SitesBLAST
Comparing AO356_28585 FitnessBrowser__pseudo5_N2C3_1:AO356_28585 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)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
55% identity, 94% coverage: 4:359/379 of query aligns to 4:362/369 of P19566
- L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P160) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D165) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E304) 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)
54% identity, 94% coverage: 4:359/379 of query aligns to 3:363/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
54% identity, 94% coverage: 4:359/379 of query aligns to 4:364/371 of P68187
- A85 (= A85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ T117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ Q119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D158) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F241) 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 (≠ N275) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (= S279) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G281) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G302) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E304) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (vs. gap) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (≠ N329) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (= G335) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F350) mutation to 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)
54% identity, 94% coverage: 4:359/379 of query aligns to 3:363/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ L13), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (≠ E133), S134 (= S135), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
54% identity, 94% coverage: 4:359/379 of query aligns to 3:363/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ L13), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), S134 (= S135), Q137 (= Q138)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
54% identity, 94% coverage: 4:359/379 of query aligns to 3:363/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ L13), V17 (≠ I18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ E133), S134 (= S135), Q137 (= Q138)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
54% identity, 94% coverage: 4:359/379 of query aligns to 3:363/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ L13), V17 (≠ I18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ E133), S134 (= S135), Q137 (= Q138)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
54% identity, 94% coverage: 4:359/379 of query aligns to 1:361/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ L13), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (= S43), T41 (= T44), R126 (= R129), A130 (≠ E133), S132 (= S135), G134 (= G137), Q135 (= Q138)
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)
48% identity, 92% coverage: 3:351/379 of query aligns to 3:380/393 of P9WQI3
- H193 (= H192) 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)
47% identity, 92% coverage: 3:351/379 of query aligns to 2:353/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ L13), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (= S43), Q82 (= Q82), Q133 (≠ E133), G136 (= G136), G137 (= G137), Q138 (= Q138), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
51% identity, 92% coverage: 12:359/379 of query aligns to 4:333/344 of 2awnC
8hprD Lpqy-sugabc in state 4 (see paper)
47% identity, 92% coverage: 3:351/379 of query aligns to 2:352/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ L13), S38 (= S38), C40 (= C40), G41 (= G41), K42 (= K42), S43 (= S43), T44 (= T44), Q82 (= Q82), R129 (= R129), Q133 (≠ E133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82)
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 92% coverage: 3:351/379 of query aligns to 2:374/384 of 8hplC
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 92% coverage: 3:350/379 of query aligns to 6:366/375 of 2d62A
1g291 Malk (see paper)
47% identity, 93% coverage: 4:357/379 of query aligns to 4:371/372 of 1g291
- binding magnesium ion: D69 (= D69), E71 (= E71), K72 (vs. gap), K79 (≠ R73), D80 (≠ E74), E292 (= E285), D293 (≠ H286), K359 (≠ N346)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (≠ S43), T44 (= T44)
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
46% identity, 94% coverage: 4:359/379 of query aligns to 3:321/330 of 2awnA
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
44% identity, 93% coverage: 1:351/379 of query aligns to 4:345/353 of 1vciA
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 83% coverage: 4:318/379 of query aligns to 18:337/378 of P69874
- C26 (≠ Q12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ L13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C40) mutation to T: Loss of ATPase activity and transport.
- L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ S264) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E285) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 76% coverage: 1:289/379 of query aligns to 1:283/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 76% coverage: 1:289/379 of query aligns to 1:283/353 of 1oxvA
Query Sequence
>AO356_28585 FitnessBrowser__pseudo5_N2C3_1:AO356_28585
VIKLKLDNVNKQLGGARILRDVSLEISAGEFVVFVGPSGCGKSTLLRLIAGLDSICGGDL
LIDGRRVNDLEPRERGVGMVFQSYALYPHMSVYDNISFGLKLAKTEKTSLRERVLKTAQI
LQLDKLLQRKPRELSGGQRQRVAMGRAMAREPDILLFDEPLSNLDASLRVQMRNEIARLH
GRLGSTMIYVTHDQVEAMTLADKIVVLNGGRIEQVGSPRELYERPASRFVAGFLGSPRMN
FLAAFLHTPGETSQVESLVLGMTSLPFDSSGLAANTQLSLGIRPEHIALKAAQGTAGIAV
SGVEYLGSETYVHLDTGQDDPMVCRCEVNAGWRVGDRVELQLDIDNLHVFDTHGTALQRH
AIDRLPDDVALRPAHAGAL
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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