SitesBLAST
Comparing Dsui_3464 Dsui_3464 ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component 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)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
44% identity, 79% coverage: 1:208/263 of query aligns to 1:207/371 of P68187
- A85 (= A86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E107) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L118) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D120) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K125) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G138) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D159) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 340 G→A: Maltose transport is affected but retains ability to interact with MalT.
- 346 G→S: Normal maltose transport but constitutive mal gene expression.
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
44% identity, 79% coverage: 2:208/263 of query aligns to 1:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F13), S37 (= S42), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), Q81 (= Q83), R128 (= R130), A132 (≠ D134), S134 (= S136), G136 (= G138), Q137 (≠ M139), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (= S47), Q81 (= Q83)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
44% identity, 79% coverage: 2:208/263 of query aligns to 1:206/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F13), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R130), S134 (= S136), Q137 (≠ M139)
- binding beryllium trifluoride ion: S37 (= S42), G38 (= G43), K41 (= K46), Q81 (= Q83), S134 (= S136), G136 (= G138), H191 (= H193)
- binding magnesium ion: S42 (= S47), Q81 (= Q83)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
44% identity, 79% coverage: 2:208/263 of query aligns to 1:206/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A22), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R130), A132 (≠ D134), S134 (= S136), Q137 (≠ M139)
- binding tetrafluoroaluminate ion: S37 (= S42), G38 (= G43), K41 (= K46), Q81 (= Q83), S134 (= S136), G135 (= G137), G136 (= G138), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (= S47), Q81 (= Q83)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
44% identity, 79% coverage: 2:208/263 of query aligns to 1:206/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A22), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R130), A132 (≠ D134), S134 (= S136), Q137 (≠ M139)
- binding magnesium ion: S42 (= S47), Q81 (= Q83)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
44% identity, 79% coverage: 2:208/263 of query aligns to 1:206/374 of 2awnB
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 79% coverage: 1:208/263 of query aligns to 1:208/393 of P9WQI3
- H193 (= H193) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
46% identity, 73% coverage: 18:208/263 of query aligns to 11:204/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S42), G36 (= G43), C37 (= C44), G38 (= G45), K39 (= K46), S40 (= S47), T41 (= T48), R126 (= R130), A130 (≠ D134), S132 (= S136), G134 (= G138), Q135 (≠ M139)
Sites not aligning to the query:
1g291 Malk (see paper)
44% identity, 79% coverage: 1:209/263 of query aligns to 1:214/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ P76), D80 (= D77)
- binding pyrophosphate 2-: S38 (= S42), G39 (= G43), C40 (= C44), G41 (= G45), K42 (= K46), T43 (≠ S47), T44 (= T48)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
43% identity, 79% coverage: 1:208/263 of query aligns to 1:207/369 of P19566
- L86 (= L87) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P161) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D166) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
43% identity, 79% coverage: 1:209/263 of query aligns to 4:217/375 of 2d62A
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 71% coverage: 22:208/263 of query aligns to 16:205/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
45% identity, 71% coverage: 22:208/263 of query aligns to 18:207/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S42), G39 (= G43), G41 (= G45), K42 (= K46), S43 (= S47), Q82 (= Q83), Q133 (≠ D134), G136 (= G137), G137 (= G138), Q138 (≠ M139), H192 (= H193)
- binding magnesium ion: S43 (= S47), Q82 (= Q83)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
45% identity, 71% coverage: 22:208/263 of query aligns to 18:207/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S42), C40 (= C44), G41 (= G45), K42 (= K46), S43 (= S47), T44 (= T48), Q82 (= Q83), R129 (= R130), Q133 (≠ D134), S135 (= S136), G136 (= G137), G137 (= G138), Q159 (≠ E160), H192 (= H193)
- binding magnesium ion: S43 (= S47), Q82 (= Q83)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
46% identity, 73% coverage: 26:218/263 of query aligns to 36:229/378 of P69874
- F45 (= F35) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C44) mutation to T: Loss of ATPase activity and transport.
- L60 (= L50) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I66) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L122) mutation to M: Loss of ATPase activity and transport.
- D172 (= D159) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
44% identity, 72% coverage: 19:208/263 of query aligns to 7:176/344 of 2awnC
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
41% identity, 76% coverage: 10:208/263 of query aligns to 30:236/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12
7aheC Opua inhibited inward facing (see paper)
41% identity, 76% coverage: 10:208/263 of query aligns to 30:236/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
7ahdC Opua (e190q) occluded (see paper)
40% identity, 76% coverage: 10:208/263 of query aligns to 30:236/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ D19), S61 (= S42), G62 (= G43), G64 (= G45), K65 (= K46), S66 (= S47), T67 (= T48), Q111 (= Q83), K161 (= K133), Q162 (≠ D134), S164 (= S136), G166 (= G138), M167 (= M139), Q188 (≠ E160), H221 (= H193)
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 93% coverage: 1:244/263 of query aligns to 1:247/353 of 1oxvD
Query Sequence
>Dsui_3464 Dsui_3464 ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component
MSDILIKDVQKVFKTPGGDVTALKDINLTVKQGEFVCLLGPSGCGKSTLLNAVAGFQPPS
AGEIVIEGKKILTPGPDRGMVFQEYALFPWMTVAQNIAFGLQIQKKEKAEIDLTVNQLLD
LLHLKDFRDRFPKDLSGGMRQRVAIARVLALDSPIMLMDEPFGALDALTRRNLQDELLRI
WEKLNKTILFVTHSIEESIYLADRIVVMTYRPGTIKRDQYVTMPRPRDPSSHEFNELKRE
LGRLVMEEQQRHAADELKLAAVD
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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