SitesBLAST
Comparing PP_2797 PP_2797 acetate permease to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 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, 82% coverage: 38:487/552 of query aligns to 11:450/502 of P07117
- R257 (= R283) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ F312) 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 (≠ G376) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G381) 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 (≠ K409) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
21% identity, 52% coverage: 53:339/552 of query aligns to 25:312/480 of 5nv9A
- binding sodium ion: A52 (≠ G80), T53 (≠ D81), L55 (≠ M83), S56 (= S84), V174 (≠ T203), D178 (≠ Q207)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y82), S56 (= S84), I58 (≠ S86), T59 (= T87), G77 (≠ Y105), Q78 (≠ L106), R131 (≠ S153), F239 (≠ L270)
Sites not aligning to the query:
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
22% identity, 61% coverage: 128:464/552 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)
22% identity, 61% coverage: 128:464/552 of query aligns to 93:454/585 of 7slaA
Sites not aligning to the query:
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)
23% identity, 53% coverage: 172:464/552 of query aligns to 169:485/664 of P13866
- D204 (≠ Q207) mutation to A: Loss of activity.
- N248 (≠ T243) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ L250) modified: Disulfide link with 511
- W276 (≠ S267) to L: in GGM; about 95% reduction in activity
- T287 (≠ M282) 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 (≠ F285) 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 (≠ T286) mutation to A: Loss of D-glucose transporter activity.
- C292 (≠ V287) to Y: in GGM; loss of activity; mutation to A: Has no effect on water permeability.
- Q295 (≠ A290) to R: in GGM; loss of activity
- R300 (vs. gap) to S: in GGM; loss of activity
- A304 (vs. gap) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (vs. gap) 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 (≠ G331) modified: Disulfide link with 345
- C355 (≠ G335) modified: Disulfide link with 361
- C361 (≠ G341) modified: Disulfide link with 355
- N363 (= N343) mutation to A: Loss of water permeation.
- L369 (= L349) to S: in GGM; loss of activity
- R379 (≠ L359) to Q: in GGM; loss of activity
- A388 (= A368) to V: in GGM; loss of activity
- S396 (≠ G376) mutation to A: Loss of activity.
- F405 (≠ I385) to S: in GGM; loss of activity
- A411 (= A391) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (≠ Q403) to R: in GGM; loss of activity
- Q451 (≠ I424) mutation to A: Strong reduction in water permeation.
- L452 (= L425) mutation to A: Loss of water permeation.
- D454 (≠ E427) mutation to A: Has no effect on water permeation.
- Q457 (≠ N430) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (≠ M434) mutation to A: Loss of D-glucose transporter activity.
- V470 (= V449) to N: in GGM; about 90% reduction in activity; requires 2 nucleotide substitutions
Sites not aligning to the query:
- 51 N → S: in GGM; slightly decreased activity; dbSNP:rs17683011
- 67 W→A: Strong reduction in D-glucose transporter activity.
- 77 S→A: Loss of activity.
- 83 H→L: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and C-290.; H→Q: Loss of D-glucose transporter activity.
- 135 R → W: in GGM; loss of activity
- 159 S → P: in GGM; loss of activity
- 166 A → T: in GGM; about 90% reduction in activity
- 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
- 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.
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
22% identity, 55% coverage: 163:464/552 of query aligns to 143:468/602 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: L257 (≠ S265), M266 (≠ T274), L269 (= L281), T270 (≠ M282), Y273 (≠ F285), W274 (≠ T286), F436 (= F426), D437 (≠ E427), Q440 (≠ N430)
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: 61, 66, 70, 81, 84, 508
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
20% identity, 84% coverage: 19:479/552 of query aligns to 6:498/659 of Q9NY91
- E457 (≠ F439) 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)
21% identity, 79% coverage: 31:464/552 of query aligns to 25:485/662 of P11170
- C255 (≠ L250) modified: Disulfide link with 608
- Q457 (≠ N430) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ M434) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
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)
24% identity, 37% coverage: 21:222/552 of query aligns to 3:206/643 of Q92911
- A102 (≠ L117) 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
Query Sequence
>PP_2797 PP_2797 acetate permease
MKKLVPLALLLHSGLLLASPSLDAGQRQPLNLHAIGMFMVFVLFTLCITWWAARRTRSTT
DFYSAGGGIQGWQNGLALAGDYMSASTLLGITALIYTSGMDGYIYLIAFFAGWPVLLLLM
TERLRNLGRFTFADITSYRLDQGKVRTMAAIGSLTVVCFYLVAQMVGAGQLIRLLFGLDY
HIAVVIVGALMMLYVTFGGMVATTWVQIIKAFLLLVGGSLVLFLAMREFDFSYDALVSKA
MDTHALGERLLAPGSLLADPLTALSLSLGLVFGTAGLPHILMRFFTVSDAREARKSVLYA
TGFIGYFFNVIFLLGLASIVIVSQQPKFFEGGEVGGKLLGGGNMVVMHLAQAVGGNLLLG
FLSAVTFATILAVVSGLALAGASAIAHDLYARVIMKGAASEAQELRVTKLATLSLGLVAI
ALGILFENINVAFMVALAFGIAASANFPVLFLSMFWSGLTTRGALAAGYVGLLSAMGFVV
FSKLVWVDVLHFAEPLFPYTQPALFSMPLAFLVAYAVSRMDRTARAKAERAAFADQFVRG
QTGLGASGAVDH
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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