SitesBLAST
Comparing WP_008203190.1 NCBI__GCF_000166275.1:WP_008203190.1 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)
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)
36% identity, 99% coverage: 7:512/513 of query aligns to 28:549/561 of P69451
- Y213 (= Y176) mutation to A: Loss of activity.
- T214 (= T177) mutation to A: 10% of wild-type activity.
- G216 (= G179) mutation to A: Decreases activity.
- T217 (= T180) mutation to A: Decreases activity.
- G219 (= G182) mutation to A: Decreases activity.
- K222 (= K185) mutation to A: Decreases activity.
- E361 (= E323) mutation to A: Loss of activity.
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, 100% coverage: 1:512/513 of query aligns to 1:493/503 of P9WQ37
- R9 (≠ E9) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ N17) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K185) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ E208) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E210) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I222) 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 (= A224) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V227) 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 (≠ Q258) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G320) 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 (= W395) 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 (= D400) 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 (= R415) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R422) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G424) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K506) 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, 100% coverage: 1:512/513 of query aligns to 4:493/502 of 3r44A
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
33% identity, 99% coverage: 7:512/513 of query aligns to 15:508/518 of 4wv3B
- active site: S175 (≠ T177), T320 (≠ S322), E321 (= E323), K418 (≠ I421), W423 (≠ N426), K502 (= K506)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H221), T221 (≠ I222), F222 (= F223), A293 (≠ G295), S294 (≠ G296), E295 (≠ A297), A296 (= A298), G316 (= G318), I317 (≠ Y319), G318 (= G320), C319 (≠ M321), T320 (≠ S322), D397 (= D400), H409 (≠ I412), R412 (= R415), K502 (= K506)
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 99% coverage: 3:510/513 of query aligns to 5:504/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 177:181) binding ATP
- H214 (= H221) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G296) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAA 296:298) binding ATP
- EA 310:311 (≠ EG 317:318) binding ATP
- M314 (= M321) binding oxalate
- T315 (≠ S322) binding ATP
- H319 (≠ P326) binding oxalate; mutation to A: Abolished activity.
- D394 (= D400) binding ATP
- R409 (= R415) binding ATP; mutation to A: Abolished activity.
- K500 (= K506) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
31% identity, 99% coverage: 3:510/513 of query aligns to 5:499/506 of 5ie2A
- active site: T165 (= T177), S185 (≠ N197), H209 (= H221), T310 (≠ S322), E311 (= E323), N410 (≠ I421), K415 (≠ N426), K495 (= K506)
- binding adenosine-5'-triphosphate: T165 (= T177), S166 (= S178), G167 (= G179), T168 (= T180), T169 (= T181), S284 (≠ G296), A285 (= A297), S286 (≠ A298), Y307 (= Y319), A308 (≠ G320), M309 (= M321), T310 (≠ S322), D389 (= D400), L401 (≠ I412), R404 (= R415), K495 (= K506)
5ie3A Crystal structure of a plant enzyme (see paper)
31% identity, 99% coverage: 3:510/513 of query aligns to 5:497/504 of 5ie3A
- active site: T163 (= T177), S183 (≠ N197), H207 (= H221), T308 (≠ S322), E309 (= E323), N408 (≠ I421), K413 (≠ N426), K493 (= K506)
- binding adenosine monophosphate: S164 (= S178), S282 (≠ G296), A283 (= A297), S284 (≠ A298), Y305 (= Y319), A306 (≠ G320), M307 (= M321), T308 (≠ S322), D387 (= D400), L399 (≠ I412), R402 (= R415), K493 (= K506)
- binding oxalic acid: V208 (≠ I222), S282 (≠ G296), A306 (≠ G320), M307 (= M321), H312 (≠ P326), K493 (= K506)
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)
31% identity, 98% coverage: 8:512/513 of query aligns to 8:476/485 of 5x8fB
- active site: T151 (= T177), S171 (≠ N197), H195 (= H221), T288 (≠ S322), E289 (= E323), I387 (= I421), N392 (= N426), K470 (= K506)
- binding magnesium ion: Y23 (≠ F23), E24 (≠ M24), H70 (≠ F70), N178 (≠ I204), L202 (= L228), L214 (= L241), T296 (= T329), L297 (≠ F330), S298 (≠ N331)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ L85), L191 (= L217), P192 (= P218), H195 (= H221), I196 (= I222), S197 (≠ F223), A237 (≠ G264), V238 (= V265), L260 (≠ V293), G262 (= G295), G286 (= G320), M287 (= M321), S292 (= S325), Q293 (≠ P326), S388 (≠ R422), G389 (≠ K423), G390 (= G424), E391 (≠ L425), K420 (≠ S454), W421 (≠ L455), K450 (≠ S486), Y451 (= Y487)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
32% identity, 94% coverage: 29:512/513 of query aligns to 47:525/528 of 3ni2A