SitesBLAST
Comparing WP_030535166.1 NCBI__GCF_002893965.1:WP_030535166.1 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)
35% identity, 96% coverage: 19:531/534 of query aligns to 23:531/541 of Q5SKN9
- T184 (= T190) binding Mg(2+)
- G302 (≠ A303) binding tetradecanoyl-AMP
- Q322 (≠ H322) binding tetradecanoyl-AMP
- G323 (≠ V323) binding tetradecanoyl-AMP
- T327 (= T327) binding tetradecanoyl-AMP
- E328 (= E328) binding Mg(2+)
- D418 (= D418) binding tetradecanoyl-AMP
- K435 (= K435) binding tetradecanoyl-AMP
- K439 (≠ I439) binding tetradecanoyl-AMP
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, 93% coverage: 34:531/534 of query aligns to 31:530/539 of P0DX84
- H231 (= H234) mutation to A: Retains 74% of wild-type activity.
- W235 (= W238) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A301) mutation to P: Almost completely abolishes the activity.
- G303 (= G302) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y324) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P332) mutation to A: Retains 69% of wild-type activity.
- R432 (= R433) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K435) mutation to A: Retains 36% of wild-type activity.
- D435 (= D436) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I439) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G441) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G442) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E443) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N444) mutation to A: Retains 60% of wild-type activity.
- E474 (= E475) mutation to A: Retains 33% of wild-type activity.
- K523 (= K524) 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 (= K527) 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, 93% coverage: 34:531/534 of query aligns to 31:530/538 of 6ijbB
- active site: T185 (= T190), H205 (≠ N210), H231 (= H234), S329 (≠ T327), E330 (= E328), K438 (≠ I439), W443 (≠ N444), A523 (≠ K524)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W238), G303 (= G302), A325 (≠ V323), W326 (≠ Y324), G327 (= G325), M328 (≠ L326)
- binding adenosine monophosphate: G303 (= G302), A304 (= A303), A305 (≠ P304), H324 (= H322), W326 (≠ Y324), G327 (= G325), M328 (≠ L326), S329 (≠ T327), Q359 (= Q357), D417 (= D418)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
34% identity, 93% coverage: 34:531/534 of query aligns to 31:527/533 of 6ihkB
- active site: T185 (= T190), H202 (≠ N210), H228 (= H234), S326 (≠ T327), E327 (= E328), K435 (≠ I439), W440 (≠ N444), K520 (= K524)
- binding adenosine-5'-diphosphate: H228 (= H234), G300 (= G302), A301 (= A303), A302 (≠ P304), H321 (= H322), A322 (≠ V323), W323 (≠ Y324), G324 (= G325), M325 (≠ L326), S326 (≠ T327), Q356 (= Q357), D414 (= D418), R429 (= R433), K520 (= K524)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 94% coverage: 19:520/534 of query aligns to 16:496/510 of 1v26B
- active site: T177 (= T190), H197 (≠ N210), H223 (= H234), T320 (= T327), E321 (= E328), K432 (≠ I439), W437 (≠ N444)
- binding adenosine monophosphate: G295 (≠ A303), S296 (≠ P304), A297 (≠ P305), G316 (≠ V323), Y317 (= Y324), G318 (= G325), L319 (= L326), T320 (= T327), D411 (= D418), K428 (= K435), K432 (≠ I439), W437 (≠ N444)
- binding magnesium ion: T177 (= T190), E321 (= E328)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 87% coverage: 19:485/534 of query aligns to 16:468/491 of 1v25A
- active site: T177 (= T190), H197 (≠ N210), H223 (= H234), T320 (= T327), E321 (= E328), K432 (≠ I439), W437 (≠ N444)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H234), V224 (≠ C235), G295 (≠ A303), S296 (≠ P304), A297 (≠ P305), Y317 (= Y324), G318 (= G325), L319 (= L326), T320 (= T327), D411 (= D418), I423 (≠ L430), K432 (≠ I439), W437 (≠ N444)
- binding magnesium ion: T177 (= T190), E321 (= E328)
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, 96% coverage: 19:531/534 of query aligns to 7:494/503 of P9WQ37
- R9 (≠ E21) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E29) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K198) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (vs. gap) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A223) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C235) 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 (≠ G237) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T240) 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 (≠ G270) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G325) 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 (= W413) 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 (= D418) 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 (= R433) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S440) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G442) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K524) 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, 96% coverage: 19:531/534 of query aligns to 10:494/502 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)
28% identity, 96% coverage: 19:531/534 of query aligns to 7:477/484 of 5gtdA