SitesBLAST
Comparing GFF3780 FitnessBrowser__Phaeo:GFF3780 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)
36% identity, 95% coverage: 23:540/543 of query aligns to 23:536/541 of Q5SKN9
- T184 (= T189) binding
- G302 (= G306) binding
- Q322 (= Q326) binding
- G323 (≠ V327) binding
- T327 (= T331) binding
- E328 (= E332) binding
- D418 (= D423) binding
- K435 (= K440) binding
- K439 (≠ I444) 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)
34% identity, 92% coverage: 43:539/543 of query aligns to 39:534/539 of P0DX84
- H231 (= H233) mutation to A: Retains 74% of wild-type activity.
- W235 (= W237) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A305) mutation to P: Almost completely abolishes the activity.
- G303 (= G306) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y328) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G335) mutation to A: Retains 69% of wild-type activity.
- R432 (= R438) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K440) mutation to A: Retains 36% of wild-type activity.
- D435 (= D441) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I444) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G446) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G447) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E448) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N449) mutation to A: Retains 60% of wild-type activity.
- E474 (= E480) mutation to A: Retains 33% of wild-type activity.
- K523 (= K528) 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 (= K531) 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)
34% identity, 92% coverage: 43:539/543 of query aligns to 39:534/538 of 6ijbB
- active site: T185 (= T189), H205 (vs. gap), H231 (= H233), S329 (≠ T331), E330 (= E332), K438 (≠ I444), W443 (≠ N449), A523 (≠ K528)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W237), G303 (= G306), A325 (≠ V327), W326 (≠ Y328), G327 (= G329), M328 (≠ L330)
- binding adenosine monophosphate: G303 (= G306), A304 (= A307), A305 (≠ P308), H324 (≠ Q326), W326 (≠ Y328), G327 (= G329), M328 (≠ L330), S329 (≠ T331), Q359 (= Q361), D417 (= D423)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 94% coverage: 23:530/543 of query aligns to 16:502/510 of 1v26B
- active site: T177 (= T189), H197 (≠ M209), H223 (= H233), T320 (= T331), E321 (= E332), K432 (≠ I444), W437 (≠ N449)
- binding adenosine monophosphate: G295 (= G306), S296 (≠ A307), A297 (≠ P308), G316 (≠ V327), Y317 (= Y328), G318 (= G329), L319 (= L330), T320 (= T331), D411 (= D423), K428 (= K440), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T189), E321 (= E332)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
34% identity, 92% coverage: 43:539/543 of query aligns to 39:531/533 of 6ihkB
- active site: T185 (= T189), H202 (vs. gap), H228 (= H233), S326 (≠ T331), E327 (= E332), K435 (≠ I444), W440 (≠ N449), K520 (= K528)
- binding adenosine-5'-diphosphate: H228 (= H233), G300 (= G306), A301 (= A307), A302 (≠ P308), H321 (≠ Q326), A322 (≠ V327), W323 (≠ Y328), G324 (= G329), M325 (≠ L330), S326 (≠ T331), Q356 (= Q361), D414 (= D423), R429 (= R438), K520 (= K528)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
36% identity, 85% coverage: 23:486/543 of query aligns to 16:464/491 of 1v25A
- active site: T177 (= T189), H197 (≠ M209), H223 (= H233), T320 (= T331), E321 (= E332), K432 (≠ I444), W437 (≠ N449)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H233), V224 (≠ C234), G295 (= G306), S296 (≠ A307), A297 (≠ P308), Y317 (= Y328), G318 (= G329), L319 (= L330), T320 (= T331), D411 (= D423), I423 (= I435), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T189), E321 (= E332)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
30% identity, 95% coverage: 18:535/543 of query aligns to 17:518/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T189), G174 (= G191), T175 (= T192), T176 (≠ S193), K180 (= K197), G293 (= G306), A294 (= A307), A295 (≠ P308), Y315 (= Y328), M317 (≠ L330), S318 (≠ T331), D408 (= D423), R423 (= R438)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
30% identity, 95% coverage: 18:535/543 of query aligns to 17:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A305), G293 (= G306), A294 (= A307), A295 (≠ P308), G314 (≠ V327), Y315 (= Y328), M317 (≠ L330), S318 (≠ T331), D408 (= D423), R423 (= R438)
- binding 4'-phosphopantetheine: R93 (= R101), P220 (= P230), H223 (= H233)
8i49A Acyl-acp synthetase structure bound to atp
30% identity, 95% coverage: 18:535/543 of query aligns to 17:526/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
30% identity, 95% coverage: 18:535/543 of query aligns to 17:526/530 of 8i22A
8i8dA Acyl-acp synthetase structure bound to mc7-acp
30% identity, 95% coverage: 18:535/543 of query aligns to 17:526/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A305), G293 (= G306), A295 (≠ P308), G314 (≠ V327), Y315 (= Y328), G316 (= G329), M317 (≠ L330), S318 (≠ T331), D408 (= D423), K429 (≠ I444)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H233), W227 (= W237), G292 (≠ A305), G316 (= G329), P322 (≠ G335)
- 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 (= G447)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
30% identity, 95% coverage: 18:535/543 of query aligns to 15:524/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G306), A293 (≠ P308), G312 (≠ V327), Y313 (= Y328), G314 (= G329), M315 (≠ L330), S316 (≠ T331), D406 (= D423), R421 (= R438)
- binding magnesium ion: M315 (≠ L330), S316 (≠ T331), E317 (= E332)
8i51A Acyl-acp synthetase structure bound to amp-mc7
30% identity, 95% coverage: 18:535/543 of query aligns to 15:524/528 of 8i51A
- binding adenosine monophosphate: G291 (= G306), A293 (≠ P308), Y313 (= Y328), M315 (≠ L330), S316 (≠ T331), D406 (= D423), R421 (= R438)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W237), G290 (≠ A305), G312 (≠ V327), G314 (= G329), M315 (≠ L330), P320 (≠ G335), I321 (≠ H336)
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)
31% identity, 91% coverage: 41:536/543 of query aligns to 27:495/503 of P9WQ37
- K172 (= K197) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P220) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Y222) 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 (≠ H239) 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 (≠ G269) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G329) 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 (= W418) 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 (= D423) 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 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K528) 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.
