SitesBLAST
Comparing GFF1915 PGA1_c19470 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
50% identity, 93% coverage: 21:359/363 of query aligns to 15:370/375 of 2d62A
1g291 Malk (see paper)
50% identity, 93% coverage: 22:360/363 of query aligns to 13:368/372 of 1g291
- binding magnesium ion: D69 (≠ W78), E71 (= E80), K72 (vs. gap), K79 (= K82), D80 (= D83), E292 (= E292), D293 (≠ H293), K359 (≠ A351)
- binding pyrophosphate 2-: S38 (= S47), G39 (= G48), C40 (= C49), G41 (= G50), K42 (= K51), T43 (≠ S52), T44 (= T53)
8hprC Lpqy-sugabc in state 4 (see paper)
47% identity, 93% coverage: 28:363/363 of query aligns to 19:360/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S47), G39 (= G48), G41 (= G50), K42 (= K51), S43 (= S52), Q82 (= Q91), Q133 (≠ E142), G136 (= G145), G137 (= G146), Q138 (= Q147), H192 (= H201)
- binding magnesium ion: S43 (= S52), Q82 (= Q91)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
47% identity, 93% coverage: 28:363/363 of query aligns to 19:359/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S47), C40 (= C49), G41 (= G50), K42 (= K51), S43 (= S52), T44 (= T53), Q82 (= Q91), R129 (= R138), Q133 (≠ E142), S135 (= S144), G136 (= G145), G137 (= G146), Q159 (≠ E168), H192 (= H201)
- binding magnesium ion: S43 (= S52), Q82 (= Q91)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 93% coverage: 28:363/363 of query aligns to 17:381/384 of 8hplC
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)
50% identity, 80% coverage: 28:319/363 of query aligns to 20:321/393 of P9WQI3
- H193 (= H201) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
45% identity, 95% coverage: 11:355/363 of query aligns to 1:354/374 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)
45% identity, 95% coverage: 11:355/363 of query aligns to 1:354/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F22), S37 (= S47), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), Q81 (= Q91), R128 (= R138), A132 (≠ E142), S134 (= S144), G136 (= G146), Q137 (= Q147), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (= S52), Q81 (= Q91)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
45% identity, 95% coverage: 11:355/363 of query aligns to 1:354/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F22), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R138), S134 (= S144), Q137 (= Q147)
- binding beryllium trifluoride ion: S37 (= S47), G38 (= G48), K41 (= K51), Q81 (= Q91), S134 (= S144), G136 (= G146), H191 (= H201)
- binding magnesium ion: S42 (= S52), Q81 (= Q91)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
45% identity, 95% coverage: 11:355/363 of query aligns to 1:354/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F22), V17 (= V27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R138), A132 (≠ E142), S134 (= S144), Q137 (= Q147)
- binding tetrafluoroaluminate ion: S37 (= S47), G38 (= G48), K41 (= K51), Q81 (= Q91), S134 (= S144), G135 (= G145), G136 (= G146), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (= S52), Q81 (= Q91)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
45% identity, 95% coverage: 11:355/363 of query aligns to 1:354/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F22), V17 (= V27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R138), A132 (≠ E142), S134 (= S144), Q137 (= Q147)
- binding magnesium ion: S42 (= S52), Q81 (= Q91)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
45% identity, 95% coverage: 11:355/363 of query aligns to 2:355/371 of P68187
- A85 (= A94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R128) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E133) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G146) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D167) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R237) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F250) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ S277) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (vs. gap) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (vs. gap) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G288) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (vs. gap) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E310) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ N324) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G340) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ N346) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F355) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
46% identity, 94% coverage: 13:355/363 of query aligns to 1:352/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F22), S35 (= S47), G36 (= G48), C37 (= C49), G38 (= G50), K39 (= K51), S40 (= S52), T41 (= T53), R126 (= R138), A130 (≠ E142), S132 (= S144), G134 (= G146), Q135 (= Q147)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
47% identity, 96% coverage: 13:359/363 of query aligns to 7:348/353 of 1vciA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
46% identity, 95% coverage: 11:355/363 of query aligns to 2:353/369 of P19566
- L86 (= L95) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P169) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D174) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E310) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
45% identity, 93% coverage: 19:355/363 of query aligns to 2:324/344 of 2awnC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
48% identity, 75% coverage: 22:292/363 of query aligns to 27:297/378 of P69874
- F27 (= F22) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C49) mutation to T: Loss of ATPase activity and transport.
- L60 (= L55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L130) mutation to M: Loss of ATPase activity and transport.
- D172 (= D167) mutation to N: Loss of ATPase activity and transport.
- C276 (= C273) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E292) 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.
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 95% coverage: 11:355/363 of query aligns to 1:312/330 of 2awnA
3d31A Modbc from methanosarcina acetivorans (see paper)
40% identity, 74% coverage: 28:294/363 of query aligns to 16:276/348 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)
34% identity, 92% coverage: 23:355/363 of query aligns to 16:350/353 of 1oxvD
Sites not aligning to the query:
Query Sequence
>GFF1915 PGA1_c19470 ABC transporter, ATP-binding protein
MKQVKIETMTSHVSARDLSVRFGAVEVLKSLNLDIQKGEFLVLLGASGCGKSTLLNTIAG
LQEATEGQIWINDENVTWREPKDRGLAMVFQSYALYPKMTVRGNLAFGLRMNKVPKAEAD
KLVDEAARVLQLEELLDRRPGELSGGQRQRVAIGRALVRKVDVFLFDEPLSNLDAKLRAE
LRVELKRLHQELGATMIYVTHDQVEALTLADRIAVMKDGVVQQLDSPEEIYRRPANRYVA
QFVGLPSMNFVNGVVTESGAIQTEDFELALDQCNLASTPAPGTEVEIGIRPEHVHPANAG
GFMLDVGMVELLGSERLIWGKVGNTSIVMRDDPDTTIRSGDQVRINLKPGAFSVFSAKTG
LRI
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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