SitesBLAST
Comparing PfGW456L13_1569 Putrescine transport ATP-binding protein PotA (TC 3.A.1.11.1) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
48% 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 (≠ F85), D80 (≠ Q86), E292 (= E299), D293 (≠ R300)
- binding pyrophosphate 2-: 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)
41% identity, 96% coverage: 11:367/372 of query aligns to 3:359/369 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
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), S37 (= S50), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), Q81 (= Q94), R128 (= R145), A132 (≠ Q149), S134 (= S151), G136 (= G153), Q137 (= Q154), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
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), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (= R145), S134 (= S151), Q137 (= Q154)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q94), S134 (= S151), G136 (= G153), H191 (= H208)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
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), 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), H191 (= H208)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 93% coverage: 11:355/372 of query aligns to 2:345/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), V17 (≠ A30), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (= R145), A132 (≠ Q149), S134 (= S151), Q137 (= Q154)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
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 (≠ G118) 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 (≠ T293) 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.
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), S35 (= S50), G36 (= G51), C37 (= C52), G38 (= G53), K39 (= K54), S40 (≠ T55), T41 (= T56), R126 (= R145), A130 (≠ Q149), S132 (= S151), G134 (= G153), Q135 (= Q154)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
43% identity, 88% coverage: 7:334/372 of query aligns to 2:313/353 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, 78% coverage: 12:302/372 of query aligns to 4:288/393 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.
8hprD Lpqy-sugabc in state 4 (see paper)
47% identity, 66% coverage: 17:263/372 of query aligns to 8:249/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y21), S38 (= S50), C40 (= C52), G41 (= G53), K42 (= K54), S43 (≠ T55), T44 (= T56), Q82 (= Q94), R129 (= R145), Q133 (= Q149), S135 (= S151), G136 (= G152), G137 (= G153), Q159 (≠ E175), H192 (= H208)
- binding magnesium ion: S43 (≠ T55), Q82 (= Q94)
8hprC Lpqy-sugabc in state 4 (see paper)
47% identity, 66% coverage: 17:263/372 of query aligns to 8:249/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y21), S38 (= S50), G39 (= G51), G41 (= G53), K42 (= K54), S43 (≠ T55), Q82 (= Q94), Q133 (= Q149), G136 (= G152), G137 (= G153), Q138 (= Q154), H192 (= H208)
- binding magnesium ion: S43 (≠ T55), Q82 (= Q94)
8hplC Lpqy-sugabc in state 1 (see paper)
48% identity, 63% coverage: 30:263/372 of query aligns to 16:247/384 of 8hplC
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
39% identity, 81% coverage: 30:330/372 of query aligns to 15:309/348 of 3d31A
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 87% coverage: 32:355/372 of query aligns to 12:315/344 of 2awnC
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 67% coverage: 12:261/372 of query aligns to 4:252/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 67% coverage: 12:261/372 of query aligns to 4:252/353 of 1oxvA
Query Sequence
>PfGW456L13_1569 Putrescine transport ATP-binding protein PotA (TC 3.A.1.11.1)
MNALHSLQTLAVSIRSVRKVYGDPKTGPVALKSIDLDIRDNEFFTLLGPSGCGKTTLLRM
IAGFEFPTEGEILLYGENIADRPPFQRPVNTVFQHYALFPHMTIAENLAFGLESHPMGKV
LHKTQLAERVREMLALVQMERFANRKPAQLSGGQQQRVALARALAPHPKVLLLDEPLSAL
DLKLRQAMREELKTIQARTGITFIFVTHDQEEALTMSDRIAVLSEGEVQQVGRPEDIYER
PRNRFVADFIGETNFIEGTVTRVEDGLAWFAGPAGHPLPAQPCSDVRVGANVTLSVRPER
LHLVPATTENALPCRIEAQIYLGTDLQYQVSLSDGSRLTVRTPNCVDQSKRFAVGSQAGL
LFDQGSASVLHD
Or try a new SitesBLAST search
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