SitesBLAST
Comparing 16237 FitnessBrowser__Keio:16237 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
40% identity, 75% coverage: 5:234/308 of query aligns to 30:262/382 of 7ahhC
- binding phosphoaminophosphonic acid-adenylate ester: T39 (≠ Q14), V40 (≠ K15), G41 (≠ A16), S61 (= S36), G62 (= G37), S63 (= S38), G64 (= G39), K65 (= K40), S66 (= S41), T67 (= T42), D187 (= D159), E188 (= E160)
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 272, 273, 275, 295, 296, 297, 298, 357, 370, 372
- binding phosphoaminophosphonic acid-adenylate ester: 12, 29
7aheC Opua inhibited inward facing (see paper)
40% identity, 75% coverage: 5:234/308 of query aligns to 30:262/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 295, 296, 297, 298, 357, 372
7ahdC Opua (e190q) occluded (see paper)
39% identity, 74% coverage: 5:232/308 of query aligns to 30:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ Q14), S61 (= S36), G62 (= G37), S63 (= S38), G64 (= G39), K65 (= K40), S66 (= S41), T67 (= T42), Q111 (= Q82), K161 (≠ H133), Q162 (= Q134), S164 (= S136), G166 (= G138), M167 (≠ Q139), Q188 (≠ E160), H221 (= H193)
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)
39% identity, 78% coverage: 2:240/308 of query aligns to 3:238/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F11), V17 (≠ A16), P36 (≠ T35), S37 (= S36), G38 (= G37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (= S41), T43 (= T42), Q81 (= Q82), R128 (= R130), A132 (≠ Q134), S134 (= S136), G135 (= G137), G136 (= G138), Q137 (= Q139), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (= S41), Q81 (= Q82), D157 (= D159)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 78% coverage: 2:240/308 of query aligns to 3:238/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (≠ A16), S37 (= S36), G38 (= G37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (= S41), T43 (= T42), R128 (= R130), A132 (≠ Q134), L133 (= L135), S134 (= S136), Q137 (= Q139)
- binding beryllium trifluoride ion: S37 (= S36), G38 (= G37), K41 (= K40), Q81 (= Q82), S134 (= S136), G135 (= G137), G136 (= G138), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (= S41), Q81 (= Q82), D157 (= D159)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 78% coverage: 2:240/308 of query aligns to 3:238/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (≠ A16), S37 (= S36), G38 (= G37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (= S41), T43 (= T42), R128 (= R130), A132 (≠ Q134), S134 (= S136), Q137 (= Q139)
- binding tetrafluoroaluminate ion: S37 (= S36), G38 (= G37), K41 (= K40), Q81 (= Q82), S134 (= S136), G135 (= G137), G136 (= G138), E158 (= E160), N162 (≠ A164), H191 (= H193)
- binding magnesium ion: S42 (= S41), Q81 (= Q82)
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
39% identity, 78% coverage: 2:240/308 of query aligns to 3:238/372 of 2awoA
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 78% coverage: 2:240/308 of query aligns to 3:238/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 78% coverage: 2:240/308 of query aligns to 4:239/371 of P68187
- A85 (≠ G85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S125) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G138) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D159) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D229) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 78% coverage: 2:240/308 of query aligns to 1:236/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F11), V15 (≠ A16), S35 (= S36), G36 (= G37), C37 (≠ S38), G38 (= G39), K39 (= K40), S40 (= S41), T41 (= T42), R126 (= R130), K129 (≠ H133), A130 (≠ Q134), L131 (= L135), S132 (= S136), G133 (= G137), G134 (= G138), Q135 (= Q139), N160 (≠ A164), H189 (= H193)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
38% identity, 78% coverage: 2:240/308 of query aligns to 4:239/369 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 (= P161) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D166) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
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)
42% identity, 76% coverage: 2:236/308 of query aligns to 4:236/393 of P9WQI3
- H193 (= H193) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 77% coverage: 1:236/308 of query aligns to 17:249/378 of P69874
- C26 (≠ L10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F29) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S38) mutation to T: Loss of ATPase activity and transport.
- L60 (= L44) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F60) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D159) 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.
8hplC ABC transporter, ATP-binding protein SugC (see paper)
40% identity, 79% coverage: 2:244/308 of query aligns to 3:251/384 of 8hplC
1g291 Malk (see paper)
40% identity, 76% coverage: 2:236/308 of query aligns to 4:241/372 of 1g291
- binding magnesium ion: D69 (≠ L68), E71 (vs. gap), K72 (vs. gap), K79 (≠ L73), D80 (≠ R74), Y228 (≠ L223), D229 (≠ T224)
- binding pyrophosphate 2-: P37 (≠ T35), S38 (= S36), G39 (= G37), C40 (≠ S38), G41 (= G39), K42 (= K40), T43 (≠ S41), T44 (= T42)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
39% identity, 78% coverage: 2:242/308 of query aligns to 7:236/353 of 1vciA
8hprD ABC transporter, ATP-binding protein SugC (see paper)
40% identity, 79% coverage: 2:244/308 of query aligns to 3:253/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F11), S38 (= S36), C40 (≠ S38), G41 (= G39), K42 (= K40), S43 (= S41), T44 (= T42), Q82 (= Q82), R129 (= R130), G132 (≠ H133), Q133 (= Q134), S135 (= S136), G136 (= G137), G137 (= G138), Q138 (= Q139), Q159 (≠ E160), H192 (= H193)
- binding magnesium ion: S43 (= S41), Q82 (= Q82), D158 (= D159)
8hprC ABC transporter, ATP-binding protein SugC (see paper)
40% identity, 79% coverage: 2:244/308 of query aligns to 3:253/363 of 8hprC