SitesBLAST
Comparing PfGW456L13_1619 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1619 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
54% identity, 94% coverage: 15:543/560 of query aligns to 7:526/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G309), G293 (= G310), A295 (= A312), G314 (≠ A331), Y315 (= Y332), G316 (= G333), M317 (= M334), S318 (= S335), D408 (= D425), K429 (= K446)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H240), W227 (= W244), G292 (= G309), G316 (= G333), P322 (= P339)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R101), P220 (= P237), H223 (= H240), I269 (= I286), G432 (= G449)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
54% identity, 94% coverage: 15:543/560 of query aligns to 5:524/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G310), A293 (= A312), G312 (≠ A331), Y313 (= Y332), G314 (= G333), M315 (= M334), S316 (= S335), D406 (= D425), R421 (= R440)
- binding magnesium ion: M315 (= M334), S316 (= S335), E317 (= E336)
8i51A Acyl-acp synthetase structure bound to amp-mc7
54% identity, 94% coverage: 15:543/560 of query aligns to 5:524/528 of 8i51A
- binding adenosine monophosphate: G291 (= G310), A293 (= A312), Y313 (= Y332), M315 (= M334), S316 (= S335), D406 (= D425), R421 (= R440)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W244), G290 (= G309), G312 (≠ A331), G314 (= G333), M315 (= M334), P320 (= P339), I321 (≠ L340)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
54% identity, 94% coverage: 15:543/560 of query aligns to 7:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G309), G293 (= G310), A294 (≠ S311), A295 (= A312), G314 (≠ A331), Y315 (= Y332), M317 (= M334), S318 (= S335), D408 (= D425), R423 (= R440)
- binding 4'-phosphopantetheine: R93 (= R101), P220 (= P237), H223 (= H240)
8i49A Acyl-acp synthetase structure bound to atp
54% identity, 94% coverage: 15:543/560 of query aligns to 7:526/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
54% identity, 94% coverage: 15:543/560 of query aligns to 7:526/530 of 8i22A
8i3iA Acyl-acp synthetase structure bound to amp-pnp
53% identity, 94% coverage: 15:543/560 of query aligns to 7:518/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T189), G174 (= G191), T175 (= T192), T176 (= T193), K180 (= K197), G293 (= G310), A294 (≠ S311), A295 (= A312), Y315 (= Y332), M317 (= M334), S318 (= S335), D408 (= D425), R423 (= R440)
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)
41% identity, 89% coverage: 43:543/560 of query aligns to 47:531/541 of Q5SKN9
- T184 (= T189) binding
- G302 (= G310) binding
- Q322 (≠ A330) binding
- G323 (≠ A331) binding
- T327 (≠ S335) binding
- E328 (= E336) binding
- D418 (= D425) binding
- K435 (= K442) binding
- K439 (= K446) binding
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, 95% coverage: 17:548/560 of query aligns to 9:535/539 of P0DX84
- H231 (= H240) mutation to A: Retains 74% of wild-type activity.
- W235 (= W244) mutation to A: Almost completely abolishes the activity.
- G302 (= G309) mutation to P: Almost completely abolishes the activity.
- G303 (= G310) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y332) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P339) mutation to A: Retains 69% of wild-type activity.
- R432 (= R440) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K442) mutation to A: Retains 36% of wild-type activity.
- D435 (= D443) mutation to A: Retains 76% of wild-type activity.
- K438 (= K446) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G448) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G449) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E450) mutation to A: Retains 27% of wild-type activity.
- W443 (= W451) mutation to A: Retains 60% of wild-type activity.
- E474 (= E482) mutation to A: Retains 33% of wild-type activity.
- K523 (= K536) 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 (= K539) mutation to A: Retains 48% of wild-type activity.
