SitesBLAST
Comparing WP_059150936.1 NCBI__GCF_001046635.1:WP_059150936.1 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)
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, 97% coverage: 9:536/545 of query aligns to 3:495/503 of P9WQ37
- R9 (= R15) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D23) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K207) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T230) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E232) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I244) 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 (≠ G246) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ P249) 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 (≠ G279) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G340) 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 (= W418) 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 (= D423) 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 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K528) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
30% identity, 98% coverage: 2:536/545 of query aligns to 28:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
32% identity, 97% coverage: 9:536/545 of query aligns to 6:495/502 of 3r44A
Sites not aligning to the query:
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)
29% identity, 97% coverage: 9:536/545 of query aligns to 24:551/561 of P69451
- Y213 (= Y198) mutation to A: Loss of activity.
- T214 (= T199) mutation to A: 10% of wild-type activity.
- G216 (= G201) mutation to A: Decreases activity.
- T217 (= T202) mutation to A: Decreases activity.
- G219 (≠ A204) mutation to A: Decreases activity.
- K222 (= K207) mutation to A: Decreases activity.
- E361 (= E343) mutation to A: Loss of activity.
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)
28% identity, 96% coverage: 9:531/545 of query aligns to 5:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 199:203) binding ATP
- H214 (= H243) binding ATP; mutation to A: Abolished activity.
- S289 (≠ F315) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ FAV 315:317) binding ATP
- EA 310:311 (≠ GT 337:338) binding ATP
- M314 (≠ L341) binding oxalate
- T315 (= T342) binding ATP
- H319 (≠ G346) binding oxalate; mutation to A: Abolished activity.
- D394 (= D423) binding ATP
- R409 (= R438) binding ATP; mutation to A: Abolished activity.
- K500 (= K528) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 96% coverage: 9:531/545 of query aligns to 5:496/504 of 5ie3A
- active site: T163 (= T199), S183 (≠ N219), H207 (= H243), T308 (= T342), E309 (= E343), N408 (≠ K444), K413 (≠ N449), K493 (= K528)
- binding adenosine monophosphate: S164 (= S200), S282 (≠ F315), A283 (= A316), S284 (≠ V317), Y305 (= Y339), A306 (≠ G340), M307 (≠ L341), T308 (= T342), D387 (= D423), L399 (≠ F435), R402 (= R438), K493 (= K528)
- binding oxalic acid: V208 (≠ I244), S282 (≠ F315), A306 (≠ G340), M307 (≠ L341), H312 (≠ G346), K493 (= K528)
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 96% coverage: 9:531/545 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T199), S185 (≠ N219), H209 (= H243), T310 (= T342), E311 (= E343), N410 (≠ K444), K415 (≠ N449), K495 (= K528)
- binding adenosine-5'-triphosphate: T165 (= T199), S166 (= S200), G167 (= G201), T168 (= T202), T169 (= T203), S284 (≠ F315), A285 (= A316), S286 (≠ V317), Y307 (= Y339), A308 (≠ G340), M309 (≠ L341), T310 (= T342), D389 (= D423), L401 (≠ F435), R404 (= R438), K495 (= K528)
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)
31% identity, 93% coverage: 36:540/545 of query aligns to 62:547/559 of Q67W82
- G395 (= G390) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
30% identity, 93% coverage: 36:542/545 of query aligns to 55:540/542 of O24146