SitesBLAST
Comparing WP_054256857.1 NCBI__GCF_001298675.1:WP_054256857.1 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
46% identity, 98% coverage: 13:629/630 of query aligns to 11:621/627 of 5gxdA
- active site: T238 (= T241), T390 (= T390), E391 (= E391), N498 (= N502), R503 (= R507), K587 (= K595)
- binding adenosine monophosphate: G364 (= G364), E365 (= E365), R366 (≠ P366), H386 (≠ N386), W387 (≠ Y387), W388 (= W388), Q389 (= Q389), T390 (= T390), D477 (= D481), I489 (= I493), R492 (= R496), N498 (= N502), R503 (= R507)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (≠ R168), R170 (≠ K171), S279 (= S282), K307 (≠ L310), P308 (= P311), A332 (= A334), T334 (= T336), A363 (= A363), A500 (= A504), H502 (= H506), K532 (= K536), R562 (≠ D570), P567 (≠ A575), V568 (= V576)
Q89WV5 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) (see paper)
41% identity, 99% coverage: 4:625/630 of query aligns to 23:638/648 of Q89WV5
- G263 (= G243) mutation to I: Loss of activity.
- G266 (= G246) mutation to I: Great decrease in activity.
- K269 (= K249) mutation to G: Great decrease in activity.
- E414 (= E391) mutation to Q: Great decrease in activity.
P52910 Acetyl-coenzyme A synthetase 2; Acetate--CoA ligase 2; Acyl-activating enzyme 2; EC 6.2.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
39% identity, 99% coverage: 1:625/630 of query aligns to 37:669/683 of P52910
- K506 (= K469) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
37% identity, 99% coverage: 4:629/630 of query aligns to 39:674/676 of 8rwjD
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: G406 (= G364), P408 (= P366), T431 (≠ N386), Y432 (= Y387), Q434 (= Q389), T435 (= T390), D522 (= D481), R537 (= R496), K638 (= K595)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
40% identity, 99% coverage: 3:625/630 of query aligns to 19:634/640 of 5jrhA
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N502), R522 (= R507), K605 (= K595)
- binding (r,r)-2,3-butanediol: W93 (≠ A74), E140 (= E121), G169 (≠ T150), K266 (= K247), P267 (= P248)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D481), I508 (= I493), N517 (= N502), R522 (= R507)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (= R168), S519 (≠ A504), R580 (≠ D570), P585 (≠ A575)
- binding magnesium ion: V533 (≠ S518), H535 (= H520), I538 (= I523)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
39% identity, 99% coverage: 3:625/630 of query aligns to 19:635/641 of 2p20A
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N502), R522 (= R507), K605 (= K595)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D481), I508 (= I493), R511 (= R496), R522 (= R507)
Q8ZKF6 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
39% identity, 99% coverage: 3:625/630 of query aligns to 23:641/652 of Q8ZKF6
- R194 (≠ K171) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 3-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 2-fold reduction for CoA.
- T311 (≠ V288) binding CoA
- N335 (≠ I312) binding CoA
- A357 (= A334) mutation to V: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 3-fold reduction for CoA.
- D517 (= D498) mutation to G: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 10-fold reduction for CoA.; mutation to P: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold reduction in the affinity for ATP and 4.5-fold reduction for CoA.
- S523 (≠ A504) binding CoA
- G524 (= G505) mutation to L: No acetyl-coenzyme A synthetase activity.; mutation to S: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. Almost the same affinity as the wild-type for ATP, but 9-fold reduction in the affinity for CoA.
- R526 (= R507) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 4-fold reduction for CoA.
- R584 (≠ D570) binding CoA; mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 7-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 8-fold reduction for CoA.
- K609 (= K595) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
P27550 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Escherichia coli (strain K12) (see paper)
39% identity, 99% coverage: 3:625/630 of query aligns to 23:641/652 of P27550