SitesBLAST
Comparing WP_028998684.1 NCBI__GCF_000430725.1:WP_028998684.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 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)
25% identity, 79% coverage: 41:482/556 of query aligns to 7:444/502 of P07117
- R257 (= R287) mutation to C: Sodium-independent binding affinity for proline.
- C281 (= C316) 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 (≠ G380) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G385) 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 (= R414) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
22% identity, 81% coverage: 25:476/556 of query aligns to 9:493/659 of Q9NY91
- E457 (≠ F443) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
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)
19% identity, 82% coverage: 28:481/556 of query aligns to 18:498/662 of P11170
- C255 (≠ A244) modified: Disulfide link with 608
- Q457 (≠ F443) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ A446) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
20% identity, 51% coverage: 57:342/556 of query aligns to 29:316/496 of B4EZY7
- A56 (≠ G84) binding Na(+)
- T58 (≠ Y86) mutation to A: 2-fold increase in Neu5Ac transport.
- L59 (≠ M87) binding Na(+)
- S60 (= S88) mutation to A: Abolishes Neu5Ac transport.
- T63 (= T91) mutation to A: Abolishes Neu5Ac transport.
- Q82 (≠ F113) mutation to D: Abolishes Neu5Ac transport.
- R135 (vs. gap) mutation to E: Abolishes Neu5Ac transport.
- D182 (≠ Q211) binding Na(+); mutation to A: Abolishes Neu5Ac transport.
Sites not aligning to the query:
- 339 binding Na(+)
- 342 binding Na(+); binding Na(+); S→A: Abolishes Neu5Ac transport.
- 343 binding Na(+); S→A: Abolishes Neu5Ac transport.
- 345 binding Na(+); S→A: Reduces Neu5Ac transport.
- 346 binding Na(+); S→A: Slightly increases Neu5Ac transport.
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
20% identity, 51% coverage: 57:342/556 of query aligns to 25:312/480 of 5nv9A
- binding sodium ion: A52 (≠ G84), T53 (≠ D85), L55 (≠ M87), S56 (= S88), V174 (≠ T207), D178 (≠ Q211)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y86), S56 (= S88), I58 (≠ A90), T59 (= T91), G77 (≠ S112), Q78 (≠ F113), R131 (vs. gap), F239 (≠ L274)
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)
21% identity, 37% coverage: 24:227/556 of query aligns to 2:207/643 of Q92911
- A102 (≠ L121) natural variant: A -> P
Sites not aligning to the query:
- 226 mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- 237 D→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- 242 Required for homodimerization; Y→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.
- 243 Required for homodimerization; T→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.
- 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
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)
20% identity, 79% coverage: 28:468/556 of query aligns to 18:485/664 of P13866
- N51 (≠ R61) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (≠ G75) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (≠ D85) mutation to A: Loss of activity.
- H83 (≠ T91) 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 (= R143) to W: in GGM; loss of activity
- S159 (≠ V167) to P: in GGM; loss of activity; dbSNP:rs933026071
- A166 (≠ Q174) to T: in GGM; about 90% reduction in activity
- D204 (≠ Q211) mutation to A: Loss of activity.
- N248 (≠ V245) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ A252) modified: Disulfide link with 511
- W276 (≠ S271) to L: in GGM; about 95% reduction in activity
- T287 (≠ P282) mutation to A: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.; mutation to 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.
- Y290 (vs. gap) mutation to 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.
- W291 (vs. gap) mutation to A: Loss of D-glucose transporter activity.
- C292 (vs. gap) to Y: in GGM; loss of activity; dbSNP:rs765502638; mutation to A: Has no effect on water permeability.
- Q295 (vs. gap) to R: in GGM; loss of activity; dbSNP:rs779428134
- R300 (= R287) to S: in GGM; loss of activity
- A304 (≠ V291) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (≠ G309) mutation to Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- C345 (vs. gap) modified: Disulfide link with 351
- C351 (≠ G335) modified: Disulfide link with 345
- C355 (≠ G339) modified: Disulfide link with 361
- C361 (≠ G345) modified: Disulfide link with 355
- N363 (= N347) mutation to A: Loss of water permeation.
- L369 (= L353) to S: in GGM; loss of activity
- R379 (≠ L363) to Q: in GGM; loss of activity; dbSNP:rs747215838
- A388 (= A372) to V: in GGM; loss of activity
- S396 (≠ G380) mutation to A: Loss of activity.
- F405 (≠ I389) to S: in GGM; loss of activity
- A411 (= A395) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (≠ K413) to R: in GGM; loss of activity; dbSNP:rs1304151494
- Q451 (≠ F437) mutation to A: Strong reduction in water permeation.
- L452 (= L438) mutation to A: Loss of water permeation.
- D454 (≠ G440) mutation to A: Has no effect on water permeation.
- Q457 (≠ F443) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (≠ A446) mutation to A: Loss of D-glucose transporter activity.
- V470 (= V453) to N: in GGM; about 90% reduction in activity; requires 2 nucleotide substitutions
Sites not aligning to the query:
- 191:664 natural variant: Missing (in GGM; loss of activity)
- 379:664 natural variant: Missing (in GGM; loss of activity)
- 499 R → H: in GGM; impairs trafficking to the plasma membrane; decreases the sugar affinity; dbSNP:rs927157864
- 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; dbSNP:rs33954001
- 641 W→A: Slightly reduced D-glucose transporter activity.
- 660:661 HA→WG: Loss of D-glucose transporter activity.
