SitesBLAST
Comparing 209225 DVU0291 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 67% coverage: 7:242/354 of query aligns to 22:257/378 of P69874
- C26 (≠ T11) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ L12) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ V39) mutation to T: Loss of ATPase activity and transport.
- L60 (= L45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (vs. gap) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ F115) mutation to M: Loss of ATPase activity and transport.
- D172 (= D157) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 62% coverage: 17:234/354 of query aligns to 17:234/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
43% identity, 62% coverage: 17:234/354 of query aligns to 15:232/367 of 1q12A
- binding adenosine-5'-triphosphate: V15 (= V17), S35 (= S37), G36 (= G38), C37 (≠ V39), G38 (= G40), K39 (= K41), S40 (≠ T42), T41 (= T43), R126 (= R128), K129 (≠ A131), A130 (≠ Q132), L131 (= L133), S132 (= S134), G133 (≠ A135), G134 (= G136), Q135 (= Q137), N160 (= N162), H189 (= H191)
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
43% identity, 62% coverage: 17:234/354 of query aligns to 18:235/371 of P68187
- A85 (≠ L79) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R100) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V108) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M111) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R113) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A123) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G136) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D157) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E227) 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.
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
43% identity, 62% coverage: 17:234/354 of query aligns to 17:234/372 of 2awoA
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
43% identity, 62% coverage: 17:234/354 of query aligns to 17:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: V17 (= V17), P36 (= P36), S37 (= S37), G38 (= G38), C39 (≠ V39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (= T43), Q81 (= Q76), R128 (= R128), A132 (≠ Q132), S134 (= S134), G135 (≠ A135), G136 (= G136), Q137 (= Q137), E158 (= E158), H191 (= H191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q76), D157 (= D157)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
43% identity, 62% coverage: 17:234/354 of query aligns to 17:234/371 of 3puxA
- binding adenosine-5'-diphosphate: V17 (= V17), S37 (= S37), G38 (= G38), C39 (≠ V39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (= T43), R128 (= R128), A132 (≠ Q132), L133 (= L133), S134 (= S134), Q137 (= Q137)
- binding beryllium trifluoride ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q76), S134 (= S134), G135 (≠ A135), G136 (= G136), E158 (= E158), H191 (= H191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q76), D157 (= D157)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
43% identity, 62% coverage: 17:234/354 of query aligns to 17:234/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V17), S37 (= S37), G38 (= G38), C39 (≠ V39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (= T43), R128 (= R128), A132 (≠ Q132), S134 (= S134), Q137 (= Q137)
- binding tetrafluoroaluminate ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q76), S134 (= S134), G135 (≠ A135), G136 (= G136), E158 (= E158), N162 (= N162), H191 (= H191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q76)
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)
36% identity, 83% coverage: 17:310/354 of query aligns to 18:315/369 of P19566
- L86 (= L80) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P159) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D164) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ D301) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 63% coverage: 18:240/354 of query aligns to 21:248/353 of 1oxvD
- binding phosphoaminophosphonic acid-adenylate ester: P39 (= P36), S40 (= S37), G41 (= G38), A42 (≠ V39), G43 (= G40), K44 (= K41), T45 (= T42), T46 (= T43), Q89 (= Q76), E166 (= E158)
- binding magnesium ion: T45 (= T42), Q89 (= Q76)
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 63% coverage: 18:240/354 of query aligns to 21:248/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 63% coverage: 18:240/354 of query aligns to 21:248/353 of 1oxuA
Sites not aligning to the query:
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
40% identity, 63% coverage: 18:240/354 of query aligns to 21:248/353 of Q97UY8
- S142 (= S134) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G136) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E158) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
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)
35% identity, 91% coverage: 14:334/354 of query aligns to 16:345/393 of P9WQI3
- H193 (= H191) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
40% identity, 64% coverage: 18:242/354 of query aligns to 22:254/375 of 2d62A
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 62% coverage: 17:234/354 of query aligns to 10:204/344 of 2awnC
1g291 Malk (see paper)
40% identity, 63% coverage: 18:240/354 of query aligns to 19:249/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q65), D80 (≠ G66), Y228 (= Y221), D229 (≠ R222)
- binding pyrophosphate 2-: P37 (= P36), S38 (= S37), G39 (= G38), C40 (≠ V39), G41 (= G40), K42 (= K41), T43 (= T42), T44 (= T43)
Sites not aligning to the query:
7cagC Mycobacterium smegmatis lpqy-sugabc complex in the catalytic intermediate state (see paper)
37% identity, 73% coverage: 18:276/354 of query aligns to 16:276/362 of 7cagC
- binding adenosine-5'-triphosphate: P34 (= P36), S35 (= S37), G36 (= G38), C37 (≠ V39), G38 (= G40), K39 (= K41), S40 (≠ T42), T41 (= T43), Q79 (= Q76), L123 (≠ M125), R126 (= R128), Q130 (= Q132), S132 (= S134), G133 (≠ A135), G134 (= G136), Q135 (= Q137)
- binding magnesium ion: