SitesBLAST
Comparing WP_106712922.1 NCBI__GCF_003010955.1:WP_106712922.1 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
35% identity, 95% coverage: 15:526/537 of query aligns to 2:486/486 of 8wevA
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)
33% identity, 90% coverage: 44:526/537 of query aligns to 31:496/503 of P9WQ37
- K172 (= K190) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T215) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K217) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ G229) 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 (≠ G231) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ Q234) 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 (≠ Q265) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G324) 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 (= W406) 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 (= D411) 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 (= R426) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S433) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G435) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K517) 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)
32% identity, 90% coverage: 44:526/537 of query aligns to 34:496/502 of 3r44A
Sites not aligning to the query:
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)
29% identity, 95% coverage: 19:530/537 of query aligns to 6:513/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 182:186) binding ATP
- H214 (= H228) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G300) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAP 300:302) binding ATP
- EA 310:311 (≠ QY 321:322) binding ATP
- M314 (≠ L325) binding oxalate
- T315 (≠ G326) binding ATP
- H319 (≠ G330) binding oxalate; mutation to A: Abolished activity.
- D394 (= D411) binding ATP
- R409 (= R426) binding ATP; mutation to A: Abolished activity.
- K500 (= K517) binding ATP; binding oxalate; mutation to A: Abolished activity.
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
29% identity, 96% coverage: 21:533/537 of query aligns to 6:484/485 of 5x8fB
- active site: T151 (= T182), S171 (≠ V202), H195 (= H228), T288 (≠ G326), E289 (= E327), I387 (= I432), N392 (= N437), K470 (= K517)
- binding magnesium ion: Y23 (≠ W38), E24 (≠ G39), H70 (≠ F86), N178 (≠ D209), L202 (= L235), L214 (= L247), T296 (≠ V334), L297 (= L335), S298 (≠ P336)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R101), L191 (≠ A224), P192 (= P225), H195 (= H228), I196 (≠ G229), S197 (≠ A230), A237 (≠ T271), V238 (= V272), L260 (≠ I297), G262 (≠ A299), G286 (= G324), M287 (≠ L325), S292 (≠ G330), Q293 (≠ N331), S388 (= S433), G389 (= G434), G390 (= G435), E391 (≠ S436), K420 (≠ M465), W421 (= W466), K450 (≠ H497), Y451 (= Y498)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 96% coverage: 21:533/537 of query aligns to 6:484/484 of 5gtdA
- active site: T151 (= T182), S171 (≠ V202), H195 (= H228), T288 (≠ G326), E289 (= E327)
- binding adenosine-5'-monophosphate: G263 (= G300), G264 (vs. gap), Y285 (≠ F323), G286 (= G324), M287 (≠ L325), T288 (≠ G326), D366 (= D411), V378 (≠ I423)
- binding magnesium ion: F314 (≠ T358), S315 (≠ G359)
- binding 2-succinylbenzoate: H195 (= H228), S197 (≠ A230), A237 (≠ T271), L260 (≠ I297), G262 (≠ A299), G263 (= G300), G286 (= G324), M287 (≠ L325), S292 (≠ G330), Q293 (≠ N331)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 95% coverage: 19:528/537 of query aligns to 6:506/506 of 5ie2A
- active site: T165 (= T182), S185 (≠ V202), H209 (= H228), T310 (≠ G326), E311 (= E327), N410 (≠ I432), K415 (≠ N437), K495 (= K517)
- binding adenosine-5'-triphosphate: T165 (= T182), S166 (= S183), G167 (= G184), T168 (= T185), T169 (= T186), S284 (≠ G300), A285 (= A301), S286 (≠ P302), Y307 (≠ F323), A308 (≠ G324), M309 (≠ L325), T310 (≠ G326), D389 (= D411), L401 (≠ I423), R404 (= R426), K495 (= K517)
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 95% coverage: 19:528/537 of query aligns to 6:504/504 of 5ie3A
- active site: T163 (= T182), S183 (≠ V202), H207 (= H228), T308 (≠ G326), E309 (= E327), N408 (≠ I432), K413 (≠ N437), K493 (= K517)
- binding adenosine monophosphate: S164 (= S183), S282 (≠ G300), A283 (= A301), S284 (≠ P302), Y305 (≠ F323), A306 (≠ G324), M307 (≠ L325), T308 (≠ G326), D387 (= D411), L399 (≠ I423), R402 (= R426), K493 (= K517)
- binding oxalic acid: V208 (≠ I232), S282 (≠ G300), A306 (≠ G324), M307 (≠ L325), H312 (≠ G330), K493 (= K517)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
31% identity, 95% coverage: 19:530/537 of query aligns to 29:533/536 of 5wm2A