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)
29% identity, 96% coverage: 20:539/543 of query aligns to 5:481/485 of 5x8fB
- active site: T151 (= T189), S171 (≠ M209), H195 (= H233), T288 (= T331), E289 (= E332), I387 (= I444), N392 (= N449), K470 (= K528)
- binding magnesium ion: Y23 (= Y39), E24 (≠ G40), H70 (≠ F86), N178 (≠ A216), L202 (≠ S240), L214 (≠ F252), T296 (≠ K339), L297 (≠ C340), S298 (≠ A352)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R101), L191 (≠ V229), P192 (= P230), H195 (= H233), I196 (≠ C234), S197 (≠ N235), A237 (= A275), V238 (≠ A276), L260 (= L303), G262 (≠ A305), G286 (= G329), M287 (≠ L330), S292 (≠ G335), Q293 (≠ H336), S388 (= S445), G389 (= G446), G390 (= G447), E391 (= E448), K420 (= K477), W421 (= W478), K450 (≠ G509), Y451 (≠ F510)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 96% coverage: 20:539/543 of query aligns to 5:481/484 of 5gtdA
- active site: T151 (= T189), S171 (≠ M209), H195 (= H233), T288 (= T331), E289 (= E332)
- binding adenosine-5'-monophosphate: G263 (= G306), G264 (≠ A307), Y285 (= Y328), G286 (= G329), M287 (≠ L330), T288 (= T331), D366 (= D423), V378 (≠ I435)
- binding magnesium ion: F314 (≠ V368), S315 (≠ D377)
- binding 2-succinylbenzoate: H195 (= H233), S197 (≠ N235), A237 (= A275), L260 (= L303), G262 (≠ A305), G263 (= G306), G286 (= G329), M287 (≠ L330), S292 (≠ G335), Q293 (≠ H336)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 91% coverage: 41:536/543 of query aligns to 30:495/502 of 3r44A
Sites not aligning to the query:
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 96% coverage: 20:539/543 of query aligns to 4:478/481 of 5busA
- active site: T150 (= T189), S170 (≠ M209), H194 (= H233), T287 (= T331), E288 (= E332)
- binding adenosine monophosphate: H194 (= H233), G262 (= G306), G263 (≠ A307), S283 (≠ V327), M286 (≠ L330), T287 (= T331), D365 (= D423), V377 (≠ I435), R380 (= R438), K467 (= K528)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 95% coverage: 20:536/543 of query aligns to 4:475/475 of 5burA
- active site: T150 (= T189), S170 (≠ M209), H194 (= H233), T287 (= T331), E288 (= E332)
- binding adenosine-5'-triphosphate: T150 (= T189), S151 (= S190), T153 (= T192), T154 (≠ S193), K158 (= K197), G263 (≠ A307), S283 (≠ V327), T287 (= T331), D365 (= D423), V377 (≠ I435), R380 (= R438)
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)
31% identity, 92% coverage: 34:535/543 of query aligns to 48:542/559 of Q67W82
- G395 (= G390) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Query Sequence
>GFF3780 FitnessBrowser__Phaeo:GFF3780
MQKNYEKFGKVAANYVPLSPVSFLNRAETLHSDRPAVIYGDLRRTWGEVATRIRGVAAGL
VSLGIGRGDTVSVLCPNIPELFELQFALPLTGAVINTLNTRLEPETIAYILDHADTKAVI
VDRELIPLLSMAFAAMGRSVSVIEIDDRNVAAPHTLVGKPYEELLTDGAGGAPLDLPQDE
WDAIALNYTSGTSGRPKGVVYHHRGAYLMALGTAAAWQTPHYPIYLSVVPMFHCNGWGHS
WVMAMLGGTMVFTRTPSPDLILDAIRSHGVTHFGAAPIVLQMLAEAEAETGSTTPFDPAI
KVLTAGAPPPPSVLQKTKAMGLDVMQVYGLTETYGHISKCLWQDSWADKIEAEQAQLQAQ
QGIAMPMVEAVSVIDTDTGIPVARDGQTQGEIAVRGNTVMKGYYKDADATDKAFENGWFW
SGDGAVVHADGYMQIRDRLKDVIISGGENISSVEVEAVLYRHPAVQAAAVVAKPDPKWGE
VPCAFIELRTGSDLTSEEIIAFCRTHLAGFKAPKTVVFTSLPKTSTGKIQKFQLRDAAKT
MST
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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