SitesBLAST
Comparing PfGW456L13_4890 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4890 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)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
53% identity, 97% coverage: 16:543/547 of query aligns to 8:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G308), G293 (= G309), A295 (= A311), G314 (= G330), Y315 (= Y331), G316 (= G332), M317 (= M333), S318 (= S334), D408 (= D424), K429 (= K445)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H239), W227 (= W243), G292 (= G308), G316 (= G332), P322 (= P338)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R101), P220 (= P236), H223 (= H239), I269 (= I285), G432 (= G448)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
53% identity, 97% coverage: 16:543/547 of query aligns to 8:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G308), G293 (= G309), A294 (≠ S310), A295 (= A311), G314 (= G330), Y315 (= Y331), M317 (= M333), S318 (= S334), D408 (= D424), R423 (= R439)
- binding 4'-phosphopantetheine: R93 (= R101), P220 (= P236), H223 (= H239)
8i49A Acyl-acp synthetase structure bound to atp
53% identity, 97% coverage: 16:543/547 of query aligns to 8:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
53% identity, 97% coverage: 16:543/547 of query aligns to 8:527/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
53% identity, 97% coverage: 16:543/547 of query aligns to 6:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G309), A293 (= A311), G312 (= G330), Y313 (= Y331), G314 (= G332), M315 (= M333), S316 (= S334), D406 (= D424), R421 (= R439)
- binding magnesium ion: M315 (= M333), S316 (= S334), E317 (= E335)
8i51A Acyl-acp synthetase structure bound to amp-mc7
53% identity, 97% coverage: 16:543/547 of query aligns to 6:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G309), A293 (= A311), Y313 (= Y331), M315 (= M333), S316 (= S334), D406 (= D424), R421 (= R439)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W243), G290 (= G308), G312 (= G330), G314 (= G332), M315 (= M333), P320 (= P338), I321 (≠ L339)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
53% identity, 97% coverage: 16:543/547 of query aligns to 8:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T188), G174 (= G190), T175 (= T191), T176 (= T192), K180 (= K196), G293 (= G309), A294 (≠ S310), A295 (= A311), Y315 (= Y331), M317 (= M333), S318 (= S334), D408 (= D424), R423 (= R439)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
42% identity, 92% coverage: 43:547/547 of query aligns to 47:536/541 of Q5SKN9
- T184 (= T188) binding
- G302 (= G309) binding
- Q322 (≠ A329) binding
- G323 (= G330) binding
- T327 (≠ S334) binding
- E328 (= E335) binding
- D418 (= D424) binding
- K435 (= K441) binding
- K439 (= K445) binding
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 89% coverage: 43:531/547 of query aligns to 40:496/510 of 1v26B
- active site: T177 (= T188), H197 (= H208), H223 (= H239), T320 (≠ S334), E321 (= E335), K432 (= K445), W437 (= W450)
- binding adenosine monophosphate: G295 (= G309), S296 (= S310), A297 (= A311), G316 (= G330), Y317 (= Y331), G318 (= G332), L319 (≠ M333), T320 (≠ S334), D411 (= D424), K428 (= K441), K432 (= K445), W437 (= W450)
- binding magnesium ion: T177 (= T188), E321 (= E335)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
42% identity, 84% coverage: 43:503/547 of query aligns to 40:484/491 of 1v25A
- active site: T177 (= T188), H197 (= H208), H223 (= H239), T320 (≠ S334), E321 (= E335), K432 (= K445), W437 (= W450)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H239), V224 (= V240), G295 (= G309), S296 (= S310), A297 (= A311), Y317 (= Y331), G318 (= G332), L319 (≠ M333), T320 (≠ S334), D411 (= D424), I423 (= I436), K432 (= K445), W437 (= W450)
- binding magnesium ion: T177 (= T188), E321 (= E335)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
37% identity, 96% coverage: 17:543/547 of query aligns to 9:531/539 of P0DX84
- H231 (= H239) mutation to A: Retains 74% of wild-type activity.
- W235 (= W243) mutation to A: Almost completely abolishes the activity.
- G302 (= G308) mutation to P: Almost completely abolishes the activity.
- G303 (= G309) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y331) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P338) mutation to A: Retains 69% of wild-type activity.
- R432 (= R439) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K441) mutation to A: Retains 36% of wild-type activity.
- D435 (= D442) mutation to A: Retains 76% of wild-type activity.
- K438 (= K445) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G447) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G448) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E449) mutation to A: Retains 27% of wild-type activity.
- W443 (= W450) mutation to A: Retains 60% of wild-type activity.
- E474 (= E481) mutation to A: Retains 33% of wild-type activity.
