SitesBLAST
Comparing WP_011383734.1 AMB_RS06730 nitrate 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
44% identity, 41% coverage: 35:220/452 of query aligns to 46:237/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
44% identity, 41% coverage: 35:220/452 of query aligns to 46:237/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
7ahdC Opua (e190q) occluded (see paper)
44% identity, 41% coverage: 35:220/452 of query aligns to 46:237/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S50), G62 (= G51), G64 (= G53), K65 (= K54), S66 (= S55), T67 (= T56), Q111 (= Q91), K161 (= K141), Q162 (≠ E142), S164 (= S144), G166 (= G146), M167 (= M147), Q188 (≠ E168), H221 (= H204)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 49% coverage: 5:226/452 of query aligns to 12:226/378 of P69874
- C26 (≠ T19) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F20) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I43) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S52) mutation to T: Loss of ATPase activity and transport.
- L60 (= L58) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ Y74) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ I130) mutation to M: Loss of ATPase activity and transport.
- D172 (= D167) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
37% identity, 43% coverage: 29:221/452 of query aligns to 20:218/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 44% coverage: 27:226/452 of query aligns to 14:211/374 of 2awnB
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)
40% identity, 44% coverage: 27:226/452 of query aligns to 15:212/371 of P68187
- A85 (= A94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D128) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G133) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G146) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D167) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
40% identity, 44% coverage: 27:226/452 of query aligns to 14:211/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S50), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), Q81 (= Q91), R128 (≠ A138), A132 (≠ E142), S134 (= S144), G136 (= G146), Q137 (≠ M147), E158 (= E168), H191 (= H204)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 44% coverage: 27:226/452 of query aligns to 14:211/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ A138), S134 (= S144), Q137 (≠ M147)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q91), S134 (= S144), G136 (= G146), H191 (= H204)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 44% coverage: 27:226/452 of query aligns to 14:211/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V30), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ A138), A132 (≠ E142), S134 (= S144), Q137 (≠ M147)
- binding tetrafluoroaluminate ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q91), S134 (= S144), G135 (= G145), G136 (= G146), E158 (= E168), H191 (= H204)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 44% coverage: 27:226/452 of query aligns to 14:211/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V30), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ A138), A132 (≠ E142), S134 (= S144), Q137 (≠ M147)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 44% coverage: 27:226/452 of query aligns to 12:209/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S50), G36 (= G51), C37 (≠ S52), G38 (= G53), K39 (= K54), S40 (= S55), T41 (= T56), R126 (≠ A138), A130 (≠ E142), S132 (= S144), G134 (= G146), Q135 (≠ M147)
Sites not aligning to the query:
1g291 Malk (see paper)
37% identity, 43% coverage: 27:220/452 of query aligns to 15:214/372 of 1g291
- binding magnesium ion: D69 (≠ G81), E71 (≠ A83), K72 (= K84), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S50), G39 (= G51), C40 (≠ S52), G41 (= G53), K42 (= K54), T43 (≠ S55), T44 (= T56)
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, 48% coverage: 9:226/452 of query aligns to 2:212/369 of P19566
- L86 (= L95) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P169) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D174) 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)
39% identity, 44% coverage: 29:226/452 of query aligns to 9:181/344 of 2awnC
Q9AT00 Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic; ABC transporter I family member 13; ABC transporter ABCI.13; AtABCI13; Non-intrinsic ABC protein 11; AtNAP11 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
39% identity, 47% coverage: 7:217/452 of query aligns to 81:307/345 of Q9AT00
- F94 (= F20) mutation to A: Reduced ATPase activity and transport properties.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 46% coverage: 13:219/452 of query aligns to 6:214/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 46% coverage: 13:219/452 of query aligns to 6:214/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 46% coverage: 13:219/452 of query aligns to 6:214/353 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)
36% identity, 46% coverage: 13:219/452 of query aligns to 6:214/353 of Q97UY8
- S142 (= S144) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G146) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E168) 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
>WP_011383734.1 AMB_RS06730 nitrate ABC transporter ATP-binding protein
MADITTSTALLDLRGVRKTFLTPDRRERTVLEGVDFKLEEGEIVALLGKSGSGKSTLLRI
MAGLIKANGGEVKYRGHLMTGPAKGISMVFQSFALFPWLTVEENVELGLEAAGVAKAERE
ERANEAIDLIGLGGYESAYPKELSGGMRQRVGFARALVMRPDVLLLDEPFSALDVLTSET
LREDLLELWDERKIPTKGILLVSHNIEEAVSMADRVLVFSSDPGRVRAEIRVNLPRPRDT
ESAAFRQIVDEVYTLMTANVRGGGLGAAEQLTLGYRLPDTTPGKMAGLLETVAEAPFNGR
ADLPQLAEETELEDDQLFHLFEGLRVLGLARIAAGDIFVTPAGQAFVEADDAVRKDLFAE
ALVKHIPLAAHIRRVLDERKDHRAPEDRFLQELQDYLTDDEAERVLETTITWGRYAEIFD
YDYNAGVLMLPEEVVEEMEAEEEARDESGLRE
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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