SitesBLAST
Comparing AO356_21615 AO356_21615 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
37% identity, 92% coverage: 1:341/369 of query aligns to 4:351/375 of 2d62A
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)
41% identity, 86% coverage: 1:319/369 of query aligns to 1:320/393 of P9WQI3
- H193 (= H199) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1g291 Malk (see paper)
37% identity, 93% coverage: 1:342/369 of query aligns to 1:349/372 of 1g291
- binding magnesium ion: D69 (= D75), E71 (vs. gap), K72 (vs. gap), K79 (≠ E79), D80 (≠ H80), E292 (= E290), D293 (≠ H293)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
38% identity, 88% coverage: 2:326/369 of query aligns to 1:324/384 of 8hplC
8hprD Lpqy-sugabc in state 4 (see paper)
38% identity, 86% coverage: 2:317/369 of query aligns to 1:317/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (= T50), Q82 (= Q88), R129 (≠ K135), Q133 (≠ N139), S135 (≠ T141), G136 (≠ A142), G137 (≠ D143), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (= S49), Q82 (= Q88)
8hprC Lpqy-sugabc in state 4 (see paper)
38% identity, 86% coverage: 2:317/369 of query aligns to 1:317/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q88), Q133 (≠ N139), G136 (≠ A142), G137 (≠ D143), Q138 (≠ E144), H192 (= H199)
- binding magnesium ion: S43 (= S49), Q82 (= Q88)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
36% identity, 92% coverage: 1:341/369 of query aligns to 4:329/353 of 1vciA
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 85% coverage: 1:315/369 of query aligns to 1:312/371 of P68187
- A85 (≠ V91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I123) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q130) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (≠ D143) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D165) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ T235) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L248) 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 (= G280) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ K284) 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 (≠ A305) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E311) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 85% coverage: 2:315/369 of query aligns to 1:311/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ G19), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q88), R128 (≠ K135), A132 (≠ N139), S134 (≠ T141), G136 (≠ D143), Q137 (≠ E144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 85% coverage: 2:315/369 of query aligns to 1:311/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ G19), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K135), S134 (≠ T141), Q137 (≠ E144)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (≠ T141), G136 (≠ D143), H191 (= H199)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 85% coverage: 2:315/369 of query aligns to 1:311/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ G19), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K135), A132 (≠ N139), S134 (≠ T141), Q137 (≠ E144)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (≠ T141), G135 (≠ A142), G136 (≠ D143), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 85% coverage: 2:315/369 of query aligns to 1:311/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ G19), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K135), A132 (≠ N139), S134 (≠ T141), Q137 (≠ E144)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 85% coverage: 2:315/369 of query aligns to 1:311/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 85% coverage: 4:315/369 of query aligns to 1:309/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ G19), S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (= T50), R126 (≠ K135), A130 (≠ N139), S132 (≠ T141), G134 (≠ D143), Q135 (≠ E144)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
34% identity, 85% coverage: 1:314/369 of query aligns to 1:309/369 of P19566
- L86 (≠ V92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P167) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D172) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E311) 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)
32% identity, 80% coverage: 1:294/369 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)
32% identity, 80% coverage: 1:294/369 of query aligns to 1:283/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
32% identity, 80% coverage: 1:294/369 of query aligns to 1:283/353 of 1oxuA
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)
32% identity, 80% coverage: 1:294/369 of query aligns to 1:283/353 of Q97UY8
- S142 (≠ T141) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (≠ D143) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E166) 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+).
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
33% identity, 85% coverage: 2:315/369 of query aligns to 1:281/344 of 2awnC
Query Sequence
>AO356_21615 AO356_21615 ABC transporter ATP-binding protein
MAEIRLQNLAHSYTSTPAGPEDYAIREMNHIWEQGGAYALLGPSGCGKSTLLNIISGLLS
PSEGQVMFDSKVVNDLTPEHRNIAQVFQFPVVYDTMTVFDNLAFPLRNQGMAEARIHTKV
QEIAEVLDLQNLLDKKARNLTADEKQKVSMGRGLVRDDVSAILFDEPLTVIDPHLKWKLR
RKLKQIHEQFNITMVYVTHDQLEASTFADKIAVMYGGQIVQFGTPRDLFERPSHTFVGYF
IGSPGMNLIEVTAQPGGVGFASTHLPLSETLQRRVAEAEGKSLKVGIRPEFVHVWDGPYD
DAMQADVVHVEDLGTYKILTLNLDGAPLKVRLAEDKPVPEGTAYISFPAQWLMVYADEYL
LEPLSEVQP
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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