SitesBLAST
Comparing WP_053937789.1 NCBI__GCF_001294205.1:WP_053937789.1 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: 1:553/554 of query aligns to 1:552/561 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.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
33% identity, 91% coverage: 46:551/554 of query aligns to 27:484/486 of 8wevA
Sites not aligning to the query:
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: 39:550/554 of query aligns to 46:536/546 of Q84P21
- K530 (= K544) 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)
29% identity, 91% coverage: 49:553/554 of query aligns to 30:496/503 of P9WQ37
- K172 (= K222) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ D248) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R250) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I262) 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 (≠ S264) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A267) 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 (≠ P299) 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 (≠ Y434) 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 (= K544) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 91% coverage: 49:553/554 of query aligns to 33:496/502 of 3r44A
Sites not aligning to the query:
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 94% coverage: 31:551/554 of query aligns to 26:526/530 of 5bsmA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding adenosine-5'-triphosphate: S182 (≠ T214), S183 (≠ G215), G184 (= G216), T185 (= T217), T186 (= T218), K190 (= K222), H230 (= H261), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), D413 (= D439), I425 (= I451), R428 (= R454), K519 (= K544)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 94% coverage: 31:551/554 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T214), S201 (≠ N234), H229 (= H261), T328 (= T360), E329 (= E361), K433 (≠ L460), Q438 (≠ N465), K518 (= K544)
- binding adenosine monophosphate: A301 (≠ G334), G326 (= G358), T328 (= T360), D412 (= D439), K429 (= K456), K433 (≠ L460), Q438 (≠ N465)
- binding coenzyme a: L102 (= L107), P226 (= P258), H229 (= H261), Y231 (≠ F263), F253 (≠ R286), K435 (≠ S462), G436 (= G463), F437 (= F464), F498 (≠ N524)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
29% identity, 94% coverage: 31:551/554 of query aligns to 33:533/542 of O24146
- S189 (≠ T214) binding ATP
- S190 (≠ G215) binding ATP
- G191 (= G216) binding ATP
- T192 (= T217) binding ATP
- T193 (= T218) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K222) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H261) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F263) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A267) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P285) binding CoA
- A309 (≠ G334) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E355) binding ATP
- G332 (≠ A356) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T360) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ A365) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M367) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D439) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R454) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K456) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L460) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S462) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G463) binding CoA
- Q446 (≠ N465) binding AMP
- K526 (= K544) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 94% coverage: 31:551/554 of query aligns to 26:526/529 of 5bsvA