SitesBLAST
Comparing WP_017751862.1 NCBI__GCF_000816635.1:WP_017751862.1 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)
36% identity, 92% coverage: 30:459/466 of query aligns to 22:439/446 of A0A0H2VG78
- D22 (= D30) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R112) mutation to A: Loss of transport activity.
- I105 (≠ V115) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E132) mutation to A: Loss of transport activity.
- Q137 (= Q147) mutation to A: Loss of transport activity.
- Q250 (= Q268) mutation to A: Loss of transport activity.
- Q251 (= Q269) mutation to A: Loss of transport activity.
- N256 (= N274) mutation to A: Loss of transport activity.
- W357 (= W377) mutation to A: Loss of transport activity.
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
32% identity, 99% coverage: 6:466/466 of query aligns to 3:487/491 of P0AGF4
- F24 (= F27) mutation to A: Decreases xylose transport.
- G83 (= G80) mutation to A: Abolishes xylose transport.
- R133 (= R112) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E132) mutation to A: Abolishes xylose transport.
- R160 (= R139) mutation to A: Abolishes xylose transport.
- Q168 (= Q147) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Q288 (= Q268) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 268:269) binding beta-D-xylose
- Q289 (= Q269) mutation to A: Strongly decreases xylose transport.
- N294 (= N274) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Y298 (= Y278) mutation to A: Abolishes xylose transport.
- N325 (≠ S305) mutation to A: No effect on xylose transport.
- G340 (≠ N321) mutation to A: Abolishes xylose transport.
- R341 (= R322) mutation R->A,W: Abolishes xylose transport.
- W392 (= W377) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- E397 (= E382) mutation to A: Abolishes xylose transport.
- R404 (= R389) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ N400) binding beta-D-xylose
- W416 (= W401) 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)
33% identity, 96% coverage: 9:454/466 of query aligns to 2:471/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
33% identity, 96% coverage: 9:454/466 of query aligns to 2:471/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
33% identity, 96% coverage: 9:454/466 of query aligns to 2:471/475 of 4gbyA
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 98% coverage: 2:458/466 of query aligns to 20:480/509 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.
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 70% coverage: 9:332/466 of query aligns to 23:352/582 of O23492
Sites not aligning to the query:
- 559:561 LLE→AAA: No effect on targeting.
- 559:582 mutation Missing: No effect on targeting.
- 564:565 FK→AA: No effect on targeting.
- 570:575 RRREKK→AAAAAA: No effect on targeting.
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, 94% coverage: 20:459/466 of query aligns to 19:469/492 of P11166
- N34 (= N35) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (≠ D45) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to T: Loss of glycosylation site.
- R51 (≠ P51) to H: in EIG12; uncertain significance; dbSNP:rs201815571
- T60 (≠ S60) to M: in EIG12; uncertain significance; decreased glucose transport; dbSNP:rs142986731
- M77 (≠ A66) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G80) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R112) 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 (= G116) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S123) binding cytochalasin B
- P149 (= P135) to A: in EIG12; uncertain significance
- R153 (= R139) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity; dbSNP:rs1643479461
- L169 (= L155) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (= I180) mutation to C: Strongly decreases glucose transport.
- L204 (≠ M192) mutation to C: Abolishes glucose transport.
- P205 (≠ L193) mutation to C: Abolishes glucose transport.
- R212 (= R200) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (≠ H205) to S: in EIG12; decreased glucose transport
- R223 (≠ D210) 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 (≠ E213) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (= R219) 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 (= E230) to V: in EIG12; decreased glucose transport; dbSNP:rs2124449030
- A275 (≠ G261) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (= Q268) binding cytochalasin B
- QQLS 282:285 (≠ QQFA 268:271) 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 (= G272) 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 (= T281) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (= V291) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G302) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ Y312) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ N318) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R322) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G329) mutation to C: Strongly decreases glucose transport.
- W388 (= W377) binding cytochalasin B
- N411 (= N400) Not glycosylated; binding cytochalasin B; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ L425) 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 (≠ K448) 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
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, 96% coverage: 19:466/466 of query aligns to 16:471/493 of P32037
- N43 (= N48) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 70% coverage: 9:336/466 of query aligns to 24:354/580 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)
29% identity, 94% coverage: 20:459/466 of query aligns to 19:469/492 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.
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, 94% coverage: 19:458/466 of query aligns to 16:466/496 of P11169
- Q159 (= Q147) binding D-glucose
- QLS 277:279 (≠ AII 265:267) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 268:269) binding D-glucose
- N286 (= N274) binding D-glucose
- N315 (≠ S305) binding D-glucose
- E378 (≠ Q369) binding D-glucose
- W386 (= W377) binding D-glucose
P38695 Probable glucose transporter HXT5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 98% coverage: 1:458/466 of query aligns to 67:550/592 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)
29% identity, 94% coverage: 19:458/466 of query aligns to 16:466/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q147), I166 (≠ Q154), Q280 (= Q268), Q281 (= Q269), N286 (= N274), F377 (≠ D368), W386 (= W377)
- binding alpha-D-glucopyranose: Q159 (= Q147), I162 (= I150), I166 (≠ Q154), Q280 (= Q268), Q281 (= Q269), N286 (= N274), W386 (= W377)
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
29% identity, 94% coverage: 19:458/466 of query aligns to 13:463/468 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 (= F27), T25 (≠ S31), N29 (= N35), Q156 (= Q147), I163 (≠ Q154), Q278 (= Q269), F286 (≠ M277), A308 (≠ N301), N312 (≠ S305), F374 (≠ D368), E375 (≠ Q369), N406 (= N400), W407 (= W401), N410 (= N404)
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
29% identity, 94% coverage: 19:458/466 of query aligns to 14:464/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (≠ S31), A66 (vs. gap), S69 (vs. gap), Q157 (= Q147), I164 (≠ Q154), Q278 (= Q268), Q279 (= Q269), N284 (= N274), N313 (≠ S305), F375 (≠ D368), W384 (= W377), N411 (= N404), F412 (= F405), G415 (= G408)
7sptA Crystal structure of exofacial state human glucose transporter glut3 (see paper)
29% identity, 94% coverage: 19:458/466 of query aligns to 16:466/470 of 7sptA
P39003 High-affinity hexose transporter HXT6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 94% coverage: 16:454/466 of query aligns to 68:525/570 of P39003
Sites not aligning to the query:
- 560 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P39004 High-affinity hexose transporter HXT7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 94% coverage: 16:454/466 of query aligns to 68:525/570 of P39004
Sites not aligning to the query:
- 560 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5eqiA Human glut1 in complex with cytochalasin b (see paper)
28% identity, 91% coverage: 20:445/466 of query aligns to 11:447/447 of 5eqiA
Query Sequence
>WP_017751862.1 NCBI__GCF_000816635.1:WP_017751862.1
MEQTVNKDKKKFLRKISILATFGSLLFGYDSGVINGALTFIARKDQLNLTPLTEGLVTSS
LLLGAAIGAVLMGHFSDKYGRKKVLKVLAAVFFFSTIGCSISPNAEIIIICRFIVGIGVG
GVSVVVPTLLAEMAPTKIRGSLVSRDQFMIVTGQLLAYIFNGILGNVFENPGIWRYMIAI
SSIPAVVLWFGMLVVPETPRWLASHGKIADALEILRQTREEQEAEAEIKEIQKNIEAESS
LERATFKELGIPWIRRIVIIGCLIAIIQQFAGVNVLMYYGTTVLEKSGFGVKTALIANIG
NGIMSVVASWIYMHLLSNRCNRRPLLIIGYCGTTVTWLAITIVSHVLSGSGTLPFVIVIL
TMIFLAIDQATLGPLTWLLLSEIFPLRVRGMGYGVATFFNWIGNFAVGLTFPILIAYFGL
SSTFLIFVLLGVLCIICAIMVVPETRGKSLEQMEDYFRSYKTRSES
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