SitesBLAST
Comparing Pf6N2E2_1433 Branched-chain amino acid transport ATP-binding protein LivG (TC 3.A.1.4.1) 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)
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
31% identity, 96% coverage: 9:257/260 of query aligns to 4:253/254 of 1g6hA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
31% identity, 96% coverage: 9:257/260 of query aligns to 4:253/253 of 1g9xB
6mjpA Lptb(e163q)fgc from vibrio cholerae (see paper)
31% identity, 97% coverage: 9:259/260 of query aligns to 2:237/240 of 6mjpA
6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter (see paper)
30% identity, 95% coverage: 10:257/260 of query aligns to 3:235/235 of 6mhzA
- binding adp orthovanadate: Y12 (≠ F19), N37 (= N44), G38 (= G45), G40 (= G47), K41 (= K48), T42 (≠ S49), T43 (≠ S50), Q84 (= Q91), S136 (≠ T157), S138 (≠ P159), G139 (≠ Y160), G140 (= G161), E162 (= E183), G166 (= G187), H194 (= H216)
6s8nB Cryo-em structure of lptb2fgc in complex with lipopolysaccharide (see paper)
30% identity, 95% coverage: 10:257/260 of query aligns to 3:235/238 of 6s8nB
6s8gA Cryo-em structure of lptb2fgc in complex with amp-pnp (see paper)
30% identity, 95% coverage: 10:257/260 of query aligns to 3:235/238 of 6s8gA
- binding phosphoaminophosphonic acid-adenylate ester: Y12 (≠ F19), R15 (≠ V22), N37 (= N44), G40 (= G47), K41 (= K48), T42 (≠ S49), T43 (≠ S50), Q84 (= Q91), S136 (≠ T157), S138 (≠ P159), E141 (≠ L162)
6mbnA Lptb e163q in complex with atp (see paper)
30% identity, 95% coverage: 10:257/260 of query aligns to 4:236/241 of 6mbnA
6b89A E. Coli lptb in complex with adp and novobiocin (see paper)
30% identity, 95% coverage: 10:256/260 of query aligns to 3:234/234 of 6b89A
- binding adenosine-5'-diphosphate: Y12 (≠ F19), R15 (≠ V22), V17 (≠ A24), N37 (= N44), G38 (= G45), G40 (= G47), K41 (= K48), T42 (≠ S49), T43 (≠ S50)
- binding magnesium ion: T42 (≠ S49), Q84 (= Q91)
- binding novobiocin: L71 (≠ P78), H72 (= H79), P83 (≠ F90), A86 (≠ I93), S87 (≠ A94), F89 (= F96), R90 (≠ K97), R91 (≠ G98), L92 (≠ M99), V101 (≠ G108), Q135 (≠ G156), R149 (= R170)
4p31A Crystal structure of a selenomethionine derivative of e. Coli lptb in complex with adp-magensium (see paper)
30% identity, 95% coverage: 10:256/260 of query aligns to 3:234/234 of 4p31A
6b8bA E. Coli lptb in complex with adp and a novobiocin derivative (see paper)
30% identity, 95% coverage: 10:255/260 of query aligns to 3:233/233 of 6b8bA
- binding adenosine-5'-diphosphate: Y12 (≠ F19), R15 (≠ V22), V17 (≠ A24), G38 (= G45), G40 (= G47), K41 (= K48), T42 (≠ S49), T43 (≠ S50)
- binding (3s,5s,7s)-N-{7-[(3-O-carbamoyl-6-deoxy-5-methyl-4-O-methyl-beta-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-1-benzopyran-3-yl}tricyclo[3.3.1.1~3,7~]decane-1-carboxamide: F89 (= F96), R90 (≠ K97), R91 (≠ G98)
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)
31% identity, 95% coverage: 12:258/260 of query aligns to 6:237/393 of P9WQI3
- H193 (= H216) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 98% coverage: 4:257/260 of query aligns to 12:249/378 of P69874
- C26 (≠ S18) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F19) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I37) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A46) mutation to T: Loss of ATPase activity and transport.
