SitesBLAST
Comparing 18059 b4031 D-xylose transporter (NCBI) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:491/491 of query aligns to 1:491/491 of P0AGF4
- F24 (= F24) mutation to A: Decreases xylose transport.
- G83 (= G83) mutation to A: Abolishes xylose transport.
- R133 (= R133) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E153) mutation to A: Abolishes xylose transport.
- R160 (= R160) mutation to A: Abolishes xylose transport.
- Q168 (= Q168) binding ; mutation to A: Abolishes xylose transport.
- Q288 (= Q288) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 288:289) binding
- Q289 (= Q289) mutation to A: Strongly decreases xylose transport.
- N294 (= N294) binding ; mutation to A: Abolishes xylose transport.
- Y298 (= Y298) mutation to A: Abolishes xylose transport.
- N325 (= N325) mutation to A: No effect on xylose transport.
- G340 (= G340) mutation to A: Abolishes xylose transport.
- R341 (= R341) mutation R->A,W: Abolishes xylose transport.
- W392 (= W392) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E397) mutation to A: Abolishes xylose transport.
- R404 (= R404) mutation to A: Strongly decreases xylose transport.
- Q415 (= Q415) binding
- W416 (= W416) mutation to A: Strongly decreases xylose transport.
4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
100% identity, 97% coverage: 5:479/491 of query aligns to 1:475/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
100% identity, 97% coverage: 5:479/491 of query aligns to 1:475/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
100% identity, 97% coverage: 5:479/491 of query aligns to 1:475/475 of 4gbyA
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
30% identity, 87% coverage: 58:486/491 of query aligns to 45:446/446 of A0A0H2VG78
- R102 (= R133) mutation to A: Loss of transport activity.
- I105 (≠ G136) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E153) mutation to A: Loss of transport activity.
- Q137 (= Q168) mutation to A: Loss of transport activity.
- Q250 (= Q288) mutation to A: Loss of transport activity.
- Q251 (= Q289) mutation to A: Loss of transport activity.
- N256 (= N294) mutation to A: Loss of transport activity.
- W357 (= W392) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 22 D→N: Affects symport activity. May function as an uniporter.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 97% coverage: 5:481/491 of query aligns to 26:482/509 of Q8VZR6
- ER 481:482 (≠ PE 480:481) mutation to AA: No effect on targeting.
Sites not aligning to the query:
- 479:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 500:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 502:504 mutation LLE->AAA,SSS: Leads to plasma membrane relocalization.
Q9LT15 Sugar transport protein 10; AtSTP10; D-glucose-H(+) symport protein STP10; D-glucose-proton symporter STP10; Hexose transporter 10 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 96% coverage: 7:479/491 of query aligns to 22:490/514 of Q9LT15
- F39 (= F24) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ T28) mutation to A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- C77 (vs. gap) modified: Disulfide link with 449; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- E162 (= E153) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q168) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (≠ Q175) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q288) binding
- Q296 (= Q289) binding
- N301 (= N294) binding
- N332 (= N325) binding
- D344 (= D337) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W392) binding
- C449 (≠ A437) modified: Disulfide link with 77; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
7aaqA Sugar/h+ symporter stp10 in outward occluded conformation (see paper)
29% identity, 96% coverage: 7:479/491 of query aligns to 2:470/487 of 7aaqA
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
29% identity, 96% coverage: 7:479/491 of query aligns to 7:475/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ T28), I90 (≠ C78), H94 (≠ F82), V98 (≠ D86), F101 (≠ K89), N138 (≠ S144), P142 (= P148), N158 (≠ V164), F161 (≠ N167), Q162 (= Q168), I165 (= I171), D210 (≠ E222), G391 (= G388), P392 (= P389), W395 (= W392), M419 (≠ W416)
- binding beta-D-glucopyranose: Q280 (= Q288), N286 (= N294), M289 (≠ L297), G391 (= G388), W395 (= W392)
P32037 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Mus musculus (Mouse) (see paper)
30% identity, 99% coverage: 2:489/491 of query aligns to 3:476/493 of P32037
- N43 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 76% coverage: 5:378/491 of query aligns to 23:380/580 of Q9C757
Sites not aligning to the query:
- 399 C→A: Strongly decreased nickel inhibition; when associated with A-402, A-410 and A-413.; C→S: No effect on inostol transport or nickel inhibition. No effect on inostol transport or nickel inhibition; when associated with S-410.
