SitesBLAST
Comparing Ac3H11_1002 FitnessBrowser__acidovorax_3H11:Ac3H11_1002 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
50% identity, 66% coverage: 11:245/356 of query aligns to 5:244/375 of 2d62A
1g291 Malk (see paper)
45% identity, 76% coverage: 28:299/356 of query aligns to 18:290/372 of 1g291
- binding magnesium ion: D69 (= D79), E71 (vs. gap), K72 (vs. gap), K79 (≠ A83), D80 (≠ A84)
- binding pyrophosphate 2-: S38 (= S48), G39 (= G49), C40 (= C50), G41 (= G51), K42 (= K52), T43 (≠ S53), T44 (= T54)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
51% identity, 65% coverage: 20:251/356 of query aligns to 24:255/378 of P69874
- C26 (≠ Y22) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ A23) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ Y41) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C50) mutation to T: Loss of ATPase activity and transport.
- L60 (= L56) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L72) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V131) mutation to M: Loss of ATPase activity and transport.
- D172 (= D168) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
43% identity, 92% coverage: 11:336/356 of query aligns to 2:315/369 of P19566
- L86 (= L96) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P170) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D175) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E319) 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)
47% identity, 74% coverage: 11:274/356 of query aligns to 1:258/374 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)
47% identity, 74% coverage: 11:274/356 of query aligns to 1:258/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y22), S37 (= S48), G38 (= G49), C39 (= C50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), Q81 (= Q92), R128 (= R139), A132 (≠ E143), S134 (= S145), G136 (= G147), Q137 (= Q148), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (= S53), Q81 (= Q92)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
47% identity, 74% coverage: 11:274/356 of query aligns to 1:258/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), G38 (= G49), C39 (= C50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), R128 (= R139), S134 (= S145), Q137 (= Q148)
- binding beryllium trifluoride ion: S37 (= S48), G38 (= G49), K41 (= K52), Q81 (= Q92), S134 (= S145), G136 (= G147), H191 (= H202)
- binding magnesium ion: S42 (= S53), Q81 (= Q92)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
47% identity, 74% coverage: 11:274/356 of query aligns to 1:258/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), V17 (≠ P27), G38 (= G49), C39 (= C50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), R128 (= R139), A132 (≠ E143), S134 (= S145), Q137 (= Q148)
- binding tetrafluoroaluminate ion: S37 (= S48), G38 (= G49), K41 (= K52), Q81 (= Q92), S134 (= S145), G135 (= G146), G136 (= G147), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (= S53), Q81 (= Q92)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
47% identity, 74% coverage: 11:274/356 of query aligns to 1:258/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), V17 (≠ P27), G38 (= G49), C39 (= C50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), R128 (= R139), A132 (≠ E143), S134 (= S145), Q137 (= Q148)
- binding magnesium ion: S42 (= S53), Q81 (= Q92)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
47% identity, 74% coverage: 11:274/356 of query aligns to 2:259/371 of P68187
- A85 (= A95) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L127) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E129) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G134) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G147) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D168) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E238) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ D251) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
49% identity, 68% coverage: 32:274/356 of query aligns to 19:256/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S48), G36 (= G49), C37 (= C50), G38 (= G51), K39 (= K52), S40 (= S53), T41 (= T54), R126 (= R139), A130 (≠ E143), S132 (= S145), G134 (= G147), Q135 (= Q148)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
46% identity, 70% coverage: 11:260/356 of query aligns to 1:252/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y22), S38 (= S48), G39 (= G49), G41 (= G51), K42 (= K52), S43 (= S53), Q82 (= Q92), Q133 (≠ E143), G136 (= G146), G137 (= G147), Q138 (= Q148), H192 (= H202)
- binding magnesium ion: S43 (= S53), Q82 (= Q92)
8hprD Lpqy-sugabc in state 4 (see paper)
46% identity, 70% coverage: 11:260/356 of query aligns to 1:252/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y22), S38 (= S48), C40 (= C50), G41 (= G51), K42 (= K52), S43 (= S53), T44 (= T54), Q82 (= Q92), R129 (= R139), Q133 (≠ E143), S135 (= S145), G136 (= G146), G137 (= G147), Q159 (≠ E169), H192 (= H202)
- binding magnesium ion: S43 (= S53), Q82 (= Q92)
8hplC Lpqy-sugabc in state 1 (see paper)
46% identity, 70% coverage: 11:260/356 of query aligns to 1:250/384 of 8hplC
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, 66% coverage: 11:245/356 of query aligns to 2:236/393 of P9WQI3
- H193 (= H202) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 87% coverage: 13:323/356 of query aligns to 7:298/353 of 1vciA
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
45% identity, 68% coverage: 32:274/356 of query aligns to 14:228/344 of 2awnC
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
42% identity, 67% coverage: 13:250/356 of query aligns to 2:234/348 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)
39% identity, 67% coverage: 18:257/356 of query aligns to 9:251/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 67% coverage: 18:257/356 of query aligns to 9:251/353 of 1oxvA
Query Sequence
>Ac3H11_1002 FitnessBrowser__acidovorax_3H11:Ac3H11_1002
MHATTSAQAPAAIEIVALTKRYASGKPAVDAINLRIASGSYCCLLGPSGCGKSTTLRMIA
GHESVTSGDILLENRNITDLPAAARGTAMMFQSFALFPHLSALDNVAFSLKMKGVPKAER
QAKARDLLERVALGHLAERKPAELSGGQQQRVALARALITQPRVLLLDEPLSALDPFLRI
QMRAELRRWQKELGLTFIHVTHSQEEAMALADTMVVMNHGVIEQVGSPHEVYNRPASEFV
ARFMGGHNVIDTPEGKVGVRTDHLQIAPASAELPWGAQRMLAVVTDVEYQGTYVLLGLQK
QGVALSANATAAYSVMVSEAAFAAQPYRVGQGVQLHWTPDQAHPLSVPAPAMAAAV
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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