SitesBLAST
Comparing AZOBR_RS25875 FitnessBrowser__azobra:AZOBR_RS25875 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)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
35% identity, 95% coverage: 5:354/367 of query aligns to 9:347/353 of 1vciA
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
31% identity, 95% coverage: 5:354/367 of query aligns to 9:369/375 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)
32% identity, 96% coverage: 3:354/367 of query aligns to 4:382/393 of P9WQI3
- H193 (≠ T191) 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)
40% identity, 65% coverage: 2:241/367 of query aligns to 3:248/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ R72), D80 (≠ E73)
- binding pyrophosphate 2-: S38 (≠ T37), G39 (≠ L38), C40 (≠ S39), G41 (= G40), K42 (= K41), T43 (= T42), T44 (≠ S43)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
32% identity, 95% coverage: 3:351/367 of query aligns to 3:352/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ H11), S38 (≠ T37), G39 (≠ L38), G41 (= G40), K42 (= K41), S43 (≠ T42), Q82 (= Q81), Q133 (= Q132), G136 (= G135), G137 (= G136), Q138 (= Q137), H192 (≠ T191)
- binding magnesium ion: S43 (≠ T42), Q82 (= Q81)
8hplC Lpqy-sugabc in state 1 (see paper)
31% identity, 95% coverage: 3:351/367 of query aligns to 3:373/384 of 8hplC
8hprD Lpqy-sugabc in state 4 (see paper)
32% identity, 95% coverage: 3:351/367 of query aligns to 3:351/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ H11), S38 (≠ T37), C40 (≠ S39), G41 (= G40), K42 (= K41), S43 (≠ T42), T44 (≠ S43), Q82 (= Q81), R129 (= R128), Q133 (= Q132), S135 (= S134), G136 (= G135), G137 (= G136), Q159 (≠ E158), H192 (≠ T191)
- binding magnesium ion: S43 (≠ T42), Q82 (= Q81)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 57% coverage: 21:230/367 of query aligns to 36:245/378 of P69874
- F45 (≠ L30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S39) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ M45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L120) mutation to M: Loss of ATPase activity and transport.
- D172 (= D157) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
33% identity, 96% coverage: 5:355/367 of query aligns to 6:359/371 of P68187
- A85 (≠ I84) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P105) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R118) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E123) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G136) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D157) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L227) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ T240) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ E266) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (vs. gap) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T273) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G275) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G295) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E301) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ R315) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G336) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ F342) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F351) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
33% identity, 96% coverage: 5:355/367 of query aligns to 3:356/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ V12), S35 (≠ T37), G36 (≠ L38), C37 (≠ S39), G38 (= G40), K39 (= K41), S40 (≠ T42), T41 (≠ S43), R126 (= R128), A130 (≠ Q132), S132 (= S134), G134 (= G136), Q135 (= Q137)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
33% identity, 96% coverage: 5:355/367 of query aligns to 5:358/374 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)
33% identity, 96% coverage: 5:355/367 of query aligns to 5:358/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ V12), S37 (≠ T37), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), Q81 (= Q81), R128 (= R128), A132 (≠ Q132), S134 (= S134), G136 (= G136), Q137 (= Q137), E158 (= E158), H191 (≠ T191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
33% identity, 96% coverage: 5:355/367 of query aligns to 5:358/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ V12), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (= R128), S134 (= S134), Q137 (= Q137)
- binding beryllium trifluoride ion: S37 (≠ T37), G38 (≠ L38), K41 (= K41), Q81 (= Q81), S134 (= S134), G136 (= G136), H191 (≠ T191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
33% identity, 96% coverage: 5:355/367 of query aligns to 5:358/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ V12), V17 (≠ H17), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (= R128), A132 (≠ Q132), S134 (= S134), Q137 (= Q137)
- binding tetrafluoroaluminate ion: S37 (≠ T37), G38 (≠ L38), K41 (= K41), Q81 (= Q81), S134 (= S134), G135 (= G135), G136 (= G136), E158 (= E158), H191 (≠ T191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
33% identity, 96% coverage: 5:355/367 of query aligns to 5:358/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ V12), V17 (≠ H17), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (= R128), A132 (≠ Q132), S134 (= S134), Q137 (= Q137)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
33% identity, 96% coverage: 5:355/367 of query aligns to 6:357/369 of P19566
- L86 (≠ N85) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P159) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D164) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E301) 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)
38% identity, 61% coverage: 13:235/367 of query aligns to 16:243/353 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)
38% identity, 61% coverage: 13:235/367 of query aligns to 16:243/353 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)
38% identity, 61% coverage: 13:235/367 of query aligns to 16:243/353 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)
38% identity, 61% coverage: 13:235/367 of query aligns to 16:243/353 of Q97UY8
- S142 (= S134) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G136) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E158) 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
>AZOBR_RS25875 FitnessBrowser__azobra:AZOBR_RS25875
VGLVLDKVSRHVGGHVHLENVSLSLERGSLNVLLGPTLSGKTSLMRLMAGLDVPSAGRVL
VDGADVTGRHVRERSVAMVYQQFINYPSLTVYENIASPLRVARRPKDEIDRKVREAARLL
KLEAYLQRTPQQLSGGQQQRTAIARALVKEAQLVLLDEPLANLDYKLREELREELPKIFA
ATGAVFVYATTEPAEALLLRGNTATLWEGRLAQFGRTPDVYRRPANLTSARVFSDPPLNT
MRVHKRGLQIVLATGEHGPARGVLAELPDDDYTIGFRADHLHLTRPHADAIALSGAVAVS
EITGSESFVHIDLPRTDGGADRWVAVTRGVLEVEPGERIECFIDPRRLFVFGHDGRLAAA
PPLVMAA
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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