- 402 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-410 and A-413.
- 410 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-413.; C→S: No effect on inostol transport or nickel inhibition; when associated with S-399.
- 413 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-410.
P17809 Solute carrier family 2, facilitated glucose transporter member 1; Glucose transporter type 1, erythrocyte/brain; GLUT-1; GT1 from Mus musculus (Mouse) (see 3 papers)
28% identity, 94% coverage: 17:476/491 of query aligns to 19:465/492 of P17809
- N45 (≠ V43) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Sites not aligning to the query:
- 485 P→L: Lethality immediately after birth in knockin mice; caused by creation of a dileucine internalization motif that promotes mislocalization of the protein.
P11166 Solute carrier family 2, facilitated glucose transporter member 1; Glucose transporter type 1, erythrocyte/brain; GLUT-1; HepG2 glucose transporter from Homo sapiens (Human) (see 23 papers)
29% identity, 94% coverage: 17:476/491 of query aligns to 19:465/492 of P11166
- N34 (≠ S32) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (≠ V43) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to T: Loss of glycosylation site.
- R51 (vs. gap) to H: in EIG12; uncertain significance; dbSNP:rs201815571
- T60 (≠ A52) to M: in EIG12; uncertain significance; decreased glucose transport; dbSNP:rs142986731
- M77 (≠ I69) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G83) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R133) to C: in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity; dbSNP:rs80359818; to H: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity; dbSNP:rs80359816
- G130 (= G137) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S144) binding
- P149 (= P156) to A: in EIG12; uncertain significance
- R153 (= R160) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity
- L169 (= L176) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (≠ S205) mutation to C: Strongly decreases glucose transport.
- L204 (= L217) mutation to C: Abolishes glucose transport.
- P205 (≠ Y218) mutation to C: Abolishes glucose transport.
- R212 (= R225) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (= R230) to S: in EIG12; decreased glucose transport
- R223 (≠ Q235) to P: in EIG12; mild phenotype; reduced transporter activity; impaired phosphorylation by PKC; dbSNP:rs397514564; to Q: in EIG12; uncertain significance; no effect on glucose transport; impaired phosphorylation by PKC; dbSNP:rs397514564; to W: in GLUT1DS1; impaired phosphorylation by PKC; dbSNP:rs796053248
- S226 (≠ G238) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (≠ M244) to C: in EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type; dbSNP:rs387907313
- E243 (= E255) to V: in EIG12; decreased glucose transport
- A275 (≠ G281) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (= Q288) binding
- QQLS 282:285 (≠ QQFV 288:291) natural variant: Missing (in GLUT1DS2; accompanied by hemolytic anemia and altered erythrocyte ion concentrations; the mutation decreases glucose transport and causes a cation leak that alteres intracellular concentrations of sodium potassium and calcium)
- G286 (= G292) to D: in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage; dbSNP:rs864309514
- T295 (≠ P301) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ A309) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G322) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ A332) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ D337) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R341) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G348) mutation to C: Strongly decreases glucose transport.
