SitesBLAST
Comparing 353923 BT4397 xylose/H+ symporter (NCBI ptt file) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
38% identity, 98% coverage: 3:455/460 of query aligns to 4:475/491 of P0AGF4
- F24 (= F23) mutation to A: Decreases xylose transport.
- G83 (= G76) mutation to A: Abolishes xylose transport.
- R133 (= R108) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E128) mutation to A: Abolishes xylose transport.
- R160 (= R135) mutation to A: Abolishes xylose transport.
- Q168 (= Q143) binding ; mutation to A: Abolishes xylose transport.
- Q288 (= Q274) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 274:275) binding
- Q289 (= Q275) mutation to A: Strongly decreases xylose transport.
- N294 (= N280) binding ; mutation to A: Abolishes xylose transport.
- Y298 (≠ N284) mutation to A: Abolishes xylose transport.
- N325 (= N311) mutation to A: No effect on xylose transport.
- G340 (= G326) mutation to A: Abolishes xylose transport.
- R341 (= R327) mutation R->A,W: Abolishes xylose transport.
- W392 (= W378) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E383) mutation to A: Abolishes xylose transport.
- R404 (= R390) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ L401) binding
- W416 (= W402) 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)
38% identity, 98% coverage: 4:455/460 of query aligns to 1:471/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
38% identity, 98% coverage: 4:455/460 of query aligns to 1:471/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
38% identity, 98% coverage: 4:455/460 of query aligns to 1:471/475 of 4gbyA
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
33% identity, 94% coverage: 26:458/460 of query aligns to 22:437/446 of A0A0H2VG78
- D22 (= D26) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R108) mutation to A: Loss of transport activity.
- I105 (≠ G111) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E128) mutation to A: Loss of transport activity.
- Q137 (= Q143) mutation to A: Loss of transport activity.
- Q250 (= Q274) mutation to A: Loss of transport activity.
- Q251 (= Q275) mutation to A: Loss of transport activity.
- N256 (= N280) mutation to A: Loss of transport activity.
- W357 (= W378) mutation to A: Loss of transport activity.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 99% coverage: 1:456/460 of query aligns to 23:477/509 of Q8VZR6
Sites not aligning to the query:
- 479:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 481:482 ER→AA: No effect on targeting.
- 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)
30% identity, 98% coverage: 8:456/460 of query aligns to 24:487/514 of Q9LT15
- F39 (= F23) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ W27) 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 (= E128) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q143) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I150) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q274) binding
- Q296 (= Q275) binding
- N301 (= N280) binding
- N332 (= N311) binding
- D344 (≠ E323) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W378) binding
- C449 (≠ F412) 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)
30% identity, 98% coverage: 8:456/460 of query aligns to 4:467/487 of 7aaqA
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)
28% identity, 99% coverage: 1:454/460 of query aligns to 1:463/492 of P11166
- N34 (≠ G31) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (vs. gap) 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 (vs. gap) to M: in EIG12; uncertain significance; decreased glucose transport; dbSNP:rs142986731
- M77 (≠ L62) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G76) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R108) 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 (= G112) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S119) binding
- P149 (= P131) to A: in EIG12; uncertain significance
- R153 (= R135) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity
- L169 (= L151) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (≠ G189) mutation to C: Strongly decreases glucose transport.
- L204 (≠ A201) mutation to C: Abolishes glucose transport.
- P205 (≠ C202) mutation to C: Abolishes glucose transport.
- R212 (= R209) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (≠ G215) to S: in EIG12; decreased glucose transport
- R223 (≠ K219) 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 (= S222) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (≠ G228) 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 (≠ M239) to V: in EIG12; decreased glucose transport
- A275 (≠ G267) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (= Q274) binding
- QQLS 282:285 (≠ QQWC 274:277) 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 (= G278) 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 (≠ Q287) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ Y295) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G308) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ A318) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (= E323) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R327) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G334) mutation to C: Strongly decreases glucose transport.
- W388 (= W378) binding
- N411 (≠ L401) Not glycosylated; binding ; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ W426) 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 (≠ K449) 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
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
30% identity, 98% coverage: 8:456/460 of query aligns to 9:472/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ W27), I90 (≠ M71), H94 (≠ Y75), V98 (≠ P79), F101 (≠ L82), N138 (≠ S119), P142 (= P123), N158 (≠ V139), F161 (≠ N142), Q162 (= Q143), I165 (= I146), D210 (≠ E206), G391 (= G374), P392 (= P375), W395 (= W378), M419 (vs. gap)
- binding beta-D-glucopyranose: Q280 (= Q274), N286 (= N280), M289 (≠ F283), G391 (= G374), W395 (= W378)
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)
29% identity, 99% coverage: 1:454/460 of query aligns to 1:463/492 of P17809
- N45 (≠ G42) 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.
