SitesBLAST
Comparing PP_4946 FitnessBrowser__Putida:PP_4946 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)
P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
77% identity, 90% coverage: 51:540/542 of query aligns to 3:493/502 of P07117
- R257 (= R305) mutation to C: Sodium-independent binding affinity for proline.
- C281 (= C329) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- C344 (= C392) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (= C397) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- R376 (= R424) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
3dh4A Crystal structure of sodium/sugar symporter with bound galactose from vibrio parahaemolyticus (see paper)
25% identity, 68% coverage: 118:483/542 of query aligns to 41:426/512 of 3dh4A
Sites not aligning to the query:
Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
25% identity, 62% coverage: 81:416/542 of query aligns to 45:381/643 of Q92911
- A102 (≠ W138) natural variant: A -> P
- H226 (vs. gap) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (≠ L278) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (≠ F283) Required for homodimerization; mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
- T243 (≠ I284) Required for homodimerization; mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
Sites not aligning to the query:
- 471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
- 525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
- 536 T → Q: requires 2 nucleotide substitutions
- 556 S → Q: requires 2 nucleotide substitutions
Q9ET37 Solute carrier family 5 member 4A; SGLT3-a from Mus musculus (Mouse) (see paper)
24% identity, 79% coverage: 60:485/542 of query aligns to 33:492/656 of Q9ET37
- E457 (≠ A454) mutation to Q: Confers sodium-dependent sugar transport activity not found in the wild type protein.
Q8N695 Sodium-coupled monocarboxylate transporter 1; Apical iodide transporter; Electrogenic sodium monocarboxylate cotransporter; Sodium iodide-related cotransporter; Solute carrier family 5 member 8 from Homo sapiens (Human) (see 3 papers)
24% identity, 76% coverage: 81:492/542 of query aligns to 43:455/610 of Q8N695
- V193 (≠ A239) to I: in dbSNP:rs1709189
- F251 (≠ M290) to V: in dbSNP:rs11834933
Sites not aligning to the query:
- 608 T→A: Loss of interaction with PDZK1.
- 608:610 PDZ-binding
- 610 L→A: Loss of interaction with PDZK1.
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
22% identity, 79% coverage: 60:485/542 of query aligns to 33:492/659 of Q9NY91
- E457 (≠ A454) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
Q9GZV3 High affinity choline transporter 1; hCHT1; Hemicholinium-3-sensitive choline transporter; CHT; Solute carrier family 5 member 7 from Homo sapiens (Human) (see 5 papers)
26% identity, 79% coverage: 57:485/542 of query aligns to 9:442/580 of Q9GZV3
- D48 (≠ S89) to G: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs886039768
- G65 (= G106) to E: in CMS20; loss of choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs886039765
- I89 (= I128) to V: 40% reduction in choline transmembrane transporter activity; found in 0.06 of Ashkenazi Jews; dbSNP:rs1013940; mutation to A: Decreased choline transmembrane transporter activity, only 20% of wild-type choline uptake activity.
- P105 (≠ R144) to S: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs886039766
- Y111 (≠ A155) to H: in CMS20; no effect on localization at plasma membrane
- Y175 (= Y222) to C: in CMS20; uncertain significance; dbSNP:rs1331713195
- I291 (≠ F339) to T: in CMS20; uncertain significance; dbSNP:rs375397889
- V344 (= V386) to L: in CMS20; uncertain significance
- R361 (≠ E403) to Q: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs147656110
- F418 (≠ G461) to V: in CMS20; uncertain significance
Sites not aligning to the query:
- 446 R → G: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane
- 451 E→Q: Decreased choline transmembrane transporter activity, only 5% of wild-type choline uptake activity.
- 527:532 Dileucine-like motif
- 530 I→A: No change in protein internalization. No change in choline transmembrane transporter activity.
- 531 L→A: Loss of protein internalization to vesicular structures in neurons. Increased choline transmembrane transporter activity.
- 531:532 LV→AA: Decreased protein internalization; when associated with V-538. Increased choline transmembrane transporter activity; when associated with V-538.
- 532 V→A: Decreased protein internalization. Increased choline transmembrane transporter activity.
- 538 K→V: Decreased protein internalization; when associated with 531-L-V-532. Increased choline transmembrane transporter activity; when associated with 531-L-V-532.
7sl9A Cryoem structure of smct1 (see paper)
24% identity, 75% coverage: 89:492/542 of query aligns to 30:434/497 of 7sl9A
P11170 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
30% identity, 21% coverage: 376:487/542 of query aligns to 380:494/662 of P11170
- Q457 (≠ A450) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ W453) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 255 modified: Disulfide link with 608
- 608 modified: Disulfide link with 255
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
31% identity, 19% coverage: 376:478/542 of query aligns to 349:454/585 of 7slaA
Sites not aligning to the query:
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
31% identity, 19% coverage: 376:478/542 of query aligns to 348:453/582 of 7sl8A
Sites not aligning to the query:
P31639 Sodium/glucose cotransporter 2; Na(+)/glucose cotransporter 2; Low affinity sodium-glucose cotransporter; Solute carrier family 5 member 2 from Homo sapiens (Human) (see paper)
24% identity, 70% coverage: 47:425/542 of query aligns to 16:428/672 of P31639
- V95 (≠ E123) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (vs. gap) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (≠ S191) mutation to A: Decreases D-glucose transporter activity.
