SitesBLAST
Comparing PfGW456L13_4763 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)
43% identity, 97% coverage: 5:339/345 of query aligns to 18:374/378 of P69874
- C26 (≠ Q13) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F14) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F32) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S41) mutation to T: Loss of ATPase activity and transport.
- L60 (= L47) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I63) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V122) mutation to M: Loss of ATPase activity and transport.
- D172 (= D159) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E261) 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
54% identity, 68% coverage: 5:237/345 of query aligns to 7:245/375 of 2d62A
1g291 Malk (see paper)
53% identity, 68% coverage: 4:237/345 of query aligns to 3:242/372 of 1g291
- binding magnesium ion: D69 (≠ H64), E71 (= E66), K72 (≠ E67), K79 (≠ Y74), D80 (≠ Q75)
- binding pyrophosphate 2-: S38 (= S39), G39 (= G40), C40 (≠ S41), G41 (= G42), K42 (= K43), T43 (= T44), T44 (= T45)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
44% identity, 75% coverage: 5:263/345 of query aligns to 7:278/353 of 1vciA
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, 72% coverage: 19:266/345 of query aligns to 19:290/393 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.
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 66% coverage: 10:237/345 of query aligns to 8:236/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S39), G39 (= G40), G41 (= G42), K42 (= K43), S43 (≠ T44), Q82 (= Q83), Q133 (= Q134), G136 (= G137), G137 (= G138), Q138 (= Q139), H192 (= H193)
- binding magnesium ion: S43 (≠ T44), Q82 (= Q83)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
47% identity, 68% coverage: 4:237/345 of query aligns to 3:236/369 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.
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 66% coverage: 10:237/345 of query aligns to 8:236/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S39), C40 (≠ S41), G41 (= G42), K42 (= K43), S43 (≠ T44), T44 (= T45), Q82 (= Q83), R129 (= R130), Q133 (= Q134), S135 (= S136), G136 (= G137), G137 (= G138), Q159 (≠ E160), H192 (= H193)
- binding magnesium ion: S43 (≠ T44), Q82 (= Q83)
8hplC Lpqy-sugabc in state 1 (see paper)
49% identity, 63% coverage: 19:237/345 of query aligns to 16:234/384 of 8hplC
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
46% identity, 68% coverage: 4:237/345 of query aligns to 2:235/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
46% identity, 68% coverage: 4:237/345 of query aligns to 3:236/371 of P68187
- A85 (= A86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ G107) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A118) 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 (≠ G125) 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.
- R228 (≠ T229) 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)
46% identity, 68% coverage: 4:237/345 of query aligns to 2:235/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F14), S37 (= S39), G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), Q81 (= Q83), R128 (= R130), A132 (≠ Q134), S134 (= S136), G136 (= G138), Q137 (= Q139), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
46% identity, 68% coverage: 4:237/345 of query aligns to 2:235/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F14), G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), R128 (= R130), S134 (= S136), Q137 (= Q139)
- binding beryllium trifluoride ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S136), G136 (= G138), H191 (= H193)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
46% identity, 68% coverage: 4:237/345 of query aligns to 2:235/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A19), G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), R128 (= R130), A132 (≠ Q134), S134 (= S136), Q137 (= Q139)
- binding tetrafluoroaluminate ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S136), G135 (= G137), G136 (= G138), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
46% identity, 68% coverage: 4:237/345 of query aligns to 2:235/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A19), G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), R128 (= R130), A132 (≠ Q134), S134 (= S136), Q137 (= Q139)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
46% identity, 68% coverage: 5:237/345 of query aligns to 1:233/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F14), S35 (= S39), G36 (= G40), C37 (≠ S41), G38 (= G42), K39 (= K43), S40 (≠ T44), T41 (= T45), R126 (= R130), A130 (≠ Q134), S132 (= S136), G134 (= G138), Q135 (= Q139)
3d31A Modbc from methanosarcina acetivorans (see paper)
42% identity, 69% coverage: 5:243/345 of query aligns to 2:236/348 of 3d31A
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, 83% coverage: 9:295/345 of query aligns to 8:315/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 83% coverage: 9:295/345 of query aligns to 8:315/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 83% coverage: 9:295/345 of query aligns to 8:315/353 of 1oxuA
Query Sequence
>PfGW456L13_4763 Putrescine transport ATP-binding protein PotA (TC 3.A.1.11.1)
MTLAVQFTNVSRQFGEVKAVDRVSIDIQDGEFFSMLGPSGSGKTTCLRLIAGFEQPSAGS
IRIHGEEAAGLPPYQRDVNTVFQDYALFPHMNVRDNVAYGLKVKGVGKAERLKRAEEALD
MVALGGYGERKPVQLSGGQRQRVALARALVNRPRVLLLDEPLGALDLKLREQMQGELKKL
QRQLGITFIFVTHDQTEALSMSDRVAVFNKGRIEQVDSPRNLYMKPATTFVAEFVGTSNV
IRGDLAWQLSGNPQPFSIRPEHVRFAEGPLASHEIEVSGLLHDIQYQGSATRYELKLENG
QTLNISKANNQWLDTSAQHQTGQRISARWAREAMIPLHDTVAGGV
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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