SitesBLAST
Comparing WP_019387229.1 NCBI__GCF_000283015.1:WP_019387229.1 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
53% identity, 99% coverage: 2:625/632 of query aligns to 1:625/627 of 5gxdA
- active site: T238 (= T239), T390 (= T391), E391 (= E392), N498 (= N499), R503 (= R504), K587 (= K588)
- binding adenosine monophosphate: G364 (= G365), E365 (= E366), R366 (= R367), H386 (= H387), W387 (= W388), W388 (= W389), Q389 (= Q390), T390 (= T391), D477 (= D478), I489 (= I490), R492 (= R493), N498 (= N499), R503 (= R504)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (= E168), R170 (≠ K171), S279 (= S280), K307 (= K308), P308 (= P309), A332 (= A333), T334 (= T335), A363 (= A364), A500 (= A501), H502 (= H503), K532 (= K533), R562 (= R563), P567 (≠ A568), V568 (= V569)
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)
39% identity, 97% coverage: 3:618/632 of query aligns to 23:638/648 of Q89WV5
- G263 (= G241) mutation to I: Loss of activity.
- G266 (= G244) mutation to I: Great decrease in activity.
- K269 (= K247) mutation to G: Great decrease in activity.
- E414 (= E392) mutation to Q: Great decrease in 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, 98% coverage: 2:618/632 of query aligns to 23:641/652 of P27550
- K609 (= K588) modified: N6-acetyllysine; by autocatalysis
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)
38% identity, 98% coverage: 2:618/632 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 (≠ V286) binding CoA
- N335 (≠ R311) binding CoA
- A357 (= A333) 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 (= D495) 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 (≠ A501) binding CoA
- G524 (= G502) 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 (= R504) 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 (= R563) 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 (= K588) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
38% identity, 98% coverage: 2:618/632 of query aligns to 19:635/641 of 2p20A
- active site: T260 (= T239), T412 (= T391), E413 (= E392), N517 (= N499), R522 (= R504), K605 (= K588)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G365), E384 (= E366), P385 (≠ R367), T408 (≠ H387), W409 (= W388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D478), I508 (= I490), R511 (= R493), R522 (= R504)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
38% identity, 98% coverage: 2:618/632 of query aligns to 18:631/637 of 2p2fA
- active site: T259 (= T239), T411 (= T391), E412 (= E392), N516 (= N499), R521 (= R504), K604 (= K588)
- binding adenosine monophosphate: G382 (= G365), E383 (= E366), P384 (≠ R367), T407 (≠ H387), W408 (= W388), W409 (= W389), Q410 (= Q390), T411 (= T391), D495 (= D478), I507 (= I490), R510 (= R493), N516 (= N499), R521 (= R504)
- binding coenzyme a: F158 (= F140), R186 (≠ E168), W304 (= W284), T306 (≠ V286), P329 (= P309), A352 (= A333), A355 (= A336), S518 (≠ A501), R579 (= R563), P584 (≠ A568)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
38% identity, 98% coverage: 2:618/632 of query aligns to 19:634/640 of 5jrhA
- active site: T260 (= T239), T412 (= T391), E413 (= E392), N517 (= N499), R522 (= R504), K605 (= K588)
- binding (r,r)-2,3-butanediol: W93 (≠ Y74), E140 (≠ Q121), G169 (≠ I150), K266 (≠ T245), P267 (= P246)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G365), E384 (= E366), P385 (≠ R367), T408 (≠ H387), W409 (= W388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D478), I508 (= I490), N517 (= N499), R522 (= R504)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (≠ E168), S519 (≠ A501), R580 (= R563), P585 (≠ A568)
- binding magnesium ion: V533 (≠ A515), H535 (≠ N517), I538 (≠ V520)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 94% coverage: 2:598/632 of query aligns to 19:615/634 of 1pg3A