P32037 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Mus musculus (Mouse) (see paper)
32% identity, 96% coverage: 15:456/460 of query aligns to 16:463/493 of P32037
- N43 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P38695 Probable glucose transporter HXT5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 98% coverage: 8:456/460 of query aligns to 85:547/592 of P38695
Sites not aligning to the query:
- 61 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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, 96% coverage: 15:456/460 of query aligns to 16:463/496 of P11169
- Q159 (= Q143) binding
- QLS 277:279 (≠ AVF 271:273) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 274:275) binding
- N286 (= N280) binding
- N315 (= N311) binding
- E378 (≠ A370) binding
- W386 (= W378) binding
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
29% identity, 96% coverage: 15:456/460 of query aligns to 13:460/468 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 (= F23), T25 (≠ W27), N29 (≠ G31), Q156 (= Q143), I163 (= I150), Q278 (= Q275), F286 (= F283), A308 (≠ T307), N312 (= N311), F374 (≠ Y369), E375 (≠ A370), N406 (≠ L401), W407 (= W402), N410 (≠ S405)
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
29% identity, 96% coverage: 15:456/460 of query aligns to 16:463/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q143), I166 (= I150), Q280 (= Q274), Q281 (= Q275), N286 (= N280), F377 (≠ Y369), W386 (= W378)
- binding alpha-D-glucopyranose: Q159 (= Q143), I162 (= I146), I166 (= I150), Q280 (= Q274), Q281 (= Q275), N286 (= N280), W386 (= W378)
5c65A Structure of the human glucose transporter glut3 / slc2a3
28% identity, 96% coverage: 15:456/460 of query aligns to 12:451/457 of 5c65A
- binding Octyl Glucose Neopentyl Glycol : L42 (vs. gap), L58 (vs. gap), F75 (≠ M66), S76 (≠ V67), L79 (≠ M70), R87 (≠ K78), L95 (≠ F86), L96 (≠ I87), L121 (≠ F109), P199 (≠ C202)
- binding cholesterol hemisuccinate: I270 (≠ V268), S396 (≠ A400), T399 (≠ V403)
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
29% identity, 96% coverage: 15:456/460 of query aligns to 14:461/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (≠ W27), A66 (= A57), S69 (vs. gap), Q157 (= Q143), I164 (= I150), Q278 (= Q274), Q279 (= Q275), N284 (= N280), N313 (= N311), F375 (≠ Y369), W384 (= W378), N411 (≠ S405), F412 (= F406), G415 (≠ T409)
5eqiA Human glut1 in complex with cytochalasin b (see paper)
29% identity, 94% coverage: 16:446/460 of query aligns to 11:447/447 of 5eqiA
5eqhA Human glut1 in complex with inhibitor (2~{s})-3-(2-bromophenyl)-2-[2- (4-methoxyphenyl)ethanoylamino]-~{n}-[(1~{s})-1- phenylethyl]propanamide (see paper)
29% identity, 94% coverage: 16:446/460 of query aligns to 11:447/447 of 5eqhA
Query Sequence
>353923 BT4397 xylose/H+ symporter (NCBI ptt file)
MKSYNKKFVYSICLVSAMGGLLFGYDWVVIGGAKPFYELYFGIADSPTMQGLAMSVALLG
CLIGAMVAGMMADRYGRKPLLLISAFIFLSSAYATGAFSVFSWFLAARFLGGIGIGIASG
LSPMYIAEVAPTSIRGKLVSLNQLTIVLGILGAQIANWLIAEPIPADFTPADICASWNGQ
MGWRWMFWGAAFPAAVFLLLACFIPESPRWLAMKGKREKAWSVLSRIGGNRYAEQELQMV
EQTSASKSEGGLKLLFSRPFRKVLVLGVIVAVFQQWCGTNVIFNYAQEIFQSAGYSLGDV
LFNIVVTGVANVIFTFVAIYTVERLGRRALMLLGAGGLAGIYLVLGTCYFFQVSGFFMVV
LVVLAIACYAMSLGPITWVLLAEIFPNRVRGVAMATCTFALWVGSFTLTYTFPLLNTALG
SYGTFWIYSAICVFGFLFFLRALPETKGKSLETLEKDLIK
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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