SitesBLAST
Comparing Pf6N2E2_1726 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1726 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)
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)
37% identity, 98% coverage: 10:539/540 of query aligns to 10:536/541 of Q5SKN9
- T184 (= T189) binding
- G302 (= G304) binding
- Q322 (≠ H324) binding
- G323 (≠ V325) binding
- T327 (= T329) binding
- E328 (= E330) binding
- D418 (= D421) binding
- K435 (= K438) binding
- K439 (≠ I442) binding
8i3iA Acyl-acp synthetase structure bound to amp-pnp
31% identity, 97% coverage: 13:536/540 of query aligns to 12:520/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T189), G174 (= G191), T175 (= T192), T176 (= T193), K180 (= K197), G293 (= G304), A294 (= A305), A295 (= A306), Y315 (= Y326), M317 (≠ L328), S318 (≠ T329), D408 (= D421), R423 (= R436)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 98% coverage: 10:539/540 of query aligns to 3:505/510 of 1v26B
- active site: T177 (= T189), H197 (≠ N209), H223 (= H233), T320 (= T329), E321 (= E330), K432 (≠ I442), W437 (≠ N447)
- binding adenosine monophosphate: G295 (= G304), S296 (≠ A305), A297 (= A306), G316 (≠ V325), Y317 (= Y326), G318 (= G327), L319 (= L328), T320 (= T329), D411 (= D421), K428 (= K438), K432 (≠ I442), W437 (≠ N447)
- binding magnesium ion: T177 (= T189), E321 (= E330)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
31% identity, 97% coverage: 13:536/540 of query aligns to 10:526/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G304), A293 (= A306), G312 (≠ V325), Y313 (= Y326), G314 (= G327), M315 (≠ L328), S316 (≠ T329), D406 (= D421), R421 (= R436)
- binding magnesium ion: M315 (≠ L328), S316 (≠ T329), E317 (= E330)
8i51A Acyl-acp synthetase structure bound to amp-mc7
31% identity, 97% coverage: 13:536/540 of query aligns to 10:526/528 of 8i51A
- binding adenosine monophosphate: G291 (= G304), A293 (= A306), Y313 (= Y326), M315 (≠ L328), S316 (≠ T329), D406 (= D421), R421 (= R436)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W237), G290 (≠ A303), G312 (≠ V325), G314 (= G327), M315 (≠ L328), P320 (≠ G333), I321 (≠ P334)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
37% identity, 88% coverage: 10:484/540 of query aligns to 3:464/491 of 1v25A
- active site: T177 (= T189), H197 (≠ N209), H223 (= H233), T320 (= T329), E321 (= E330), K432 (≠ I442), W437 (≠ N447)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H233), V224 (≠ C234), G295 (= G304), S296 (≠ A305), A297 (= A306), Y317 (= Y326), G318 (= G327), L319 (= L328), T320 (= T329), D411 (= D421), I423 (= I433), K432 (≠ I442), W437 (≠ N447)
- binding magnesium ion: T177 (= T189), E321 (= E330)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
31% identity, 97% coverage: 13:536/540 of query aligns to 12:528/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A303), G293 (= G304), A294 (= A305), A295 (= A306), G314 (≠ V325), Y315 (= Y326), M317 (≠ L328), S318 (≠ T329), D408 (= D421), R423 (= R436)
- binding 4'-phosphopantetheine: R93 (= R101), P220 (= P230), H223 (= H233)
8i49A Acyl-acp synthetase structure bound to atp
31% identity, 97% coverage: 13:536/540 of query aligns to 12:528/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
31% identity, 97% coverage: 13:536/540 of query aligns to 12:528/530 of 8i22A
8i8dA Acyl-acp synthetase structure bound to mc7-acp
31% identity, 97% coverage: 13:536/540 of query aligns to 12:528/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A303), G293 (= G304), A295 (= A306), G314 (≠ V325), Y315 (= Y326), G316 (= G327), M317 (≠ L328), S318 (≠ T329), D408 (= D421), K429 (≠ I442)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H233), W227 (= W237), G292 (≠ A303), G316 (= G327), P322 (≠ G333)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R101), P220 (= P230), H223 (= H233), I269 (≠ V279), G432 (= G445)
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)
33% identity, 93% coverage: 40:539/540 of query aligns to 35:535/539 of P0DX84
- H231 (= H233) mutation to A: Retains 74% of wild-type activity.
- W235 (= W237) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A303) mutation to P: Almost completely abolishes the activity.
- G303 (= G304) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y326) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G333) mutation to A: Retains 69% of wild-type activity.
- R432 (= R436) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K438) mutation to A: Retains 36% of wild-type activity.
- D435 (= D439) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I442) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G444) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G445) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E446) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N447) mutation to A: Retains 60% of wild-type activity.
- E474 (= E478) mutation to A: Retains 33% of wild-type activity.
- K523 (= K527) 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 (= K530) 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)
33% identity, 93% coverage: 40:539/540 of query aligns to 35:535/538 of 6ijbB
- active site: T185 (= T189), H205 (≠ N209), H231 (= H233), S329 (≠ T329), E330 (= E330), K438 (≠ I442), W443 (≠ N447), A523 (≠ K527)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W237), G303 (= G304), A325 (≠ V325), W326 (≠ Y326), G327 (= G327), M328 (≠ L328)
- binding adenosine monophosphate: G303 (= G304), A304 (= A305), A305 (= A306), H324 (= H324), W326 (≠ Y326), G327 (= G327), M328 (≠ L328), S329 (≠ T329), Q359 (= Q359), D417 (= D421)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
33% identity, 93% coverage: 40:539/540 of query aligns to 35:532/533 of 6ihkB
- active site: T185 (= T189), H202 (≠ N209), H228 (= H233), S326 (≠ T329), E327 (= E330), K435 (≠ I442), W440 (≠ N447), K520 (= K527)
- binding adenosine-5'-diphosphate: H228 (= H233), G300 (= G304), A301 (= A305), A302 (= A306), H321 (= H324), A322 (≠ V325), W323 (≠ Y326), G324 (= G327), M325 (≠ L328), S326 (≠ T329), Q356 (= Q359), D414 (= D421), R429 (= R436), K520 (= K527)
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)
32% identity, 95% coverage: 23:535/540 of query aligns to 7:495/503 of P9WQ37
- R9 (≠ E25) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D33) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K197) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G220) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ H222) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C234) 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 (≠ G236) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ P240) 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 (≠ Q269) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G327) 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 (= W416) 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 (= D421) 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 (= R436) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S443) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G445) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K527) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 95% coverage: 23:535/540 of query aligns to 10:495/502 of 3r44A
Sites not aligning to the query:
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
27% identity, 95% coverage: 26:538/540 of query aligns to 10:481/484 of 5gtdA
- active site: T151 (= T189), S171 (≠ N209), H195 (= H233), T288 (= T329), E289 (= E330)
- binding adenosine-5'-monophosphate: G263 (= G304), G264 (≠ A305), Y285 (= Y326), G286 (= G327), M287 (≠ L328), T288 (= T329), D366 (= D421), V378 (≠ I433)
- binding magnesium ion: F314 (≠ P364), S315 (≠ T365)
- binding 2-succinylbenzoate: H195 (= H233), S197 (≠ N235), A237 (≠ G275), L260 (≠ M301), G262 (≠ A303), G263 (= G304), G286 (= G327), M287 (≠ L328), S292 (≠ G333), Q293 (≠ P334)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
27% identity, 95% coverage: 26:538/540 of query aligns to 10:481/485 of 5x8fB
- active site: T151 (= T189), S171 (≠ N209), H195 (= H233), T288 (= T329), E289 (= E330), I387 (= I442), N392 (= N447), K470 (= K527)
- binding magnesium ion: Y23 (≠ H39), E24 (≠ G40), H70 (≠ F86), N178 (≠ T216), L202 (≠ P240), L214 (≠ F252), T296 (≠ L337), L297 (≠ C338), S298 (≠ A339)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R101), L191 (= L229), P192 (= P230), H195 (= H233), I196 (≠ C234), S197 (≠ N235), A237 (≠ G275), V238 (≠ A276), L260 (≠ M301), G262 (≠ A303), G286 (= G327), M287 (≠ L328), S292 (≠ G333), Q293 (≠ P334), S388 (= S443), G389 (= G444), G390 (= G445), E391 (= E446), K420 (= K475), W421 (= W476), K450 (≠ G508), Y451 (≠ F509)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
27% identity, 95% coverage: 26:538/540 of query aligns to 9:478/481 of 5busA
- active site: T150 (= T189), S170 (≠ N209), H194 (= H233), T287 (= T329), E288 (= E330)
- binding adenosine monophosphate: H194 (= H233), G262 (= G304), G263 (≠ A305), S283 (≠ V325), M286 (≠ L328), T287 (= T329), D365 (= D421), V377 (≠ I433), R380 (= R436), K467 (= K527)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
27% identity, 94% coverage: 26:535/540 of query aligns to 9:475/475 of 5burA
- active site: T150 (= T189), S170 (≠ N209), H194 (= H233), T287 (= T329), E288 (= E330)
- binding adenosine-5'-triphosphate: T150 (= T189), S151 (= S190), T153 (= T192), T154 (= T193), K158 (= K197), G263 (≠ A305), S283 (≠ V325), T287 (= T329), D365 (= D421), V377 (≠ I433), R380 (= R436)
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, 96% coverage: 14:534/540 of query aligns to 34:547/556 of Q9S725
- K211 (= K197) mutation to S: Drastically reduces the activity.
- M293 (≠ C274) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V302) mutation K->L,A: Affects the substrate specificity.
- E401 (= E389) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ F391) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R436) mutation to Q: Drastically reduces the activity.
- K457 (≠ G444) mutation to S: Drastically reduces the activity.
- K540 (= K527) mutation to N: Abolishes the activity.
Query Sequence
>Pf6N2E2_1726 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1726
MSIYEQGFAPTGVNHTALTPLSFIERTASVYPDYPAVIHGSIRRTWADTYRRCRRLASAL
AGRGIGKNDTVAVMLPNIPAMLEAHFGVPMIGAVLNALNVRLDAEAIAFMLAHGEAKVLI
ADREFHDVVQAAIGMLDHPPLVIDLDDPEYGEGQAVSELDYEAFLAEGDPDFAWQWPDDE
WQAISLNYTSGTTGNPKGVVYHHRGAYLNSLGNQMTWAMGNHPVYLWTLPMFHCNGWCYP
WTVTALAGVHVFLRRVDPQKILNLIREHQITHLCGAPIVLNALVNMPDSAKAAIDHPVSA
MVAGAAPPAKVIGAVEEMGIKVTHVYGLTEVYGPVTLCAWHAAWDELPLEQRAQIKARQG
VRYPTLEGLMVADPRTLEPTPHDGQTIGEIFMRGNTVMKGYLKNPSATAEAFEGGWFHTG
DLAVTHADGYVEIRDRLKDIIISGGENISTIELEGVLYRHPAVLEAAVVARPDEKWGETP
CAFITLKSDHTDVREAEIISFCREHLAGFKVPRTVVFTQLPKTSTGKIQKFVLRDMAKNL
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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