SitesBLAST
Comparing WP_039652874.1 NCBI__GCF_000816635.1:WP_039652874.1 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)
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
41% identity, 93% coverage: 24:446/455 of query aligns to 22:441/446 of A0A0H2VG78
- D22 (= D24) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R104) mutation to A: Loss of transport activity.
- I105 (≠ L107) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E124) mutation to A: Loss of transport activity.
- Q137 (= Q139) mutation to A: Loss of transport activity.
- Q250 (= Q253) mutation to A: Loss of transport activity.
- Q251 (= Q254) mutation to A: Loss of transport activity.
- N256 (= N259) mutation to A: Loss of transport activity.
- W357 (= W362) mutation to A: Loss of transport activity.
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)
34% identity, 93% coverage: 15:438/455 of query aligns to 33:485/514 of Q9LT15
- F39 (= F21) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ I25) 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 (= E124) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q139) binding beta-D-glucose; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (≠ M146) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q253) binding beta-D-glucose
- Q296 (= Q254) binding beta-D-glucose
- N301 (= N259) binding beta-D-glucose
- N332 (≠ F290) binding beta-D-glucose
- D344 (= D302) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W362) binding beta-D-glucose
- C449 (≠ E401) 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)
34% identity, 93% coverage: 14:438/455 of query aligns to 12:465/487 of 7aaqA
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
33% identity, 93% coverage: 14:438/455 of query aligns to 17:470/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ I25), I90 (≠ A68), H94 (≠ F71), V98 (≠ R75), F101 (≠ M78), N138 (≠ S115), P142 (= P119), N158 (≠ S135), F161 (≠ N138), Q162 (= Q139), I165 (= I142), D210 (≠ E186), G391 (≠ A358), P392 (≠ A359), W395 (= W362), M419 (≠ W386)
- binding beta-D-glucopyranose: Q280 (= Q253), N286 (= N259), M289 (≠ F262), G391 (≠ A358), W395 (= W362)
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
31% identity, 97% coverage: 10:449/455 of query aligns to 13:484/491 of P0AGF4
- F24 (= F21) mutation to A: Decreases xylose transport.
- G83 (= G72) mutation to A: Abolishes xylose transport.
- R133 (= R104) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E124) mutation to A: Abolishes xylose transport.
- R160 (= R131) mutation to A: Abolishes xylose transport.
- Q168 (= Q139) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Q288 (= Q253) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 253:254) binding beta-D-xylose
- Q289 (= Q254) mutation to A: Strongly decreases xylose transport.
- N294 (= N259) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Y298 (= Y263) mutation to A: Abolishes xylose transport.
- N325 (≠ F290) mutation to A: No effect on xylose transport.
- G340 (≠ K305) mutation to A: Abolishes xylose transport.
- R341 (= R306) mutation R->A,W: Abolishes xylose transport.
- W392 (= W362) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- E397 (= E367) mutation to A: Abolishes xylose transport.
- R404 (= R374) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ N385) binding beta-D-xylose
- W416 (= W386) mutation to A: Strongly decreases xylose transport.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 96% coverage: 17:452/455 of query aligns to 41:489/509 of Q8VZR6
- ER 481:482 (= ER 444:445) 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.
4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
32% identity, 95% coverage: 10:439/455 of query aligns to 9:471/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
32% identity, 95% coverage: 10:439/455 of query aligns to 9:471/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
32% identity, 95% coverage: 10:439/455 of query aligns to 9:471/475 of 4gbyA
9g11A Sugar/h+ symporter stp6 in inward occluded conformation with glucose bound
32% identity, 95% coverage: 15:444/455 of query aligns to 13:468/476 of 9g11A
- binding beta-D-glucopyranose: Q275 (= Q254), I279 (≠ A258), N280 (= N259), W387 (= W362)
- binding cholesterol hemisuccinate: L313 (= L292), A314 (= A293), R324 (= R303), F329 (≠ S308), Q333 (≠ S312), Q333 (≠ S312), H337 (≠ G316), H337 (≠ G316)
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
32% identity, 96% coverage: 3:438/455 of query aligns to 2:459/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (≠ I25), A66 (≠ G52), S69 (vs. gap), Q157 (= Q139), I164 (≠ M146), Q278 (= Q253), Q279 (= Q254), N284 (= N259), N313 (≠ F290), F375 (≠ Y353), W384 (= W362), N411 (= N389), F412 (≠ I390), G415 (≠ A393)
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
32% identity, 96% coverage: 3:438/455 of query aligns to 4:461/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q139), I166 (≠ M146), Q280 (= Q253), Q281 (= Q254), N286 (= N259), F377 (≠ Y353), W386 (= W362)