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
39% identity, 88% coverage: 43:532/560 of query aligns to 40:496/510 of 1v26B
- active site: T177 (= T189), H197 (= H209), H223 (= H240), T320 (≠ S335), E321 (= E336), K432 (= K446), W437 (= W451)
- binding adenosine monophosphate: G295 (= G310), S296 (= S311), A297 (= A312), G316 (≠ A331), Y317 (= Y332), G318 (= G333), L319 (≠ M334), T320 (≠ S335), D411 (= D425), K428 (= K442), K432 (= K446), W437 (= W451)
- binding magnesium ion: T177 (= T189), E321 (= E336)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
37% identity, 95% coverage: 17:548/560 of query aligns to 9:535/538 of 6ijbB
- active site: T185 (= T189), H205 (= H209), H231 (= H240), S329 (= S335), E330 (= E336), K438 (= K446), W443 (= W451), A523 (≠ K536)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W244), G303 (= G310), A325 (= A331), W326 (≠ Y332), G327 (= G333), M328 (= M334)
- binding adenosine monophosphate: G303 (= G310), A304 (≠ S311), A305 (= A312), H324 (≠ A330), W326 (≠ Y332), G327 (= G333), M328 (= M334), S329 (= S335), Q359 (≠ A365), D417 (= D425)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
37% identity, 95% coverage: 17:548/560 of query aligns to 9:532/533 of 6ihkB
- active site: T185 (= T189), H202 (= H209), H228 (= H240), S326 (= S335), E327 (= E336), K435 (= K446), W440 (= W451), K520 (= K536)
- binding adenosine-5'-diphosphate: H228 (= H240), G300 (= G310), A301 (≠ S311), A302 (= A312), H321 (≠ A330), A322 (= A331), W323 (≠ Y332), G324 (= G333), M325 (= M334), S326 (= S335), Q356 (≠ A365), D414 (= D425), R429 (= R440), K520 (= K536)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 80% coverage: 43:488/560 of query aligns to 40:464/491 of 1v25A
- active site: T177 (= T189), H197 (= H209), H223 (= H240), T320 (≠ S335), E321 (= E336), K432 (= K446), W437 (= W451)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H240), V224 (= V241), G295 (= G310), S296 (= S311), A297 (= A312), Y317 (= Y332), G318 (= G333), L319 (≠ M334), T320 (≠ S335), D411 (= D425), I423 (= I437), K432 (= K446), W437 (= W451)
- binding magnesium ion: T177 (= T189), E321 (= E336)
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
27% identity, 89% coverage: 43:543/560 of query aligns to 64:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
26% identity, 90% coverage: 42:543/560 of query aligns to 28:494/503 of P9WQ37
- K172 (= K197) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R224) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ T228) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V241) 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 (= A243) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L246) 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 (≠ K276) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G333) 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 (= W420) 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 (= D425) 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 (= R440) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T447) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G449) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K536) 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.
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)
26% identity, 89% coverage: 44:543/560 of query aligns to 64:547/556 of Q9S725
- K211 (= K197) mutation to S: Drastically reduces the activity.
- M293 (≠ H281) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I308) mutation K->L,A: Affects the substrate specificity.
- E401 (= E393) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V395) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R440) mutation to Q: Drastically reduces the activity.
- K457 (≠ G448) mutation to S: Drastically reduces the activity.
- K540 (= K536) mutation to N: Abolishes the activity.
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)
28% identity, 94% coverage: 30:555/560 of query aligns to 39:554/559 of Q67W82
- G395 (= G392) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
25% identity, 90% coverage: 42:543/560 of query aligns to 31:494/502 of 3r44A
Sites not aligning to the query:
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)
25% identity, 94% coverage: 15:543/560 of query aligns to 21:550/561 of P69451
- Y213 (= Y188) mutation to A: Loss of activity.
- T214 (= T189) mutation to A: 10% of wild-type activity.
- G216 (= G191) mutation to A: Decreases activity.
- T217 (= T192) mutation to A: Decreases activity.
- G219 (= G194) mutation to A: Decreases activity.
- K222 (= K197) mutation to A: Decreases activity.
- E361 (= E336) mutation to A: Loss of activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
26% identity, 89% coverage: 45:543/560 of query aligns to 50:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H242), F245 (≠ W244), T249 (≠ A250), G314 (= G310), A315 (≠ S311), P316 (≠ A312), G337 (≠ A331), Y338 (= Y332), G339 (= G333), L340 (≠ M334), T341 (≠ S335), A346 (≠ L340), D420 (= D425), I432 (= I437), K527 (= K536)
Query Sequence
>PfGW456L13_1619 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1619
MLKTRVIPPAEGAYQYPLLIKRLLMSGARYEKTREIIYRDKLRYSYPTLIERVARLANVL
TAAGVKPGDAVGVMDWDSHRYLECMFAIPMIGAVIHTINVRLSPEQILYTMNHAEDRFVL
VNSEFVGLYKAIEGQLTTVDKTLLLTDLPEKTADLPNLVGEYEQLLAAASPQYDFEDFDE
NSVATTFYTTGTTGNPKGVYFTHRQLVLHTMGVSTIMGAIDSVRLLGTNDVYMPITPMFH
VHAWGLPYVATMLGLKQVYPGRYDPEYLVELWRKEKVTFSHCVPTILQMVLNAKAAQTVD
FGGWKIVIGGSALNRTLYEAAKAKGIQLTAAYGMSETGPLVSCAHLNDELMAGTEDERTT
YRIKAGVPGPLVEAAIVDSEGNFLPADGETQGELVLRAPWLTEGYFNEPQKGAELWAGGW
LHTGDVATLDSMGVIDIRDRIKDVIKTGGEWISSLDLEDLISRHAAVREVAVVGIPDPQW
GERPFALLVLREGHAIGARELKEHLKPFVELGHLSKWAIPSQIALVTEIPKTSVGKLDKK
RIRVDISEWQATNSTFLSTL
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