- W388 (= W392) binding
- N411 (≠ Q415) Not glycosylated; binding ; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ W446) natural variant: Missing (in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage)
- R458 (≠ K469) to W: in EIG12; decreased glucose transport; dbSNP:rs13306758
Sites not aligning to the query:
- 485 P → L: in GLUT1DS1; creates a dileucine internalization motif that promotes recruitment of clathrin and mislocalization of the protein to endocytic compartments
5c65A Structure of the human glucose transporter glut3 / slc2a3
29% identity, 97% coverage: 4:479/491 of query aligns to 1:454/457 of 5c65A
- binding Octyl Glucose Neopentyl Glycol : L42 (vs. gap), L58 (= L56), F75 (≠ A73), S76 (≠ L74), L79 (≠ Y77), R87 (= R85), L95 (≠ V93), L96 (= L94), L121 (≠ I134), P199 (≠ Y218)
- binding cholesterol hemisuccinate: I270 (≠ V282), S396 (≠ A414), T399 (≠ L417)
P11169 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Homo sapiens (Human) (see paper)
29% identity, 99% coverage: 1:488/491 of query aligns to 1:475/496 of P11169
- Q159 (= Q168) binding
- QLS 277:279 (≠ SIF 285:287) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 288:289) binding
- N286 (= N294) binding
- N315 (= N325) binding
- E378 (≠ A384) binding
- W386 (= W392) binding
P38695 Probable glucose transporter HXT5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 95% coverage: 15:479/491 of query aligns to 91:550/592 of P38695
Sites not aligning to the query:
- 61 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
30% identity, 98% coverage: 1:479/491 of query aligns to 1:466/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q168), I166 (≠ Q175), Q280 (= Q288), Q281 (= Q289), N286 (= N294), F377 (= F383), W386 (= W392)
- binding alpha-D-glucopyranose: Q159 (= Q168), I162 (= I171), I166 (≠ Q175), Q280 (= Q288), Q281 (= Q289), N286 (= N294), W386 (= W392)
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
29% identity, 97% coverage: 4:479/491 of query aligns to 3:464/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (= T28), A66 (= A62), S69 (≠ L65), Q157 (= Q168), I164 (≠ Q175), Q278 (= Q288), Q279 (= Q289), N284 (= N294), N313 (= N325), F375 (= F383), W384 (= W392), N411 (= N419), F412 (≠ Y420), G415 (≠ S423)
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
29% identity, 97% coverage: 4:479/491 of query aligns to 2:463/468 of 7spsA
- binding methyl N-[(2-{4-[4-(5-fluoro-2-methoxyphenyl)piperazin-1-yl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}phenyl)methyl]-beta-alaninate: F21 (= F24), T25 (= T28), N29 (≠ S32), Q156 (= Q168), I163 (≠ Q175), Q278 (= Q289), F286 (≠ L297), A308 (≠ V321), N312 (= N325), F374 (= F383), E375 (≠ A384), N406 (≠ Q415), W407 (= W416), N410 (= N419)
7sptA Crystal structure of exofacial state human glucose transporter glut3 (see paper)
29% identity, 98% coverage: 1:479/491 of query aligns to 1:466/470 of 7sptA
Query Sequence
>18059 b4031 D-xylose transporter (NCBI)
MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFC
VASALIGCIIGGALGGYCSNRFGRRDSLKIAAVLFFISGVGSAWPELGFTSINPDNTVPV
YLAGYVPEFVIYRIIGGIGVGLASMLSPMYIAELAPAHIRGKLVSFNQFAIIFGQLLVYC
VNYFIARSGDASWLNTDGWRYMFASECIPALLFLMLLYTVPESPRWLMSRGKQEQAEGIL
RKIMGNTLATQAVQEIKHSLDHGRKTGGRLLMFGVGVIVIGVMLSIFQQFVGINVVLYYA
PEVFKTLGASTDIALLQTIIVGVINLTFTVLAIMTVDKFGRKPLQIIGALGMAIGMFSLG
TAFYTQAPGIVALLSMLFYVAAFAMSWGPVCWVLLSEIFPNAIRGKALAIAVAAQWLANY
FVSWTFPMMDKNSWLVAHFHNGFSYWIYGCMGVLAALFMWKFVPETKGKTLEELEALWEP
ETKKTQQTATL
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory