SitesBLAST
Comparing Ac3H11_792 FitnessBrowser__acidovorax_3H11:Ac3H11_792 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)
39% identity, 87% coverage: 23:332/358 of query aligns to 18:345/372 of 1g291
- binding magnesium ion: D69 (≠ R74), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q78), D80 (≠ E79), E292 (= E284), D293 (≠ Y285)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (= T48), T44 (= T49)
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, 85% coverage: 23:326/358 of query aligns to 21:320/353 of 1vciA
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
34% identity, 93% coverage: 23:355/358 of query aligns to 21:371/375 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)
40% identity, 80% coverage: 1:286/358 of query aligns to 1:287/393 of P9WQI3
- H193 (= H198) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprC Lpqy-sugabc in state 4 (see paper)
39% identity, 80% coverage: 2:286/358 of query aligns to 1:286/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ K13), S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (≠ T48), Q82 (= Q87), Q133 (≠ G138), G136 (≠ A141), G137 (≠ D142), Q138 (≠ A143), H192 (= H198)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q87)
8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 80% coverage: 2:286/358 of query aligns to 1:286/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ K13), S38 (= S43), C40 (= C45), G41 (= G46), K42 (= K47), S43 (≠ T48), T44 (= T49), Q82 (= Q87), R129 (≠ Q134), Q133 (≠ G138), S135 (≠ A140), G136 (≠ A141), G137 (≠ D142), Q159 (≠ E165), H192 (= H198)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q87)
8hplC Lpqy-sugabc in state 1 (see paper)
40% identity, 74% coverage: 23:286/358 of query aligns to 16:284/384 of 8hplC
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 73% coverage: 27:286/358 of query aligns to 21:289/374 of 2awnB
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)
36% identity, 73% coverage: 27:286/358 of query aligns to 21:289/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), Q81 (= Q87), R128 (≠ Q134), A132 (≠ G138), S134 (≠ A140), G136 (≠ D142), Q137 (≠ A143), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 73% coverage: 27:286/358 of query aligns to 21:289/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (≠ Q134), S134 (≠ A140), Q137 (≠ A143)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (≠ A140), G136 (≠ D142), H191 (= H198)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 73% coverage: 27:286/358 of query aligns to 21:289/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (≠ Q134), A132 (≠ G138), S134 (≠ A140), Q137 (≠ A143)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (≠ A140), G135 (≠ A141), G136 (≠ D142), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 73% coverage: 27:286/358 of query aligns to 21:289/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (≠ Q134), A132 (≠ G138), S134 (≠ A140), Q137 (≠ A143)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
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)
36% identity, 73% coverage: 27:286/358 of query aligns to 22:290/371 of P68187
- A85 (≠ V90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (≠ D142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D164) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ T234) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F247) 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 (= G275) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ Q278) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G280) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
36% identity, 73% coverage: 27:286/358 of query aligns to 19:287/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (≠ T48), T41 (= T49), R126 (≠ Q134), A130 (≠ G138), S132 (≠ A140), G134 (≠ D142), Q135 (≠ A143)
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)
37% identity, 73% coverage: 27:286/358 of query aligns to 22:288/369 of P19566
- L86 (≠ I91) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P166) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D171) 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.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 73% coverage: 27:286/358 of query aligns to 14:259/344 of 2awnC
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 75% coverage: 23:290/358 of query aligns to 20:285/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 75% coverage: 23:290/358 of query aligns to 20:285/353 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)
35% identity, 75% coverage: 23:290/358 of query aligns to 20:285/353 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)
35% identity, 75% coverage: 23:290/358 of query aligns to 20:285/353 of Q97UY8
- S142 (≠ A140) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (≠ D142) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E165) 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+).
Query Sequence
>Ac3H11_792 FitnessBrowser__acidovorax_3H11:Ac3H11_792
MARISLDLAHSYKPNPQQDSDYALLPLKMEFEDGGAYALLGPSGCGKTTMLNIMSGLLVP
SHGKVLFDGRDVTRASPQERNIAQVFQFPVIYDTMTVAENLAFPLRNRKVPEGQIKQRVG
VIAEMLEMSGQLNQRAAGLAADAKQKISLGRGLVRADVAAVLFDEPLTVIDPHLKWQLRR
KLKQIHHELKLTLIYVTHDQVEALTFADQVVVMTRGKAVQVGSADALFERPAHTFVGHFI
GSPGMNFLPAHRDGENLSVAGHRLASPVGRALPAGALQVGIRPEYLALAQPQQAGALPGT
VVQVQDIGTYQMLTAKVGEHTVKARFTPETRLPSSGDTAWLQVLGEHTCYYKNEELLA
Or try a new SitesBLAST search
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