; CC Vmax=50.29 umol/min/mg enzyme for D-galactose CC {ECO:0000269|PubMed:31996846}; CC Vmax=33.11 umol/min/mg enzyme for D-fructose CC {ECO:0000269|PubMed:31996846}; CC Vmax=8.72 umol/min/mg enzyme for D-glucosamine CC {ECO:0000269|PubMed:31996846}; CC Note=kcat is 19.35 sec(-1) for D-glucose transport (PubMed:31996846). CC kcat is 11.95 sec(-1) for D-mannose transport (PubMed:31996846). kcat CC is 46.10 sec(-1) for D-galactose transport (PubMed:31996846). kcat is CC 30.36 sec(-1) for D-fructose transport (PubMed:31996846). kcat is CC 8.01 sec(-1) for D-glucosamine transport (PubMed:31996846). CC {ECO:0000269|PubMed:31996846}; CC Temperature dependence: CC Active from 32 to 42 degrees Celsius (PubMed:12238947). Retains 50% CC of its maximal activity at 20 degrees Celsius (PubMed:12238947). CC {ECO:0000269|PubMed:12238947}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31996846}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10066789}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- DEVELOPMENTAL STAGE: Highly expressed at the small ring stage CC (PubMed:10066789). Levels decrease at 16 hours after erythrocyte CC invasion and increase again when parasites develop into more mature CC stages (PubMed:10066789). Expressed at intermediate levels in CC trophozoites and meronts (PubMed:10066789). CC {ECO:0000269|PubMed:10066789}. CC -!- MISCELLANEOUS: Experiments with hexose analogs indicate that hydroxyl CC groups at positions C-3 and C-4 of glucose are important for high CC affinity interactions with HT1. {ECO:0000269|PubMed:10066789, CC ECO:0000269|PubMed:10954735, ECO:0000269|PubMed:31996846}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar CC transporter (TC 2.A.1.1) family. {ECO:0000305}. CC -!- CAUTION: Contradicting results for mutagenesis of Gln-169 CC (PubMed:10954735, PubMed:31996846). In one study, mutagenesis of Gln- CC 169 resulted in the loss of both D-glucose and D-fructose transport CC activities (PubMed:31996846). In the other study, mutation at this CC position abolished D-fructose transport but not D-glucose transport CC activity (PubMed:10954735). {ECO:0000269|PubMed:10954735, CC ECO:0000269|PubMed:31996846}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LN999943; CZT98059.1; -; Genomic_DNA. DR RefSeq; XP_001349558.1; XM_001349522.1. DR PDB; 6M20; X-ray; 2.60 A; A/B/C/D=1-504. DR PDB; 6M2L; X-ray; 3.70 A; A/B=1-504. DR PDB; 6RW3; X-ray; 3.65 A; A/B/C/D=20-504. DR PDBsum; 6M20; -. DR PDBsum; 6M2L; -. DR PDBsum; 6RW3; -. DR AlphaFoldDB; Q7KWJ5; -. DR SMR; Q7KWJ5; -. DR STRING; 36329.Q7KWJ5; -. DR GuidetoPHARMACOLOGY; 3069; -. DR SwissPalm; Q7KWJ5; -. DR PaxDb; 5833-PFB0210c; -. DR EnsemblProtists; CZT98059; CZT98059; PF3D7_0204700. DR GeneID; 812640; -. DR KEGG; pfa:PF3D7_0204700; -. DR VEuPathDB; PlasmoDB:PF3D7_0204700; -. DR HOGENOM; CLU_001265_30_5_1; -. DR InParanoid; Q7KWJ5; -. DR OMA; WAITASF; -. DR OrthoDB; 509035at2759; -. DR PhylomeDB; Q7KWJ5; -. DR Reactome; R-PFA-189200; Cellular hexose transport. DR Reactome; R-PFA-196836; Vitamin C (ascorbate) metabolism. DR Reactome; R-PFA-422356; Regulation of insulin secretion. DR Reactome; R-PFA-5653890; Lactose synthesis. DR Reactome; R-PFA-6798695; Neutrophil degranulation. DR Reactome; R-PFA-8981373; Intestinal hexose absorption. DR Proteomes; UP000001450; Chromosome 2. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IEA:TreeGrafter. DR GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:GeneDB. DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:GeneDB. DR GO; GO:0015149; F:hexose transmembrane transporter activity; IDA:GeneDB. DR GO; GO:0070837; P:dehydroascorbic acid transport; IEA:TreeGrafter. DR GO; GO:0046323; P:glucose import; IEA:TreeGrafter. DR GO; GO:0008645; P:hexose transmembrane transport; IDA:GeneDB. DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central. DR CDD; cd17315; MFS_GLUT_like; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR045263; GLUT. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005828; MFS_sugar_transport-like. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR003663; Sugar/inositol_transpt. DR InterPro; IPR005829; Sugar_transporter_CS. DR NCBIfam; TIGR00879; SP; 1. DR PANTHER; PTHR23503:SF8; FACILITATED GLUCOSE TRANSPORTER PROTEIN 1; 1. DR PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1. DR Pfam; PF00083; Sugar_tr; 1. DR PRINTS; PR00171; SUGRTRNSPORT. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1. DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disulfide bond; Membrane; Reference proteome; KW Sugar transport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..504 FT /note="Hexose transporter 1" FT /id="PRO_0000460194" FT TOPO_DOM 1..29 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 30..50 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 51..78 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 100..104 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 126..129 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 130..150 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 151..165 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 166..186 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 187..207 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 208..228 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 229..293 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 294..314 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 315..331 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 332..352 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 353..358 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 359..379 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 380..392 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 393..413 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 414..429 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 430..450 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 451..455 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 456..476 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 477..504 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT BINDING 169 FT /ligand="alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:17925" FT /evidence="ECO:0000269|PubMed:31996846, FT ECO:0007744|PDB:6RW3" FT BINDING 169 FT /ligand="beta-D-glucose" FT /ligand_id="ChEBI:CHEBI:15903" FT /evidence="ECO:0000269|PubMed:32860739, FT ECO:0007744|PDB:6M20" FT BINDING 305 FT /ligand="alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:17925" FT /evidence="ECO:0000269|PubMed:31996846, FT ECO:0007744|PDB:6RW3" FT BINDING 305 FT /ligand="beta-D-glucose" FT /ligand_id="ChEBI:CHEBI:15903" FT /evidence="ECO:0000269|PubMed:32860739, FT ECO:0007744|PDB:6M20" FT BINDING 306 FT /ligand="alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:17925" FT /evidence="ECO:0000269|PubMed:31996846, FT ECO:0007744|PDB:6RW3" FT BINDING 311 FT /ligand="alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:17925" FT /evidence="ECO:0000269|PubMed:31996846, FT ECO:0007744|PDB:6RW3" FT BINDING 311 FT /ligand="beta-D-glucose" FT /ligand_id="ChEBI:CHEBI:15903" FT /evidence="ECO:0000269|PubMed:32860739, FT ECO:0007744|PDB:6M20" FT BINDING 341 FT /ligand="beta-D-glucose" FT /ligand_id="ChEBI:CHEBI:15903" FT /evidence="ECO:0000269|PubMed:32860739, FT ECO:0007744|PDB:6M20" FT BINDING 412 FT /ligand="alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:17925" FT /evidence="ECO:0000269|PubMed:31996846, FT ECO:0007744|PDB:6RW3" FT DISULFID 61..70 FT /evidence="ECO:0000269|PubMed:32860739, FT ECO:0007744|PDB:6M20, ECO:0007744|PDB:6M2L" FT MUTAGEN 48 FT /note="N->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 51 FT /note="K->A: Reduces D-glucose and D-fructose transport FT activity. Reduces susceptibility to inhibition