SitesBLAST
Comparing WP_025762291.1 NCBI__GCF_000566685.1:WP_025762291.1 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)
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)
58% identity, 98% coverage: 8:624/629 of query aligns to 22:638/648 of Q89WV5
- G263 (= G248) mutation to I: Loss of activity.
- G266 (= G251) mutation to I: Great decrease in activity.
- K269 (= K254) mutation to G: Great decrease in activity.
- E414 (= E399) 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)
56% identity, 99% coverage: 7:626/629 of query aligns to 22:643/652 of P27550
- K609 (= K592) 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)
56% identity, 99% coverage: 7:626/629 of query aligns to 22:643/652 of Q8ZKF6
- R194 (≠ K178) 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 (= T293) binding CoA
- N335 (≠ T317) binding CoA
- A357 (= A339) 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 (= D500) 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 (= S506) binding CoA
- G524 (= G507) 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 (= R509) 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 (≠ S567) 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 (= K592) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
56% identity, 99% coverage: 7:626/629 of query aligns to 18:636/640 of 5jrhA
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N504), R522 (= R509), K605 (= K592)
- binding (r,r)-2,3-butanediol: W93 (= W80), E140 (= E128), G169 (≠ D157), K266 (= K252), P267 (= P253)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G369), E384 (= E370), P385 (= P371), T408 (= T394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D483), I508 (= I495), N517 (= N504), R522 (= R509)
- binding coenzyme a: F159 (= F147), G160 (= G148), G161 (= G149), R187 (= R175), S519 (= S506), R580 (≠ S567), P585 (= P572)
- binding magnesium ion: V533 (≠ N520), H535 (= H522), I538 (≠ V525)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
55% identity, 99% coverage: 7:626/629 of query aligns to 18:637/641 of 2p20A
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N504), R522 (= R509), K605 (= K592)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G369), E384 (= E370), P385 (= P371), T408 (= T394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D483), I508 (= I495), R511 (= R498), R522 (= R509)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
55% identity, 99% coverage: 7:626/629 of query aligns to 17:633/637 of 2p2fA
- active site: T259 (= T246), T411 (= T398), E412 (= E399), N516 (= N504), R521 (= R509), K604 (= K592)
- binding adenosine monophosphate: G382 (= G369), E383 (= E370), P384 (= P371), T407 (= T394), W408 (= W395), W409 (= W396), Q410 (= Q397), T411 (= T398), D495 (= D483), I507 (= I495), R510 (= R498), N516 (= N504), R521 (= R509)
- binding coenzyme a: F158 (= F147), R186 (= R175), W304 (= W291), T306 (= T293), P329 (= P316), A352 (= A339), A355 (= A342), S518 (= S506), R579 (≠ S567), P584 (= P572)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
54% identity, 99% coverage: 7:626/629 of query aligns to 18:630/634 of 1pg3A
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N504), R522 (= R509), K605 (= K592)
- binding coenzyme a: F159 (= F147), G160 (= G148), R187 (= R175), R190 (≠ K178), A301 (= A287), T307 (= T293), P330 (= P316), A356 (= A342), S519 (= S506), R580 (≠ S567), P585 (= P572)
- binding magnesium ion: V533 (≠ N520), H535 (= H522), I538 (≠ V525)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G369), E384 (= E370), P385 (= P371), T408 (= T394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D483), R511 (= R498), R522 (= R509)
Q9NUB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see 3 papers)
52% identity, 98% coverage: 8:624/629 of query aligns to 57:674/689 of Q9NUB1