- K523 (= K535) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K538) mutation to A: Retains 48% of wild-type activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
37% identity, 96% coverage: 17:543/547 of query aligns to 9:531/538 of 6ijbB
- active site: T185 (= T188), H205 (= H208), H231 (= H239), S329 (= S334), E330 (= E335), K438 (= K445), W443 (= W450), A523 (≠ K535)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W243), G303 (= G309), A325 (= A329), W326 (≠ Y331), G327 (= G332), M328 (= M333)
- binding adenosine monophosphate: G303 (= G309), A304 (≠ S310), A305 (= A311), H324 (= H328), W326 (≠ Y331), G327 (= G332), M328 (= M333), S329 (= S334), Q359 (≠ T364), D417 (= D424)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
37% identity, 96% coverage: 17:543/547 of query aligns to 9:528/533 of 6ihkB
- active site: T185 (= T188), H202 (= H208), H228 (= H239), S326 (= S334), E327 (= E335), K435 (= K445), W440 (= W450), K520 (= K535)
- binding adenosine-5'-diphosphate: H228 (= H239), G300 (= G309), A301 (≠ S310), A302 (= A311), H321 (= H328), A322 (= A329), W323 (≠ Y331), G324 (= G332), M325 (= M333), S326 (= S334), Q356 (≠ T364), D414 (= D424), R429 (= R439), K520 (= K535)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
30% identity, 92% coverage: 42:543/547 of query aligns to 28:495/503 of P9WQ37
- K172 (= K196) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ Y219) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G221) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V240) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (= A242) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V245) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ K275) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G332) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W419) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D424) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R439) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T446) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G448) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K535) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 92% coverage: 42:543/547 of query aligns to 31:495/502 of 3r44A
Sites not aligning to the query:
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
29% identity, 92% coverage: 44:547/547 of query aligns to 64:552/556 of Q9S725
- K211 (= K196) mutation to S: Drastically reduces the activity.
- M293 (≠ H280) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L307) mutation K->L,A: Affects the substrate specificity.
- E401 (= E392) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V394) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R439) mutation to Q: Drastically reduces the activity.
- K457 (≠ G447) mutation to S: Drastically reduces the activity.
- K540 (= K535) mutation to N: Abolishes the activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
26% identity, 91% coverage: 45:543/547 of query aligns to 50:535/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H239), F245 (≠ H241), T249 (≠ V245), G314 (≠ S310), A315 (= A311), P316 (≠ L312), G337 (= G330), Y338 (= Y331), G339 (= G332), L340 (≠ M333), T341 (≠ S334), S345 (≠ P338), A346 (≠ L339), D420 (= D424), I432 (= I436), K527 (= K535)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ H241), R335 (≠ H328), G337 (= G330), G339 (= G332), L340 (≠ M333), A346 (≠ L339)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
26% identity, 91% coverage: 45:543/547 of query aligns to 50:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H239), F245 (≠ H241), T249 (≠ V245), G314 (≠ S310), A315 (= A311), P316 (≠ L312), G337 (= G330), Y338 (= Y331), G339 (= G332), L340 (≠ M333), T341 (≠ S334), A346 (≠ L339), D420 (= D424), I432 (= I436), K527 (= K535)
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
29% identity, 91% coverage: 44:542/547 of query aligns to 60:542/559 of Q67W82
- G395 (= G391) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
28% identity, 91% coverage: 45:543/547 of query aligns to 50:551/561 of P69451
- Y213 (= Y187) mutation to A: Loss of activity.
- T214 (= T188) mutation to A: 10% of wild-type activity.
- G216 (= G190) mutation to A: Decreases activity.
- T217 (= T191) mutation to A: Decreases activity.
- G219 (= G193) mutation to A: Decreases activity.
- K222 (= K196) mutation to A: Decreases activity.
- E361 (= E335) mutation to A: Loss of activity.
Query Sequence
>PfGW456L13_4890 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4890
MMATKIIPPADGAYAYPLLIKQLLLSGVRYEPGREIVYADKLRYSYQTLNKRIRRLANAL
TAAGVKAGDTVALLDWDSHRYLECFFAVPMIGAVLHTVNIRLSPEQVLFTMNHAEDDLVL
VHDDFLPLVEQIHGRLETVKGYLQLTDDEATTTSLPVLGEYEHLLSLASDQYDFPDFDEN
SVATLFYTTGTTGDPKGVYFSHRQLVLHTLNAVGTLGVYQGQPLLRSDDVYMPITPMFHV
HAWGVPYVATLMGIKQVYPGRYEPNSLVKLYREEKVTFSHCVPTILQMILNCEEGKATRF
DGWKMLLGGSALTLGVASEANAKGMVVHAGYGMSETCPLLCLTYLRDEDLQLSAEAQLPI
RIKTGTPVPLVDLKIIDADGNDVPHDGESLGEIVVRAPWLTQGYLKAPDKGAELWHNGWL
HTGDMASIDKLGGVEIKDRIKDVIKTGGEWISSLELESLISEHPGVMSVAVVGIADEQWG
ERPMAMVVCEPGQYLDRKILETHLQAFVDGGRINKWAIPKQFKFVAEIPKTSVGKINKKL
IRETEAN
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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