- L283 (≠ I286) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
Sites not aligning to the query:
- 453 F→A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
26% identity, 37% coverage: 60:261/542 of query aligns to 16:213/602 of 7wmvA
- binding N-[2-(dimethylamino)ethyl]-2-methyl-2-[4-[4-[[2-methyl-5-[(2S,3R,4R,5S,6R)-6-methylsulfanyl-3,4,5-tris(oxidanyl)oxan-2-yl]phenyl]methyl]phenyl]butanoylamino]propanamide: N61 (≠ D103), H66 (≠ Y117), L70 (= L121), I81 (≠ V132), F84 (≠ Y135)
Sites not aligning to the query:
- binding N-[2-(dimethylamino)ethyl]-2-methyl-2-[4-[4-[[2-methyl-5-[(2S,3R,4R,5S,6R)-6-methylsulfanyl-3,4,5-tris(oxidanyl)oxan-2-yl]phenyl]methyl]phenyl]butanoylamino]propanamide: 257, 266, 269, 270, 273, 274, 436, 437, 440, 508
P13866 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Homo sapiens (Human) (see 6 papers)
26% identity, 37% coverage: 60:261/542 of query aligns to 33:230/664 of P13866
- N51 (= N78) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (≠ S92) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (= S102) mutation to A: Loss of activity.
- H83 (≠ Y117) mutation to L: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and C-290.; mutation to Q: Loss of D-glucose transporter activity.
- R135 (= R165) to W: in GGM; loss of activity
- S159 (≠ C189) to P: in GGM; loss of activity
- A166 (= A197) to T: in GGM; about 90% reduction in activity
- D204 (= D235) mutation to A: Loss of activity.
Sites not aligning to the query:
- 191:664 natural variant: Missing (in GGM; loss of activity)
- 248 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Loss of N-glycosylation.
- 255 modified: Disulfide link with 511
- 276 W → L: in GGM; about 95% reduction in activity
- 287 T→A: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.; T→N: Loss of D-glucose transporter activity. Has strict selectivity for D-galactose.; mutation T->S,A: Has normal D-glucose and D-galactose transporter activity.
- 290 Y→C: Loss of D-galactose transporter activity. Has strict selectivity for D-glucose. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and L-83.
- 291 W→A: Loss of D-glucose transporter activity.
- 292 C → Y: in GGM; loss of activity; C→A: Has no effect on water permeability.
- 295 Q → R: in GGM; loss of activity
- 300 R → S: in GGM; loss of activity
- 304 A → V: in GGM; impairs trafficking to the plasma membrane
- 321 K→Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- 345 modified: Disulfide link with 351
- 351 modified: Disulfide link with 345
- 355 modified: Disulfide link with 361
- 361 modified: Disulfide link with 355
- 363 N→A: Loss of water permeation.
- 369 L → S: in GGM; loss of activity
- 379 R → Q: in GGM; loss of activity
- 379:664 natural variant: Missing (in GGM; loss of activity)
- 388 A → V: in GGM; loss of activity
- 396 S→A: Loss of activity.
- 405 F → S: in GGM; loss of activity
- 411 A → T: in GGM; slightly decreased activity; dbSNP:rs17683430
- 426 G → R: in GGM; loss of activity
- 451 Q→A: Strong reduction in water permeation.
- 452 L→A: Loss of water permeation.
- 454 D→A: Has no effect on water permeation.
- 457 Q→A: Loss of D-glucose transporter activity.; Q→C: Strong reduction in D-glucose transporter activity.
- 460 T→A: Loss of D-glucose transporter activity.
- 470 V → N: in GGM; about 90% reduction in activity; requires 2 nucleotide substitutions
- 499 R → H: in GGM; impairs trafficking to the plasma membrane; decreases the sugar affinity
- 511 modified: Disulfide link with 255
- 517 modified: Disulfide link with 522
- 522 modified: Disulfide link with 517
- 615 H → Q: in GGM; slightly decreased activity
- 641 W→A: Slightly reduced D-glucose transporter activity.
- 660:661 HA→WG: Loss of D-glucose transporter activity.
