SitesBLAST
Comparing AO353_01865 AO353_01865 cation/acetate symporter ActP to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 8 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)
24% identity, 82% coverage: 33:482/552 of query aligns to 3:462/502 of P07117
- R257 (= R286) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ T314) 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)
22% identity, 54% coverage: 44:339/552 of query aligns to 13:312/480 of 5nv9A
- binding sodium ion: A52 (≠ G83), T53 (≠ D84), L55 (≠ M86), S56 (= S87), V174 (≠ T206), D178 (≠ Q210)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y85), L55 (≠ M86), S56 (= S87), I58 (≠ A89), T59 (≠ S90), G77 (≠ Y108), Q78 (≠ S109), R131 (≠ S156), F239 (vs. gap), V277 (≠ I307)
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)
27% identity, 29% coverage: 59:220/552 of query aligns to 41:201/643 of Q92911
- A102 (≠ L120) 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
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: 27:480/552 of query aligns to 18:501/662 of P11170
- C255 (vs. gap) modified: Disulfide link with 608
- Q457 (≠ F439) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ A442) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
21% identity, 61% coverage: 131:464/552 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)
21% identity, 61% coverage: 131:464/552 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)
20% identity, 79% coverage: 27:464/552 of query aligns to 18:485/664 of P13866
- N51 (≠ R58) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (≠ G74) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (≠ D84) mutation to A: Loss of activity.
- H83 (≠ S90) 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 (= R142) to W: in GGM; loss of activity
- S159 (≠ A166) to P: in GGM; loss of activity
- A166 (≠ K173) to T: in GGM; about 90% reduction in activity
- D204 (≠ Q210) mutation to A: Loss of activity.
- N248 (= N237) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ I244) modified: Disulfide link with 511
- W276 (≠ G270) to L: in GGM; about 95% reduction in activity
- T287 (≠ M285) 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 (≠ F288) 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 (≠ T289) mutation to A: Loss of D-glucose transporter activity.
- C292 (≠ V290) to Y: in GGM; loss of activity; mutation to A: Has no effect on water permeability.
- Q295 (≠ A293) 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 (≠ Y311) 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 (≠ F331) modified: Disulfide link with 345
- C355 (≠ T335) 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 (≠ V385) to S: in GGM; loss of activity
- A411 (= A391) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (≠ S408) to R: in GGM; loss of activity
- Q451 (≠ F433) mutation to A: Strong reduction in water permeation.
- L452 (≠ M434) mutation to A: Loss of water permeation.
- D454 (≠ G436) mutation to A: Has no effect on water permeation.
- Q457 (≠ F439) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (≠ A442) mutation to A: Loss of D-glucose transporter activity.
- V470 (= V449) to N: in GGM; requires 2 nucleotide substitutions; about 90% reduction in activity
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
- 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)
20% identity, 79% coverage: 27:464/552 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 (≠ Y85), H66 (≠ S90), L70 (≠ I94), I81 (vs. gap), F84 (≠ Y103), E85 (≠ D104), A88 (≠ I107), D256 (≠ F267), L257 (≠ S268), M266 (≠ T277), L269 (= L284), T270 (≠ M285), Y273 (≠ F288), W274 (≠ T289), K304 (≠ Y311), F436 (≠ V435), D437 (≠ G436), Q440 (≠ F439)
Sites not aligning to the query:
Query Sequence
>AO353_01865 AO353_01865 cation/acetate symporter ActP
MIRRLLAALGIAAFAPAVWAAEALTGEVHKQPLNVSAILMFVVFVGATLCITYWASKRNK
SAADYYAAGGRITGLQNGLAIAGDYMSAASFLGISALVFASGYDGLIYSIGFLVGWPIIL
FLIAERLRNLGKYTFADVASYRLGQTQIRTLSACGSLVVVAFYLIAQMVGAGKLIQLLFG
LDYHVAVILVGILMCLYVLFGGMLATTWVQIIKAVLLLSGASFMALMVMKHVHFDFNTLF
SEAIKVHPKGEAIMSPGGLVKDPISAFSLGLALMFGTAGLPHILMRFFTVSDAKEARKSV
LYATGFIGYFYILTFIIGFGAILLVSTNPAFKDATGALLGGNNMAAVHLANAVGGSIFLG
FISAVAFATILAVVAGLTLAGATAVSHDLYASVIKKGKANEKDEIRVSKITTIALGVLAI
VLGILFESQNIAFMVGLAFSIAASCNFPVLLLSMYWKKLTTRGAMVGGWMGLVSAVGLMV
LGPTIWVQIMGHEKAIFPYEYPALFSMAIAFVGIWFFSITDKSAAADNERALFFPQFVRS
QTGLGASGAVSH
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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