- L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ G125) mutation to M: Loss of ATPase activity and transport.
- D172 (= D182) 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.
8hprD Lpqy-sugabc in state 4 (see paper)
29% identity, 95% coverage: 12:258/260 of query aligns to 5:236/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F19), S38 (≠ N44), C40 (≠ A46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (≠ S50), Q82 (= Q91), R129 (≠ T153), Q133 (≠ T157), S135 (≠ P159), G136 (≠ Y160), G137 (= G161), Q159 (≠ E183), H192 (= H216)
- binding magnesium ion: S43 (= S49), Q82 (= Q91)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
29% identity, 96% coverage: 10:258/260 of query aligns to 3:235/374 of 2awnB
8hprC Lpqy-sugabc in state 4 (see paper)
29% identity, 95% coverage: 12:258/260 of query aligns to 5:236/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F19), S38 (≠ N44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q91), Q133 (≠ T157), G136 (≠ Y160), G137 (= G161), Q138 (≠ L162), H192 (= H216)
- binding magnesium ion: S43 (= S49), Q82 (= Q91)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
29% identity, 96% coverage: 10:258/260 of query aligns to 1:233/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F19), S35 (≠ N44), G36 (= G45), C37 (≠ A46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (≠ S50), R126 (≠ T153), A130 (≠ T157), S132 (≠ P159), G134 (= G161), Q135 (≠ L162)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
29% identity, 96% coverage: 10:258/260 of query aligns to 4:236/371 of P68187
- A85 (= A94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R128) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A138) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V141) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A143) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q148) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G161) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D182) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E250) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
29% identity, 96% coverage: 10:258/260 of query aligns to 3:235/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F19), S37 (≠ N44), G38 (= G45), C39 (≠ A46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (≠ S50), Q81 (= Q91), R128 (≠ T153), A132 (≠ T157), S134 (≠ P159), G136 (= G161), Q137 (≠ L162), E158 (= E183), H191 (= H216)
- binding magnesium ion: S42 (= S49), Q81 (= Q91)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
29% identity, 96% coverage: 10:258/260 of query aligns to 3:235/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F19), G38 (= G45), C39 (≠ A46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (≠ S50), R128 (≠ T153), S134 (≠ P159), Q137 (≠ L162)
- binding beryllium trifluoride ion: S37 (≠ N44), G38 (= G45), K41 (= K48), Q81 (= Q91), S134 (≠ P159), G136 (= G161), H191 (= H216)
- binding magnesium ion: S42 (= S49), Q81 (= Q91)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
29% identity, 96% coverage: 10:258/260 of query aligns to 3:235/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F19), V17 (≠ A24), G38 (= G45), C39 (≠ A46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (≠ S50), R128 (≠ T153), A132 (≠ T157), S134 (≠ P159), Q137 (≠ L162)
- binding tetrafluoroaluminate ion: S37 (≠ N44), G38 (= G45), K41 (= K48), Q81 (= Q91), S134 (≠ P159), G135 (≠ Y160), G136 (= G161), E158 (= E183), H191 (= H216)
- binding magnesium ion: S42 (= S49), Q81 (= Q91)
Query Sequence
>Pf6N2E2_1433 Branched-chain amino acid transport ATP-binding protein LivG (TC 3.A.1.4.1)
MTQTAITHLLELDHISLSFKGVKAVTDISFRVAAGEICALIGPNGAGKSSLLNVISGVYQ
AQDGHIRFDRQERRRMRPHDVAVRGIARTFQNIALFKGMSVLDNVLTGRNLKRRSTWIEQ
ALRIGRARTEDDRQREAAERVIAFLHLQPWRDTLVGTLPYGLQKRVELARALAAEPRLLL
LDEPMAGMNADEKQQMSRFIVDINRELGTTVVLIEHDIGVVMDISDHVVVLDYGRKIGDG
SPEDVRQNPEVISAYLGTRH
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