SitesBLAST
Comparing NP_349832.1 NCBI__GCF_000008765.1:NP_349832.1 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)
1g291 Malk (see paper)
53% identity, 100% coverage: 1:369/369 of query aligns to 1:372/372 of 1g291
- binding magnesium ion: D69 (= D70), E71 (vs. gap), K72 (vs. gap), K79 (= K74), D80 (= D75), E292 (= E290), D293 (≠ N291), K359 (= K356)
- binding pyrophosphate 2-: S38 (= S39), G39 (= G40), C40 (= C41), G41 (= G42), K42 (= K43), T43 (≠ S44), T44 (= T45)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
52% identity, 100% coverage: 1:369/369 of query aligns to 4:375/375 of 2d62A
8hprC Lpqy-sugabc in state 4 (see paper)
52% identity, 98% coverage: 2:364/369 of query aligns to 1:356/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S39), G39 (= G40), G41 (= G42), K42 (= K43), S43 (= S44), Q82 (= Q83), Q133 (≠ A134), G136 (= G137), G137 (= G138), Q138 (= Q139), H192 (= H193)
- binding magnesium ion: S43 (= S44), Q82 (= Q83)
8hprD Lpqy-sugabc in state 4 (see paper)
52% identity, 98% coverage: 2:364/369 of query aligns to 1:355/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S39), C40 (= C41), G41 (= G42), K42 (= K43), S43 (= S44), T44 (= T45), Q82 (= Q83), R129 (= R130), Q133 (≠ A134), S135 (= S136), G136 (= G137), G137 (= G138), Q159 (≠ E160), H192 (= H193)
- binding magnesium ion: S43 (= S44), Q82 (= Q83)
8hplC Lpqy-sugabc in state 1 (see paper)
50% identity, 98% coverage: 2:364/369 of query aligns to 1:377/384 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)
49% identity, 99% coverage: 1:364/369 of query aligns to 1:383/393 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
49% identity, 98% coverage: 1:363/369 of query aligns to 1:358/371 of P68187
- A85 (= A86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P107) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A118) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E120) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A125) 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 (≠ M229) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F242) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ M255) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ S266) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (= S270) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G286) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ A309) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E315) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ K327) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G345) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (= G351) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F360) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
50% identity, 98% coverage: 1:363/369 of query aligns to 1:356/369 of P19566
- L86 (= L87) 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.
- E306 (= E315) 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)
49% identity, 98% coverage: 2:363/369 of query aligns to 1:357/374 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)
49% identity, 98% coverage: 2:363/369 of query aligns to 1:357/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S39), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), Q81 (= Q83), R128 (= R130), A132 (= A134), S134 (= S136), G136 (= G138), Q137 (= Q139), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
49% identity, 98% coverage: 2:363/369 of query aligns to 1:357/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), R128 (= R130), S134 (= S136), Q137 (= Q139)
- binding beryllium trifluoride ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S136), G136 (= G138), H191 (= H193)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
49% identity, 98% coverage: 2:363/369 of query aligns to 1:357/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ A19), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), R128 (= R130), A132 (= A134), S134 (= S136), Q137 (= Q139)
- binding tetrafluoroaluminate ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S136), G135 (= G137), G136 (= G138), E158 (= E160), H191 (= H193)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
49% identity, 98% coverage: 2:363/369 of query aligns to 1:357/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ A19), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), R128 (= R130), A132 (= A134), S134 (= S136), Q137 (= Q139)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
49% identity, 98% coverage: 4:363/369 of query aligns to 1:355/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S39), G36 (= G40), C37 (= C41), G38 (= G42), K39 (= K43), S40 (= S44), T41 (= T45), R126 (= R130), A130 (= A134), S132 (= S136), G134 (= G138), Q135 (= Q139)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
49% identity, 100% coverage: 1:369/369 of query aligns to 4:353/353 of 1vciA
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
47% identity, 94% coverage: 16:363/369 of query aligns to 7:327/344 of 2awnC
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 98% coverage: 2:363/369 of query aligns to 1:315/330 of 2awnA
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 78% coverage: 4:292/369 of query aligns to 18:299/378 of P69874
- C26 (≠ V12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F32) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C41) mutation to T: Loss of ATPase activity and transport.
- L60 (= L47) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I63) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L122) mutation to M: Loss of ATPase activity and transport.
- D172 (= D159) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ I263) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E290) 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)
34% identity, 98% coverage: 1:362/369 of query aligns to 1:352/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 98% coverage: 1:362/369 of query aligns to 1:352/353 of 1oxvA
Query Sequence
>NP_349832.1 NCBI__GCF_000008765.1:NP_349832.1
MADLSLKHIYKVYDGNVTAVKDFNLDVADKEFIVFVGPSGCGKSTTLRMIAGLEEITKGE
LTIGGRVVNDVSPKDRDIAMVFQNYALYPHMTVYENMAFGLKLRKTPKDVIDEKVKKAAE
ILDIAHLLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQMRTEIAKL
HKDLQNTFIYVTHDQTEAMTLGTRIVVMKDGVIQQVDTPQNIYEKPKNMFVAGFIGSPQM
NFVDSKVTEDSGKIMVSVEGQEIPVSGDISKILKENGYINKEVILGIRPENMDESPEFLQ
KHKDAIINAKVEVTELMGAETYIHLAKGKANFIVRVNGASTSKAGDEIKIGININKLHVF
DKETEETIL
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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