- binding alpha-D-glucopyranose: Q159 (= Q139), I162 (= I142), I166 (≠ M146), Q280 (= Q253), Q281 (= Q254), N286 (= N259), W386 (= W362)
P11169 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Homo sapiens (Human) (see paper)
32% identity, 96% coverage: 3:438/455 of query aligns to 4:461/496 of P11169
- Q159 (= Q139) binding D-glucose
- QLS 277:279 (≠ TLL 250:252) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 253:254) binding D-glucose
- N286 (= N259) binding D-glucose
- N315 (≠ F290) binding D-glucose
- E378 (≠ A354) binding D-glucose
- W386 (= W362) binding D-glucose
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
32% identity, 96% coverage: 3:438/455 of query aligns to 1:458/468 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 (= F21), T25 (≠ I25), N29 (= N29), Q156 (= Q139), I163 (≠ M146), Q278 (= Q254), F286 (= F262), A308 (≠ I286), N312 (≠ F290), F374 (≠ Y353), E375 (≠ A354), N406 (= N385), W407 (= W386), N410 (= N389)
7sptA Crystal structure of exofacial state human glucose transporter glut3 (see paper)
32% identity, 96% coverage: 3:438/455 of query aligns to 4:461/470 of 7sptA
P32037 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Mus musculus (Mouse) (see paper)
31% identity, 96% coverage: 4:438/455 of query aligns to 5:461/493 of P32037
- N43 (≠ T38) modified: carbohydrate, N-linked (GlcNAc...) asparagine
5c65A Structure of the human glucose transporter glut3 / slc2a3
32% identity, 96% coverage: 4:438/455 of query aligns to 1:449/457 of 5c65A
- binding Octyl Glucose Neopentyl Glycol : L42 (vs. gap), L58 (vs. gap), F75 (≠ S62), S76 (≠ L63), L79 (≠ S66), R87 (= R74), L95 (≠ V85), L96 (≠ I86), L121 (≠ I105), P199 (≠ F182)
- binding cholesterol hemisuccinate: I270 (≠ C247), S396 (≠ V384), T399 (≠ F387)
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)
32% identity, 96% coverage: 3:440/455 of query aligns to 6:465/492 of P17809
- N45 (vs. gap) 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)
32% identity, 96% coverage: 3:440/455 of query aligns to 6:465/492 of P11166
- N34 (= N29) 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 (= M58) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G72) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R104) 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 (= G108) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S115) binding cytochalasin B
- P149 (= P127) to A: in EIG12; uncertain significance
- R153 (= R131) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity; dbSNP:rs1643479461
- L169 (= L147) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (≠ G169) mutation to C: Strongly decreases glucose transport.
- L204 (≠ T181) mutation to C: Abolishes glucose transport.
- P205 (≠ F182) mutation to C: Abolishes glucose transport.
- R212 (= R189) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (≠ K196) to S: in EIG12; decreased glucose transport
- R223 (≠ L199) 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 (≠ K202) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (= R208) 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 (= E219) to V: in EIG12; decreased glucose transport; dbSNP:rs2124449030
- A275 (= A245) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (= Q253) binding cytochalasin B
- QQLS 282:285 (≠ QQIQ 253:256) 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 (= G257) 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 (≠ S266) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ G274) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G287) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ T297) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ D302) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R306) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G313) mutation to C: Strongly decreases glucose transport.
- W388 (= W362) binding cytochalasin B
- N411 (= N385) Not glycosylated; binding cytochalasin B; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ F410) 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 (≠ K433) 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; dbSNP:rs1159593580
P39003 High-affinity hexose transporter HXT6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 95% coverage: 15:444/455 of query aligns to 73:530/570 of P39003
Sites not aligning to the query:
- 560 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Query Sequence
>WP_039652874.1 NCBI__GCF_000816635.1:WP_039652874.1
MQKKISPKLIYFFGAFGGFMFGYDIGIINGALPGIKTTWGISPLLEGWITSGLFVGAMIG
ASLMASLADRFGRRRMIMWSAIVFVIGALGSAFSTSTSFLIFARIILGVAVGGASALVPM
YMGEISPAEERGKLSGLNQLMITIGMLIAYGINYAFVHVFEGWRWMLGGAMVPALVLLFG
TFILPESPRFLVRIGKNELARKVLQSMRSSKEAESEYQEIINSKYSDSGSFKDLFGKKAL
PAVVAGCGLTLLQQIQGANTIFYYSSQILAKVFGSDIGGVISTVGIGVVFVLATVVTLMI
VDRFKRRSLFMSGSIGMGVSLLLVGLIYPYAQANHAWAMWTVFILICVYVIFYAYSWAAV
TWIVVGELFPSQVRGIATGIASTVNWFGNILVALFFPVLLETVGLSMIFFGFAAICILGF
LFAKFVLYETKGKSLEEIETYLYERSIGKVVGLMK
Or try a new SitesBLAST search
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