SitesBLAST
Comparing WP_062736776.1 NCBI__GCF_001580365.1:WP_062736776.1 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)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
41% identity, 93% coverage: 28:494/500 of query aligns to 29:495/506 of 4gxqA
- active site: T163 (= T160), N183 (= N180), H207 (= H204), T303 (≠ S302), E304 (= E303), I403 (≠ L401), N408 (= N406), A491 (≠ K490)
- binding adenosine-5'-triphosphate: T163 (= T160), S164 (= S161), G165 (= G162), T166 (= T163), T167 (= T164), H207 (= H204), S277 (≠ G276), A278 (= A277), P279 (≠ A278), E298 (= E297), M302 (≠ L301), T303 (≠ S302), D382 (= D380), R397 (= R395)
- binding carbonate ion: H207 (= H204), S277 (≠ G276), R299 (≠ G298), G301 (= G300)
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: 3:496/500 of query aligns to 24:549/561 of P69451
- Y213 (= Y159) mutation to A: Loss of activity.
- T214 (= T160) mutation to A: 10% of wild-type activity.
- G216 (= G162) mutation to A: Decreases activity.
- T217 (= T163) mutation to A: Decreases activity.
- G219 (= G165) mutation to A: Decreases activity.
- K222 (= K168) mutation to A: Decreases activity.
- E361 (= E303) mutation to A: Loss of activity.
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)
34% identity, 94% coverage: 30:500/500 of query aligns to 67:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5ie2A Crystal structure of a plant enzyme (see paper)
34% identity, 99% coverage: 4:496/500 of query aligns to 6:501/506 of 5ie2A
- active site: T165 (= T160), S185 (≠ N180), H209 (= H204), T310 (≠ S302), E311 (= E303), N410 (≠ L401), K415 (≠ N406), K495 (= K490)
- binding adenosine-5'-triphosphate: T165 (= T160), S166 (= S161), G167 (= G162), T168 (= T163), T169 (= T164), S284 (≠ G276), A285 (= A277), S286 (≠ A278), Y307 (= Y299), A308 (≠ G300), M309 (≠ L301), T310 (≠ S302), D389 (= D380), L401 (≠ I392), R404 (= R395), K495 (= K490)
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)
34% identity, 99% coverage: 4:496/500 of query aligns to 6:506/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 160:164) binding ATP
- H214 (= H204) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G276) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAA 276:278) binding ATP
- EA 310:311 (≠ EG 297:298) binding ATP
- M314 (≠ L301) binding oxalate
- T315 (≠ S302) binding ATP
- H319 (≠ P306) binding oxalate; mutation to A: Abolished activity.
- D394 (= D380) binding ATP
- R409 (= R395) binding ATP; mutation to A: Abolished activity.
- K500 (= K490) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
34% identity, 99% coverage: 4:496/500 of query aligns to 6:499/504 of 5ie3A
- active site: T163 (= T160), S183 (≠ N180), H207 (= H204), T308 (≠ S302), E309 (= E303), N408 (≠ L401), K413 (≠ N406), K493 (= K490)
- binding adenosine monophosphate: S164 (= S161), S282 (≠ G276), A283 (= A277), S284 (≠ A278), Y305 (= Y299), A306 (≠ G300), M307 (≠ L301), T308 (≠ S302), D387 (= D380), L399 (≠ I392), R402 (= R395), K493 (= K490)
- binding oxalic acid: V208 (= V205), S282 (≠ G276), A306 (≠ G300), M307 (≠ L301), H312 (≠ P306), K493 (= K490)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 96% coverage: 4:485/500 of query aligns to 6:494/504 of 6qjzA
- active site: T169 (= T160), S189 (≠ N180), H213 (= H204), T314 (≠ S302), E315 (= E303), N414 (≠ L401), K419 (≠ N406)
- binding adenosine monophosphate: H213 (= H204), S288 (≠ G276), A289 (= A277), S290 (≠ A278), A312 (≠ G300), M313 (≠ L301), T314 (≠ S302), D393 (= D380), L405 (≠ I392), K410 (= K397), K419 (≠ N406)
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)
34% identity, 94% coverage: 27:496/500 of query aligns to 59:541/559 of Q67W82
- G395 (= G347) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
34% identity, 99% coverage: 1:493/500 of query aligns to 1:490/503 of P9WQ37
- R9 (≠ A9) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D17) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K168) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T191) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q193) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V205) 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 (≠ G207) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V210) 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 (≠ G241) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G300) 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 (= W375) 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 (= D380) 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 (= R395) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R402) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G404) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K490) 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)
31% identity, 99% coverage: 4:498/500 of query aligns to 20:527/528 of 3ni2A