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
20% identity, 79% coverage: 28:468/556 of query aligns to 1:468/602 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 (≠ Y86), H66 (≠ T91), L70 (= L95), I81 (≠ T101), F84 (= F104), L257 (≠ S269), M266 (≠ T278), L269 (= L281), T270 (≠ P282), Y273 (vs. gap), W274 (vs. gap), F436 (≠ V439), D437 (≠ G440), Q440 (≠ F443)
Sites not aligning to the query:
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
20% identity, 61% coverage: 132:468/556 of query aligns to 92:453/582 of 7sl8A
Sites not aligning to the query:
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
20% identity, 61% coverage: 132:468/556 of query aligns to 93:454/585 of 7slaA
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)
22% identity, 65% coverage: 35:397/556 of query aligns to 22:413/672 of P31639
- V95 (≠ T101) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (= F104) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (= V167) mutation to A: Decreases D-glucose transporter activity.
- L283 (= L272) 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.
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
22% identity, 65% coverage: 35:397/556 of query aligns to 2:393/586 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 (≠ Y86), H60 (≠ T91), G63 (= G94), L64 (= L95), V75 (≠ T101), F78 (= F104), E79 (≠ D105), V266 (= V275), S267 (≠ F276), Y270 (≠ T278)
Sites not aligning to the query:
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
22% identity, 65% coverage: 35:397/556 of query aligns to 2:393/586 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 (≠ Y86), G59 (≠ A90), H60 (≠ T91), G63 (= G94), L64 (= L95), F78 (= F104), E79 (≠ D105), S267 (≠ F276), W271 (≠ A279)
- binding sodium ion: A53 (≠ G84), S54 (≠ D85), I56 (≠ M87), G57 (≠ S88), A369 (≠ T373), S372 (≠ A376), S373 (≠ V377)
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)
22% identity, 65% coverage: 35:397/556 of query aligns to 2:393/586 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 (≠ Y86), H60 (≠ T91), G63 (= G94), L64 (= L95), T67 (vs. gap), V75 (≠ T101), F78 (= F104), E79 (≠ D105), V137 (= V167), V266 (= V275), S267 (≠ F276), W271 (≠ A279)
- binding sodium ion: A53 (≠ G84), I56 (≠ M87), G57 (≠ S88), A369 (≠ T373), S372 (≠ A376), S373 (≠ V377)
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
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
22% identity, 65% coverage: 35:397/556 of query aligns to 2:393/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (≠ Y86), G59 (≠ A90), H60 (≠ T91), G63 (= G94), L64 (= L95), E79 (≠ D105), V266 (= V275), S267 (≠ F276), Y270 (≠ T278), W271 (≠ A279), K301 (≠ G309)
- binding sodium ion: A53 (≠ G84), S54 (≠ D85), I56 (≠ M87), G57 (≠ S88), A369 (≠ T373), S372 (≠ A376), S373 (≠ V377)
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
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
22% identity, 65% coverage: 35:397/556 of query aligns to 2:393/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ Y86), G59 (≠ A90), H60 (≠ T91), G63 (= G94), L64 (= L95), T67 (vs. gap), F78 (= F104), E79 (≠ D105), V266 (= V275), S267 (≠ F276), W271 (≠ A279), K301 (≠ G309)
- binding sodium ion: A53 (≠ G84), I56 (≠ M87), G57 (≠ S88), A369 (≠ T373), S372 (≠ A376), S373 (≠ V377)
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
8hinA Structure of human sglt2-map17 complex with phlorizin (see paper)
23% identity, 65% coverage: 35:397/556 of query aligns to 9:389/588 of 8hinA
- binding 1-[2-[(2S,3R,4S,5S,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,6-bis(oxidanyl)phenyl]-3-(4-hydroxyphenyl)propan-1-one: S46 (≠ G72), A49 (≠ G75), S50 (≠ F76), G53 (= G79), D177 (≠ Q211), T181 (≠ A215), R276 (≠ F288), S369 (≠ V377)
Sites not aligning to the query:
Query Sequence
>WP_028998684.1 NCBI__GCF_000430725.1:WP_028998684.1
MSKIHKTLGTLALLGAAGAARAGDAIGEAQKQPLNVTAIAMFVAFVLMTLGITYWAARRT
RSASDFYTAGGGITGFQNGLAIAGDYMSAATLLGLSSMVFTRGFDGFVYIISFFVGWPVI
LFLLAERLRNLGRFTFADIASYRLDQNRIRTFAAFGSLTVVIFYLIVQMVGAGQLIKLLF
GLDYAVAVAIVGVLMVVYVTFGGMIATTWVQIVKAVLLLCGGLIMLALAMSHFGFNIETL
ASKAVSAHKSGAAIMRPGSLLADPVTAVSLSLGLVFGTAALPHIMMRFFTVPNAKEARKS
VFVASGFIGLFFLVVCLLGLAAIVIVGQDPQFYEGGKVGGALIGGSNMPVMHLAKAVGGD
LLLGFLSAVAFATILAVVSGLALAGASAIAHDIYARVIRQGKCTEEEEIKVSKRCSLLLG
VLAVVLGIAFEKQNVAFLVGLTFGIAASANFPVLVLSIYWKGLTTRGALVGGVIGLVSAV
AFVVLSKAVWVVVLGNPAPIFPYEQPALFSMPLAFFFTWLFSVTDKSARAQKEIASFRDQ
YVRAQTGIGAAAASAH
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