SitesBLAST
Comparing WP_085124880.1 NCBI__GCF_900177295.1:WP_085124880.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
34% identity, 94% coverage: 30:518/518 of query aligns to 25:502/506 of 4gxqA
- active site: T163 (= T178), N183 (≠ T199), H207 (= H223), T303 (= T322), E304 (= E323), I403 (= I422), N408 (= N427), A491 (≠ K507)
- binding adenosine-5'-triphosphate: T163 (= T178), S164 (= S179), G165 (= G180), T166 (= T181), T167 (= T182), H207 (= H223), S277 (≠ G296), A278 (= A297), P279 (≠ I298), E298 (≠ D317), M302 (≠ I321), T303 (= T322), D382 (= D401), R397 (= R416)
- binding carbonate ion: H207 (= H223), S277 (≠ G296), R299 (≠ G318), G301 (= G320)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 96% coverage: 16:514/518 of query aligns to 12:484/486 of 8wevA
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)
30% identity, 97% coverage: 12:515/518 of query aligns to 27:551/561 of P69451
- Y213 (= Y177) mutation to A: Loss of activity.
- T214 (= T178) mutation to A: 10% of wild-type activity.
- G216 (= G180) mutation to A: Decreases activity.
- T217 (= T181) mutation to A: Decreases activity.
- G219 (= G183) mutation to A: Decreases activity.
- K222 (= K186) mutation to A: Decreases activity.
- E361 (= E323) mutation to A: Loss of activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
31% identity, 91% coverage: 34:502/518 of query aligns to 31:494/504 of 6qjzA
- active site: T169 (= T178), S189 (≠ V198), H213 (= H223), T314 (= T322), E315 (= E323), N414 (≠ I422), K419 (≠ N427)
- binding adenosine monophosphate: H213 (= H223), S288 (≠ G296), A289 (= A297), S290 (vs. gap), A312 (≠ G320), M313 (≠ I321), T314 (= T322), D393 (= D401), L405 (≠ I413), K410 (= K418), K419 (≠ N427)
5ie2A Crystal structure of a plant enzyme (see paper)
32% identity, 96% coverage: 13:510/518 of query aligns to 9:498/506 of 5ie2A
- active site: T165 (= T178), S185 (≠ V198), H209 (= H223), T310 (= T322), E311 (= E323), N410 (≠ I422), K415 (≠ N427), K495 (= K507)
- binding adenosine-5'-triphosphate: T165 (= T178), S166 (= S179), G167 (= G180), T168 (= T181), T169 (= T182), S284 (≠ G296), A285 (= A297), S286 (≠ I298), Y307 (= Y319), A308 (≠ G320), M309 (≠ I321), T310 (= T322), D389 (= D401), L401 (≠ I413), R404 (= R416), K495 (= K507)
5ie3A Crystal structure of a plant enzyme (see paper)
32% identity, 96% coverage: 13:510/518 of query aligns to 9:496/504 of 5ie3A
- active site: T163 (= T178), S183 (≠ V198), H207 (= H223), T308 (= T322), E309 (= E323), N408 (≠ I422), K413 (≠ N427), K493 (= K507)
- binding adenosine monophosphate: S164 (= S179), S282 (≠ G296), A283 (= A297), S284 (≠ I298), Y305 (= Y319), A306 (≠ G320), M307 (≠ I321), T308 (= T322), D387 (= D401), L399 (≠ I413), R402 (= R416), K493 (= K507)
- binding oxalic acid: V208 (≠ S224), S282 (≠ G296), A306 (≠ G320), M307 (≠ I321), H312 (≠ T326), K493 (= K507)
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, 96% coverage: 13:510/518 of query aligns to 9:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 178:182) binding ATP
- H214 (= H223) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G296) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAI 296:298) binding ATP
- EA 310:311 (≠ DG 317:318) binding ATP
- M314 (≠ I321) binding oxalate
- T315 (= T322) binding ATP
- H319 (≠ T326) binding oxalate; mutation to A: Abolished activity.
- D394 (= D401) binding ATP
- R409 (= R416) binding ATP; mutation to A: Abolished activity.
- K500 (= K507) binding ATP; binding oxalate; mutation to A: Abolished 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)
31% identity, 97% coverage: 13:515/518 of query aligns to 7:495/503 of P9WQ37
- R9 (≠ E15) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E23) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K186) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ A210) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D212) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ S224) 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 (= A226) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L229) 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 (≠ A260) 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 (= W396) 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 (= D401) 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 (= R416) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R423) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G425) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K507) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
32% identity, 93% coverage: 35:515/518 of query aligns to 47:527/528 of 3ni2A