SitesBLAST
Comparing Ac3H11_2058 Putrescine transport ATP-binding protein PotA (TC 3.A.1.11.1) 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 82% coverage: 30:325/360 of query aligns to 36:343/378 of P69874
- F45 (≠ L39) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C48) mutation to T: Loss of ATPase activity and transport.
- L60 (= L54) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I70) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V129) mutation to M: Loss of ATPase activity and transport.
- D172 (= D166) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ L263) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E283) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: 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.
1g291 Malk (see paper)
46% identity, 73% coverage: 6:266/360 of query aligns to 2:266/372 of 1g291
- binding magnesium ion: D69 (≠ T77), E71 (vs. gap), K72 (vs. gap), K79 (≠ A81), D80 (≠ Q82), Y228 (= Y230), D229 (≠ E231)
- binding pyrophosphate 2-: P37 (= P45), S38 (= S46), G39 (= G47), C40 (= C48), G41 (= G49), K42 (= K50), T43 (= T51), T44 (= T52)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 71% coverage: 12:266/360 of query aligns to 11:269/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
49% identity, 66% coverage: 6:243/360 of query aligns to 1:234/374 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)
46% identity, 77% coverage: 6:283/360 of query aligns to 2:285/393 of P9WQI3
- H193 (= H200) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
49% identity, 66% coverage: 6:243/360 of query aligns to 1:234/372 of 2awoA
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
49% identity, 66% coverage: 6:243/360 of query aligns to 2:235/371 of P68187
- A85 (= A93) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A125) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R127) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V132) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G145) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D166) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E236) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
49% identity, 66% coverage: 6:243/360 of query aligns to 1:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y17), V17 (≠ A26), P36 (= P45), S37 (= S46), G38 (= G47), C39 (= C48), G40 (= G49), K41 (= K50), S42 (≠ T51), T43 (= T52), Q81 (= Q90), R128 (= R137), A132 (≠ E141), S134 (= S143), G135 (= G144), G136 (= G145), Q137 (= Q146), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T51), Q81 (= Q90), D157 (= D166)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
49% identity, 66% coverage: 6:243/360 of query aligns to 1:234/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y17), V17 (≠ A26), S37 (= S46), G38 (= G47), C39 (= C48), G40 (= G49), K41 (= K50), S42 (≠ T51), T43 (= T52), R128 (= R137), A132 (≠ E141), L133 (= L142), S134 (= S143), Q137 (= Q146)
- binding beryllium trifluoride ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q90), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T51), Q81 (= Q90), D157 (= D166)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
49% identity, 66% coverage: 6:243/360 of query aligns to 1:234/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y17), V17 (≠ A26), S37 (= S46), G38 (= G47), C39 (= C48), G40 (= G49), K41 (= K50), S42 (≠ T51), T43 (= T52), R128 (= R137), A132 (≠ E141), S134 (= S143), Q137 (= Q146)
- binding tetrafluoroaluminate ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q90), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), N162 (= N171), H191 (= H200)
- binding magnesium ion: S42 (≠ T51), Q81 (= Q90)
7cagC Mycobacterium smegmatis lpqy-sugabc complex in the catalytic intermediate state (see paper)
39% identity, 97% coverage: 6:354/360 of query aligns to 1:356/362 of 7cagC
- binding adenosine-5'-triphosphate: A14 (≠ T19), P34 (= P45), S35 (= S46), G36 (= G47), C37 (= C48), G38 (= G49), K39 (= K50), S40 (≠ T51), T41 (= T52), Q79 (= Q90), L123 (≠ F134), R126 (= R137), Q130 (≠ E141), S132 (= S143), G133 (= G144), G134 (= G145), Q135 (= Q146)
- binding magnesium ion: S40 (≠ T51), Q79 (= Q90)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
49% identity, 66% coverage: 6:243/360 of query aligns to 2:235/369 of P19566
- L86 (= L94) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P168) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D173) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
50% identity, 65% coverage: 10:243/360 of query aligns to 3:232/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y17), V15 (≠ A26), S35 (= S46), G36 (= G47), C37 (= C48), G38 (= G49), K39 (= K50), S40 (≠ T51), T41 (= T52), R126 (= R137), K129 (≠ S140), A130 (≠ E141), L131 (= L142), S132 (= S143), G133 (= G144), G134 (= G145), Q135 (= Q146), N160 (= N171), H189 (= H200)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
51% identity, 65% coverage: 10:243/360 of query aligns to 9:230/353 of 1vciA
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
41% identity, 68% coverage: 21:263/360 of query aligns to 36:291/382 of 7ahhC
- 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: I272 (≠ F248), P273 (= P249), L275 (≠ V251)
- binding phosphoaminophosphonic acid-adenylate ester: T39 (≠ A24), V40 (≠ L25), G41 (≠ A26), S61 (= S46), G62 (= G47), S63 (≠ C48), G64 (= G49), K65 (= K50), S66 (≠ T51), T67 (= T52), D187 (= D166), E188 (= E167)
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: 295, 296, 297, 298, 357, 370, 372
- binding phosphoaminophosphonic acid-adenylate ester: 12, 29
7aheC Opua inhibited inward facing (see paper)
41% identity, 68% coverage: 21:263/360 of query aligns to 36:291/382 of 7aheC
- 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: L275 (≠ V251)
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: 295, 296, 297, 298, 357, 372
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
47% identity, 60% coverage: 28:243/360 of query aligns to 12:204/344 of 2awnC