SitesBLAST
Comparing WP_017219985.1 NCBI__GCF_000276805.1:WP_017219985.1 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)
64% identity, 100% coverage: 1:551/551 of query aligns to 1:551/561 of P69451
- Y213 (= Y213) mutation to A: Loss of activity.
- T214 (= T214) mutation to A: 10% of wild-type activity.
- G216 (= G216) mutation to A: Decreases activity.
- T217 (= T217) mutation to A: Decreases activity.
- G219 (= G219) mutation to A: Decreases activity.
- K222 (= K222) mutation to A: Decreases activity.
- E361 (= E361) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 92% coverage: 46:551/551 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T214), N183 (= N234), H207 (= H261), T303 (= T360), E304 (= E361), I403 (≠ L460), N408 (= N465), A491 (≠ K543)
- binding adenosine-5'-triphosphate: T163 (= T214), S164 (≠ G215), G165 (= G216), T166 (= T217), T167 (= T218), H207 (= H261), S277 (≠ G334), A278 (≠ M335), P279 (≠ A336), E298 (= E355), M302 (≠ L359), T303 (= T360), D382 (= D439), R397 (= R454)
- binding carbonate ion: H207 (= H261), S277 (≠ G334), R299 (≠ G356), G301 (= G358)
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 92% coverage: 44:549/551 of query aligns to 53:536/546 of Q84P21
- K530 (= K543) mutation to N: Lossed enzymatic 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)
30% identity, 91% coverage: 49:551/551 of query aligns to 30:495/503 of P9WQ37
- K172 (= K222) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R248) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K250) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V262) 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 (= A264) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V267) 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 (≠ K299) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G358) 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 (= W434) 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 (= D439) 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 (= R454) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V461) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G463) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K543) 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.
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)
29% identity, 99% coverage: 4:550/551 of query aligns to 18:542/559 of Q67W82
- G395 (= G406) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
27% identity, 99% coverage: 4:550/551 of query aligns to 22:547/556 of Q9S725
- K211 (= K222) mutation to S: Drastically reduces the activity.
- M293 (≠ T304) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V331) mutation K->L,A: Affects the substrate specificity.
- E401 (= E407) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q409) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R454) mutation to Q: Drastically reduces the activity.
- K457 (≠ S462) mutation to S: Drastically reduces the activity.
- K540 (= K543) mutation to N: Abolishes the activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 95% coverage: 31:551/551 of query aligns to 26:527/528 of 3ni2A
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K543)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F263), S236 (≠ N268), G302 (= G334), A303 (≠ M335), P304 (≠ A336), G325 (= G356), G327 (= G358), T329 (= T360), P333 (= P364), V334 (≠ L365), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 95% coverage: 31:551/551 of query aligns to 26:527/528 of 3a9vA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K543)
- binding adenosine monophosphate: H230 (= H261), G302 (= G334), A303 (≠ M335), P304 (≠ A336), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 91% coverage: 49:551/551 of query aligns to 33:495/502 of 3r44A