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
24% identity, 69% coverage: 53:425/542 of query aligns to 2:408/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (≠ D103), G59 (≠ W107), H60 (≠ L108), G63 (= G111), L64 (= L112), E79 (vs. gap), V266 (≠ L289), S267 (≠ M290), Y270 (= Y296), W271 (≠ F297), K301 (vs. gap)
- binding sodium ion: A53 (= A101), S54 (= S102), I56 (≠ M104), G57 (≠ S105), A369 (= A385), S372 (= S388), S373 (≠ T389)
Sites not aligning to the query:
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: 433, 437
- binding : 579, 583, 584, 587, 588
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
24% identity, 69% coverage: 53:425/542 of query aligns to 2:408/586 of 8hdhA
- binding (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[3-[[5-(4-fluorophenyl)thiophen-2-yl]methyl]-4-methyl-phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ D103), G59 (≠ W107), H60 (≠ L108), G63 (= G111), L64 (= L112), F78 (vs. gap), E79 (vs. gap), S267 (≠ M290), W271 (≠ F297)
- binding sodium ion: A53 (= A101), S54 (= S102), I56 (≠ M104), G57 (≠ S105), A369 (= A385), S372 (= S388), S373 (≠ T389)
Sites not aligning to the query:
- binding (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[3-[[5-(4-fluorophenyl)thiophen-2-yl]methyl]-4-methyl-phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: 433, 434, 437, 506
- binding : 575, 579, 580, 583, 584
8hb0A Structure of human sglt2-map17 complex with ta1887 (see paper)
24% identity, 69% coverage: 53:425/542 of query aligns to 2:408/586 of 8hb0A
- binding (2R,3R,4S,5S,6R)-2-[3-[(4-cyclopropylphenyl)methyl]-4-fluoranyl-indol-1-yl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ D103), H60 (≠ L108), G63 (= G111), L64 (= L112), T67 (≠ A115), V75 (≠ E123), F78 (vs. gap), E79 (vs. gap), V137 (≠ S191), V266 (≠ L289), S267 (≠ M290), W271 (≠ F297)
- binding sodium ion: A53 (= A101), I56 (≠ M104), G57 (≠ S105), A369 (= A385), S372 (= S388), S373 (≠ T389)
Sites not aligning to the query:
- binding (2R,3R,4S,5S,6R)-2-[3-[(4-cyclopropylphenyl)methyl]-4-fluoranyl-indol-1-yl]-6-(hydroxymethyl)oxane-3,4,5-triol: 433, 437
- binding : 575, 576, 579, 580, 583, 584
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
24% identity, 69% coverage: 53:425/542 of query aligns to 2:408/586 of 7vsiA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ D103), H60 (≠ L108), G63 (= G111), L64 (= L112), V75 (≠ E123), F78 (vs. gap), E79 (vs. gap), V266 (≠ L289), S267 (≠ M290), Y270 (= Y296)
Sites not aligning to the query:
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
24% identity, 69% coverage: 53:425/542 of query aligns to 2:408/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ D103), G59 (≠ W107), H60 (≠ L108), G63 (= G111), L64 (= L112), T67 (≠ A115), F78 (vs. gap), E79 (vs. gap), V266 (≠ L289), S267 (≠ M290), W271 (≠ F297), K301 (vs. gap)
- binding sodium ion: A53 (= A101), I56 (≠ M104), G57 (≠ S105), A369 (= A385), S372 (= S388), S373 (≠ T389)
Sites not aligning to the query:
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: 433, 437
- binding : 568, 571, 572, 575, 576, 579, 580
7yniA Structure of human sglt1-map17 complex bound with substrate 4d4fdg in the occluded conformation (see paper)
31% identity, 19% coverage: 376:478/542 of query aligns to 342:447/566 of 7yniA
Sites not aligning to the query:
- binding (2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol: 51, 70, 248, 252
- binding : 548, 552, 555, 556, 559, 560, 563, 564
Query Sequence
>PP_4946 FitnessBrowser__Putida:PP_4946
MGFVGKCTGRCNLQKKNGCTFFALLHSIRRLGATTNGVVAHDKNKRQGTRMGNPLTITFV
IYIAAMVLIGFAAYRATNNLSDYILGGRSLGSVVTALSAGASDMSGWLLMGLPGAIYFAG
LSEAWIAIGLTVGAYLNWLFVAGRLRVQTEHNGDALTLPDYFSSRFEDNSGLLRIISAIV
ILVFFTIYCASGIVAGARLFESTFGMSYETALWAGAAATIAYTFVGGFLAVSWTDTVQAS
LMIFALILTPVIVLISTGGFDQTFAAIEAVNPANFDMLKGATFIGIISLMGWGLGYFGQP
HILARFMAADSVKSIAKARRISMTWMILCLAGTCAVGFFGIAYFSAHPELAGPVSENHER
VFIELAKILFNPWVAGVLLSAILAAVMSTLSCQLLVCSSALTEDFYKAFLRKNASQVELV
WVGRLMVLAVALIAIAMAANPENRVLGLVAYAWAGFGAAFGPVVLISVLWKGMTRNGALA
GIVVGALTVILWKNFDTLGLYEIIPGFLFASIAIVLVSKLGSPSQTMVKRFEAADAAYHA
DK
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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