SitesBLAST
Comparing WP_011386526.1 AMB_RS21140 acetate--CoA ligase 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)
76% identity, 100% coverage: 1:644/645 of query aligns to 1:645/648 of Q89WV5
- G263 (= G261) mutation to I: Loss of activity.
- G266 (= G264) mutation to I: Great decrease in activity.
- K269 (= K267) mutation to G: Great decrease in activity.
- E414 (= E412) 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)
68% identity, 100% coverage: 1:642/645 of query aligns to 1:646/652 of P27550
- K609 (= K605) 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)
68% identity, 99% coverage: 5:642/645 of query aligns to 7:646/652 of Q8ZKF6
- R194 (= R191) 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 (= T306) binding
- N335 (= N330) binding
- A357 (= A352) 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 (= D513) 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 (= S519) binding
- G524 (= G520) 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 (= R522) 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 (= R580) binding ; 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 (= K605) 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)
68% identity, 99% coverage: 5:642/645 of query aligns to 3:639/640 of 5jrhA
- active site: T260 (= T259), T412 (= T411), E413 (= E412), N517 (= N517), R522 (= R522), K605 (= K605)
- binding (r,r)-2,3-butanediol: W93 (= W94), K102 (≠ A103), V138 (≠ I139), E140 (= E141), G169 (= G170), R170 (= R171), L216 (≠ V215), R218 (= R217), Y259 (= Y258), K266 (= K265), P267 (= P266)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G382), E384 (= E383), P385 (= P384), D407 (= D406), T408 (= T407), W409 (= W408), W410 (= W409), Q411 (= Q410), T412 (= T411), D496 (= D496), I508 (= I508), R511 (= R511), N517 (= N517), R522 (= R522)
- binding coenzyme a: F159 (= F160), G160 (= G161), G161 (= G162), R187 (= R188), I192 (≠ V193), D302 (= D301), S519 (= S519), H521 (= H521), R580 (= R580), P585 (= P585)
- binding magnesium ion: V533 (= V533), H535 (= H535), I538 (≠ V538)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
68% identity, 99% coverage: 5:642/645 of query aligns to 3:640/641 of 2p20A
- active site: T260 (= T259), T412 (= T411), E413 (= E412), N517 (= N517), R522 (= R522), K605 (= K605)
- binding adenosine-5'-monophosphate-propyl ester: V306 (= V305), T307 (= T306), G383 (= G382), E384 (= E383), P385 (= P384), D407 (= D406), T408 (= T407), W409 (= W408), W410 (= W409), Q411 (= Q410), T412 (= T411), D496 (= D496), I508 (= I508), R511 (= R511), N517 (= N517), R522 (= R522)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
68% identity, 99% coverage: 5:642/645 of query aligns to 2:636/637 of 2p2fA
- active site: T259 (= T259), T411 (= T411), E412 (= E412), N516 (= N517), R521 (= R522), K604 (= K605)
- binding adenosine monophosphate: G382 (= G382), E383 (= E383), P384 (= P384), D406 (= D406), T407 (= T407), W408 (= W408), W409 (= W409), Q410 (= Q410), T411 (= T411), D495 (= D496), I507 (= I508), R510 (= R511), N516 (= N517), R521 (= R522)
- binding coenzyme a: F158 (= F160), G159 (= G161), G160 (= G162), R186 (= R188), I191 (≠ V193), A300 (= A300), W304 (= W304), T306 (= T306), V328 (≠ I328), P329 (= P329), A352 (= A352), T354 (= T354), A355 (= A355), S518 (= S519), G519 (= G520), R579 (= R580), P584 (= P585)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
67% identity, 99% coverage: 5:642/645 of query aligns to 3:633/634 of 1pg3A