SitesBLAST
Comparing WP_009152150.1 NCBI__GCF_000244955.1:WP_009152150.1 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)
41% identity, 95% coverage: 8:508/525 of query aligns to 16:533/541 of Q5SKN9
- T184 (= T165) binding Mg(2+)
- G302 (= G278) binding tetradecanoyl-AMP
- Q322 (≠ H298) binding tetradecanoyl-AMP
- G323 (≠ L299) binding tetradecanoyl-AMP
- T327 (= T303) binding tetradecanoyl-AMP
- E328 (= E304) binding Mg(2+)
- D418 (= D394) binding tetradecanoyl-AMP
- K435 (= K411) binding tetradecanoyl-AMP
- K439 (≠ I415) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
39% identity, 93% coverage: 8:495/525 of query aligns to 9:496/510 of 1v26B
- active site: T177 (= T165), H197 (≠ Q185), H223 (= H209), T320 (= T303), E321 (= E304), K432 (≠ I415), W437 (≠ N420)
- binding adenosine monophosphate: G295 (= G278), S296 (≠ A279), A297 (≠ P280), G316 (≠ L299), Y317 (= Y300), G318 (= G301), L319 (= L302), T320 (= T303), D411 (= D394), K428 (= K411), K432 (≠ I415), W437 (≠ N420)
- binding magnesium ion: T177 (= T165), E321 (= E304)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 86% coverage: 8:457/525 of query aligns to 9:464/491 of 1v25A
- active site: T177 (= T165), H197 (≠ Q185), H223 (= H209), T320 (= T303), E321 (= E304), K432 (≠ I415), W437 (≠ N420)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H209), V224 (≠ C210), G295 (= G278), S296 (≠ A279), A297 (≠ P280), Y317 (= Y300), G318 (= G301), L319 (= L302), T320 (= T303), D411 (= D394), I423 (≠ L406), K432 (≠ I415), W437 (≠ N420)
- binding magnesium ion: T177 (= T165), E321 (= E304)
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, 97% coverage: 1:507/525 of query aligns to 1:531/539 of P0DX84
- H231 (= H209) mutation to A: Retains 74% of wild-type activity.
- W235 (= W213) mutation to A: Almost completely abolishes the activity.
- G302 (= G277) mutation to P: Almost completely abolishes the activity.
- G303 (= G278) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y300) mutation to A: Retains 7.7% of wild-type activity.
- P333 (vs. gap) mutation to A: Retains 69% of wild-type activity.
- R432 (= R409) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K411) mutation to A: Retains 36% of wild-type activity.
- D435 (= D412) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I415) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G417) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G418) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E419) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N420) mutation to A: Retains 60% of wild-type activity.
- E474 (= E451) mutation to A: Retains 33% of wild-type activity.
- K523 (= K499) 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 (= K502) 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, 97% coverage: 1:507/525 of query aligns to 1:531/538 of 6ijbB
- active site: T185 (= T165), H205 (≠ Q185), H231 (= H209), S329 (≠ T303), E330 (= E304), K438 (≠ I415), W443 (≠ N420), A523 (≠ K499)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W213), G303 (= G278), A325 (≠ L299), W326 (≠ Y300), G327 (= G301), M328 (≠ L302)
- binding adenosine monophosphate: G303 (= G278), A304 (= A279), A305 (≠ P280), H324 (= H298), W326 (≠ Y300), G327 (= G301), M328 (≠ L302), S329 (≠ T303), Q359 (= Q333), D417 (= D394)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
33% identity, 97% coverage: 1:507/525 of query aligns to 1:528/533 of 6ihkB
- active site: T185 (= T165), H202 (≠ Q185), H228 (= H209), S326 (≠ T303), E327 (= E304), K435 (≠ I415), W440 (≠ N420), K520 (= K499)
- binding adenosine-5'-diphosphate: H228 (= H209), G300 (= G278), A301 (= A279), A302 (≠ P280), H321 (= H298), A322 (≠ L299), W323 (≠ Y300), G324 (= G301), M325 (≠ L302), S326 (≠ T303), Q356 (= Q333), D414 (= D394), R429 (= R409), K520 (= K499)
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)
35% identity, 90% coverage: 35:508/525 of query aligns to 29:496/503 of P9WQ37
- K172 (= K173) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S196) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ S198) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C210) 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 (≠ G212) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ F215) 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 (≠ G245) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G301) 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 (= W389) 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 (= D394) 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 (= R409) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S416) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G418) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K499) 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.
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
31% identity, 90% coverage: 35:507/525 of query aligns to 35:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T165), G174 (= G167), T175 (= T168), T176 (= T169), K180 (= K173), G293 (= G278), A294 (= A279), A295 (≠ P280), Y315 (= Y300), M317 (≠ L302), S318 (≠ T303), D408 (= D394), R423 (= R409)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
31% identity, 90% coverage: 35:507/525 of query aligns to 33:525/528 of 8i6mA