by compound FT HTI-1. Reduces susceptibility to inhibition by compound FT HTI-1; when associated with A-447." FT /evidence="ECO:0000269|PubMed:31996846, FT ECO:0000269|PubMed:32860739" FT MUTAGEN 51 FT /note="K->Q: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 168 FT /note="H->N: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 169 FT /note="Q->A: Abolishes D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 169 FT /note="Q->N: In one study, shown to abolish D-glucose and FT D-fructose transport activity. In another study, shown to FT abolish D-fructose transport with no significant effects on FT D-glucose uptake and affinity. Reduces susceptibility to FT inhibition by compound 3361." FT /evidence="ECO:0000269|PubMed:10954735, FT ECO:0000269|PubMed:12792024, ECO:0000269|PubMed:31996846" FT MUTAGEN 302..304 FT /note="SGL->AGT: No significant effects on affinity for D- FT glucose and D-fructose." FT /evidence="ECO:0000269|PubMed:12042321" FT MUTAGEN 302 FT /note="S->A: No significant effects on affinity for D- FT glucose and D-fructose." FT /evidence="ECO:0000269|PubMed:12042321" FT MUTAGEN 304 FT /note="L->T: No significant effects on affinity for D- FT glucose and D-fructose." FT /evidence="ECO:0000269|PubMed:12042321" FT MUTAGEN 305 FT /note="Q->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 306 FT /note="Q->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 310 FT /note="I->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 311 FT /note="N->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 314 FT /note="V->F: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 315 FT /note="S->A: No significant effects on D-glucose and D- FT fructose transport activities. Reduces turnover number for FT D-glucose." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 315 FT /note="S->Y: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 316 FT /note="N->A,Y: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 317 FT /note="S->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 318 FT /note="N->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 319 FT /note="E->A: No significant effects on D-glucose and D- FT fructose transport activities. Reduces turnover number for FT D-glucose." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 341 FT /note="N->A: Abolishes D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 403 FT /note="F->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 404 FT /note="A->E: Modestly reduces D-glucose and D-fructose FT transport activities and affinities for these substrates." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 412 FT /note="W->A: Reduces D-fructose transport with no FT significant effect on D-glucose uptake." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 435 FT /note="N->A: Reduces D-fructose transport with no FT significant effect on D-glucose uptake." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 436 FT /note="W->A: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 439 FT /note="A->N: Reduces D-glucose and D-fructose transport FT activity." FT /evidence="ECO:0000269|PubMed:31996846" FT MUTAGEN 447 FT /note="D->A: Reduces susceptibility to inhibition by FT compound HTI-1; when associated with A-51." FT /evidence="ECO:0000269|PubMed:32860739" SQ SEQUENCE 504 AA; 56417 MW; 79AE4CB7D514FA58 CRC64; MTKSSKDICS ENEGKKNGKS GFFSTSFKYV LSACIASFIF GYQVSVLNTI KNFIVVEFEW CKGEKDRLNC SNNTIQSSFL LASVFIGAVL GCGFSGYLVQ FGRRLSLLII YNFFFLVSIL TSITHHFHTI LFARLLSGFG IGLVTVSVPM YISEMTHKDK KGAYGVMHQL FITFGIFVAV MLGLAMGEGP KADSTEPLTS FAKLWWRLMF LFPSVISLIG ILALVVFFKE ETPYFLFEKG RIEESKNILK KIYETDNVDE PLNAIKEAVE QNESAKKNSL SLLSALKIPS YRYVIILGCL LSGLQQFTGI NVLVSNSNEL YKEFLDSHLI TILSVVMTAV NFLMTFPAIY IVEKLGRKTL LLWGCVGVLV AYLPTAIANE INRNSNFVKI LSIVATFVMI ISFAVSYGPV LWIYLHEMFP SEIKDSAASL ASLVNWVCAI IVVFPSDIII KKSPSILFIV FSVMSILTFF FIFFFIKETK GGEIGTSPYI TMEERQKHMT KSVV //