SitesBLAST
Comparing Pf1N1B4_4847 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4847 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)
52% identity, 98% coverage: 1:361/367 of query aligns to 1:362/369 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 (= E306) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
51% identity, 98% coverage: 1:361/367 of query aligns to 1:364/371 of P68187
- A85 (= A85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G124) 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 (≠ L228) 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 (≠ T265) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G276) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T280) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G282) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ V300) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E306) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (= S319) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G337) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ H343) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F352) 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)
51% identity, 98% coverage: 2:361/367 of query aligns to 1:363/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F13), V17 (≠ I18), P36 (= P37), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (≠ Q133), S134 (= S135), G135 (= G136), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82), D157 (= D158)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
51% identity, 98% coverage: 2:361/367 of query aligns to 1:363/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ I18), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ Q133), L133 (= L134), S134 (= S135), Q137 (= Q138)
- binding beryllium trifluoride 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), D157 (= D158)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
51% identity, 98% coverage: 2:361/367 of query aligns to 1:363/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ I18), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ Q133), S134 (= S135), Q137 (= Q138)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), N162 (= N163), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
51% identity, 98% coverage: 2:361/367 of query aligns to 1:363/374 of 2awnB
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
51% identity, 98% coverage: 2:361/367 of query aligns to 1:363/372 of 2awoA
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
51% identity, 98% coverage: 4:361/367 of query aligns to 1:361/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F13), V15 (≠ I18), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (= S43), T41 (= T44), R126 (= R129), K129 (= K132), A130 (≠ Q133), L131 (= L134), S132 (= S135), G133 (= G136), G134 (= G137), Q135 (= Q138), N160 (= N163), H189 (= H192)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
50% identity, 95% coverage: 13:361/367 of query aligns to 5:333/344 of 2awnC
8hprC ABC transporter, ATP-binding protein SugC (see paper)
48% identity, 93% coverage: 19:361/367 of query aligns to 19:362/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), S43 (= S43), T44 (= T44), Q82 (= Q82), G132 (≠ K132), Q133 (= Q133), L134 (= L134), S135 (= S135), G136 (= G136), G137 (= G137), Q138 (= Q138), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82)
Sites not aligning to the query:
8hprD ABC transporter, ATP-binding protein SugC (see paper)
48% identity, 93% coverage: 19:361/367 of query aligns to 19:361/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S38), C40 (= C40), G41 (= G41), K42 (= K42), S43 (= S43), T44 (= T44), Q82 (= Q82), R129 (= R129), G132 (≠ K132), Q133 (= Q133), S135 (= S135), G136 (= G136), G137 (= G137), Q138 (= Q138), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82), D158 (= D158)
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)
44% identity, 99% coverage: 1:365/367 of query aligns to 1:393/393 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.
8hplC ABC transporter, ATP-binding protein SugC (see paper)
47% identity, 93% coverage: 19:361/367 of query aligns to 17:383/384 of 8hplC