SitesBLAST
Comparing WP_010536987.1 NCBI__GCF_000226135.1:WP_010536987.1 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)
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 beta-D-xylose; mutation to A: Abolishes xylose transport.
- Q288 (= Q274) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 274:275) binding beta-D-xylose
- Q289 (= Q275) mutation to A: Strongly decreases xylose transport.
- N294 (= N280) binding beta-D-xylose; 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 beta-D-xylose; 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 beta-D-xylose
- 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)
39% 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)
39% 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)
39% 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)
32% identity, 93% coverage: 29:458/460 of query aligns to 25:437/446 of A0A0H2VG78
- 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.
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)
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 beta-D-glucose; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I150) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q274) binding beta-D-glucose
- Q296 (= Q275) binding beta-D-glucose
- N301 (= N280) binding beta-D-glucose
- N332 (= N311) binding beta-D-glucose
- D344 (≠ E323) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W378) binding beta-D-glucose
- 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
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