SitesBLAST
Comparing WP_008198284.1 NCBI__GCF_000166275.1:WP_008198284.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
57% identity, 98% coverage: 11:630/630 of query aligns to 23:643/648 of Q89WV5
- G263 (= G249) mutation to I: Loss of activity.
- G266 (= G252) mutation to I: Great decrease in activity.
- K269 (= K255) mutation to G: Great decrease in activity.
- E414 (= E400) 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, 98% coverage: 11:630/630 of query aligns to 24:646/652 of P27550
- K609 (= K593) 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)
55% identity, 98% coverage: 11:630/630 of query aligns to 24:646/652 of Q8ZKF6
- R194 (≠ K180) 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 (= T294) binding CoA
- N335 (≠ T318) binding CoA
- A357 (= A340) 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 (= D501) 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 (= S507) binding CoA
- G524 (= G508) 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 (= R510) 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 (≠ S568) 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 (= K593) 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)
55% identity, 98% coverage: 11:630/630 of query aligns to 20:639/640 of 5jrhA
- active site: T260 (= T247), T412 (= T399), E413 (= E400), N517 (= N505), R522 (= R510), K605 (= K593)
- binding (r,r)-2,3-butanediol: W93 (= W82), E140 (= E130), G169 (≠ D159), K266 (= K253), P267 (= P254)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G370), E384 (= E371), P385 (= P372), T408 (= T395), W409 (= W396), W410 (= W397), Q411 (= Q398), T412 (= T399), D496 (= D484), I508 (= I496), N517 (= N505), R522 (= R510)
- binding coenzyme a: F159 (= F149), G160 (≠ A150), G161 (= G151), R187 (= R177), S519 (= S507), R580 (≠ S568), P585 (= P573)
- binding magnesium ion: V533 (≠ N521), H535 (= H523), I538 (≠ V526)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
55% identity, 98% coverage: 11:630/630 of query aligns to 20:640/641 of 2p20A
- active site: T260 (= T247), T412 (= T399), E413 (= E400), N517 (= N505), R522 (= R510), K605 (= K593)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G370), E384 (= E371), P385 (= P372), T408 (= T395), W409 (= W396), W410 (= W397), Q411 (= Q398), T412 (= T399), D496 (= D484), I508 (= I496), R511 (= R499), R522 (= R510)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
55% identity, 98% coverage: 11:630/630 of query aligns to 19:636/637 of 2p2fA
- active site: T259 (= T247), T411 (= T399), E412 (= E400), N516 (= N505), R521 (= R510), K604 (= K593)
- binding adenosine monophosphate: G382 (= G370), E383 (= E371), P384 (= P372), T407 (= T395), W408 (= W396), W409 (= W397), Q410 (= Q398), T411 (= T399), D495 (= D484), I507 (= I496), R510 (= R499), N516 (= N505), R521 (= R510)
- binding coenzyme a: F158 (= F149), R186 (= R177), W304 (= W292), T306 (= T294), P329 (= P317), A352 (= A340), A355 (= A343), S518 (= S507), R579 (≠ S568), P584 (= P573)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
54% identity, 98% coverage: 11:630/630 of query aligns to 20:633/634 of 1pg3A
- active site: T260 (= T247), T412 (= T399), E413 (= E400), N517 (= N505), R522 (= R510), K605 (= K593)
- binding coenzyme a: F159 (= F149), G160 (≠ A150), R187 (= R177), R190 (≠ K180), A301 (= A288), T307 (= T294), P330 (= P317), A356 (= A343), S519 (= S507), R580 (≠ S568), P585 (= P573)
- binding magnesium ion: V533 (≠ N521), H535 (= H523), I538 (≠ V526)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G370), E384 (= E371), P385 (= P372), T408 (= T395), W409 (= W396), W410 (= W397), Q411 (= Q398), T412 (= T399), D496 (= D484), R511 (= R499), R522 (= R510)
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)
50% identity, 98% coverage: 8:626/630 of query aligns to 37:670/683 of P52910