SitesBLAST
Comparing WP_101589454.1 NCBI__GCF_900169175.1:WP_101589454.1 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)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
41% identity, 91% coverage: 36:503/513 of query aligns to 26:480/486 of 8wevA
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)
35% identity, 96% coverage: 12:506/513 of query aligns to 25:549/561 of P69451
- Y213 (= Y174) mutation to A: Loss of activity.
- T214 (= T175) mutation to A: 10% of wild-type activity.
- G216 (= G177) mutation to A: Decreases activity.
- T217 (= T178) mutation to A: Decreases activity.
- G219 (= G180) mutation to A: Decreases activity.
- K222 (= K183) mutation to A: Decreases activity.
- E361 (= E316) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
34% identity, 95% coverage: 24:509/513 of query aligns to 16:500/506 of 4gxqA
- active site: T163 (= T175), N183 (≠ T195), H207 (= H219), T303 (= T315), E304 (= E316), I403 (= I415), N408 (= N420), A491 (≠ K500)
- binding adenosine-5'-triphosphate: T163 (= T175), S164 (= S176), G165 (= G177), T166 (= T178), T167 (= T179), H207 (= H219), S277 (≠ G289), A278 (= A290), P279 (≠ A291), E298 (= E310), M302 (≠ L314), T303 (= T315), D382 (= D394), R397 (= R409)
- binding carbonate ion: H207 (= H219), S277 (≠ G289), R299 (≠ G311), G301 (= G313)
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)
35% identity, 95% coverage: 21:506/513 of query aligns to 13:493/503 of P9WQ37
- R17 (≠ D25) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K183) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G206) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D208) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V220) 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 (≠ G222) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T225) 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 (= R256) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G313) 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 (= W389) 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 (= D394) 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 (= R409) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ H416) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G418) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K500) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
35% identity, 95% coverage: 21:506/513 of query aligns to 16:493/502 of 3r44A
Sites not aligning to the query:
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
35% identity, 90% coverage: 36:495/513 of query aligns to 27:494/504 of 6qjzA
- active site: T169 (= T175), S189 (≠ T195), H213 (= H219), T314 (= T315), E315 (= E316), N414 (≠ I415), K419 (≠ N420)
- binding adenosine monophosphate: H213 (= H219), S288 (≠ G289), A289 (= A290), S290 (≠ A291), A312 (≠ G313), M313 (≠ L314), T314 (= T315), D393 (= D394), L405 (≠ I406), K410 (= K411), K419 (≠ N420)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 97% coverage: 10:506/513 of query aligns to 7:525/528 of 3ni2A
- active site: S182 (≠ T175), S202 (≠ T195), H230 (= H219), T329 (= T315), E330 (= E316), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F221), S236 (≠ T225), G302 (= G289), A303 (= A290), P304 (≠ A291), G325 (= G311), G327 (= G313), T329 (= T315), P333 (≠ A319), V334 (= V320), D413 (= D394), K430 (= K411), K434 (≠ I415), Q439 (≠ N420)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 97% coverage: 10:506/513 of query aligns to 7:525/528 of 3a9vA
- active site: S182 (≠ T175), S202 (≠ T195), H230 (= H219), T329 (= T315), E330 (= E316), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding adenosine monophosphate: H230 (= H219), G302 (= G289), A303 (= A290), P304 (≠ A291), Y326 (= Y312), G327 (= G313), M328 (≠ L314), T329 (= T315), D413 (= D394), K430 (= K411), K434 (≠ I415), Q439 (≠ N420)
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)
37% identity, 91% coverage: 36:504/513 of query aligns to 27:504/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 175:179) binding ATP
- H214 (= H219) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G289) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAA 289:291) binding ATP
- EA 310:311 (≠ EG 310:311) binding ATP
- M314 (≠ L314) binding oxalate
- T315 (= T315) binding ATP
- H319 (≠ A319) binding oxalate; mutation to A: Abolished activity.
- D394 (= D394) binding ATP
- R409 (= R409) binding ATP; mutation to A: Abolished activity.
- K500 (= K500) binding ATP; binding oxalate; mutation to A: Abolished activity.
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)
32% identity, 91% coverage: 40:507/513 of query aligns to 58:537/546 of Q84P21