SitesBLAST
Comparing AO353_25420 AO353_25420 spermidine/putrescine ABC transporter ATP-binding protein 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)
49% identity, 88% coverage: 12:340/372 of query aligns to 18:341/378 of P69874
- C26 (≠ V20) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y21) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F43) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C52) mutation to T: Loss of ATPase activity and transport.
- L60 (= L58) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L74) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V137) mutation to M: Loss of ATPase activity and transport.
- D172 (= D174) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ L278) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E299) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 78% coverage: 12:302/372 of query aligns to 7:298/375 of 2d62A
1g291 Malk (see paper)
46% identity, 78% coverage: 11:302/372 of query aligns to 3:295/372 of 1g291
- binding magnesium ion: D69 (= D81), E71 (vs. gap), K72 (vs. gap), K79 (≠ Y85), D80 (≠ Q86), Y228 (= Y238), D229 (≠ E239), E292 (= E299), D293 (≠ R300)
- binding pyrophosphate 2-: P37 (= P49), S38 (= S50), G39 (= G51), C40 (= C52), G41 (= G53), K42 (= K54), T43 (= T55), T44 (= T56)
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)
40% identity, 96% coverage: 11:368/372 of query aligns to 3:360/369 of P19566
- L86 (= L98) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P176) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D181) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ I320) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 93% coverage: 11:355/372 of query aligns to 2:345/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 93% coverage: 11:355/372 of query aligns to 3:346/371 of P68187
- A85 (= A97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V130) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M133) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A135) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E140) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G153) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D174) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R244) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F255) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (vs. gap) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G289) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ A293) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ S295) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ C314) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ I320) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ D334) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (≠ S349) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (= G355) mutation to S: Normal maltose transport but constitutive mal gene expression.
Sites not aligning to the query:
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
41% identity, 93% coverage: 11:355/372 of query aligns to 2:345/372 of 2awoA
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
41% identity, 93% coverage: 11:355/372 of query aligns to 2:345/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y21), V17 (≠ A30), P36 (= P49), S37 (= S50), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), Q81 (= Q94), R128 (= R145), A132 (≠ Q149), S134 (= S151), G135 (= G152), G136 (= G153), Q137 (= Q154), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94), D157 (= D174)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 93% coverage: 11:355/372 of query aligns to 2:345/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), V17 (≠ A30), S37 (= S50), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (= R145), A132 (≠ Q149), L133 (= L150), S134 (= S151), Q137 (= Q154)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q94), S134 (= S151), G135 (= G152), G136 (= G153), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94), D157 (= D174)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 93% coverage: 11:355/372 of query aligns to 2:345/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), V17 (≠ A30), S37 (= S50), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (= R145), A132 (≠ Q149), S134 (= S151), Q137 (= Q154)
- binding tetrafluoroaluminate ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q94), S134 (= S151), G135 (= G152), G136 (= G153), E158 (= E175), N162 (≠ A179), H191 (= H208)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
41% identity, 92% coverage: 12:355/372 of query aligns to 1:343/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y21), V15 (≠ A30), S35 (= S50), G36 (= G51), C37 (= C52), G38 (= G53), K39 (= K54), S40 (≠ T55), T41 (= T56), R126 (= R145), K129 (≠ T148), A130 (≠ Q149), L131 (= L150), S132 (= S151), G133 (= G152), G134 (= G153), Q135 (= Q154), N160 (≠ A179), H189 (= H208)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
45% identity, 82% coverage: 30:334/372 of query aligns to 21:313/353 of 1vciA
Sites not aligning to the query:
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)
43% identity, 85% coverage: 17:333/372 of query aligns to 9:309/393 of P9WQI3
- H193 (= H208) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
7cagC Mycobacterium smegmatis lpqy-sugabc complex in the catalytic intermediate state (see paper)
48% identity, 64% coverage: 25:263/372 of query aligns to 10:246/362 of 7cagC