SitesBLAST
Comparing WP_017257106.1 NCBI__GCF_000302595.1:WP_017257106.1 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)
59% identity, 98% coverage: 10:634/635 of query aligns to 22:642/648 of Q89WV5
- G263 (= G254) mutation to I: Loss of activity.
- G266 (= G257) mutation to I: Great decrease in activity.
- K269 (= K260) mutation to G: Great decrease in activity.
- E414 (= E405) 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)
55% identity, 98% coverage: 10:634/635 of query aligns to 23:645/652 of P27550
- K609 (= K598) 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, 99% coverage: 9:634/635 of query aligns to 22:645/652 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 (= T299) binding CoA
- N335 (≠ T323) binding CoA
- A357 (= A345) 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 (= D506) 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 (= S512) binding CoA
- G524 (= G513) 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 (= R515) 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 (≠ S573) 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 (= K598) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
54% identity, 99% coverage: 9:634/635 of query aligns to 18:639/641 of 2p20A
- active site: T260 (= T252), T412 (= T404), E413 (= E405), N517 (= N510), R522 (= R515), K605 (= K598)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G375), E384 (= E376), P385 (= P377), T408 (= T400), W409 (= W401), W410 (= W402), Q411 (= Q403), T412 (= T404), D496 (= D489), I508 (= I501), R511 (= R504), R522 (= R515)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
54% identity, 99% coverage: 9:634/635 of query aligns to 18:638/640 of 5jrhA
- active site: T260 (= T252), T412 (= T404), E413 (= E405), N517 (= N510), R522 (= R515), K605 (= K598)
- binding (r,r)-2,3-butanediol: W93 (= W82), E140 (= E130), G169 (≠ D159), K266 (= K258), P267 (= P259)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G375), E384 (= E376), P385 (= P377), T408 (= T400), W409 (= W401), W410 (= W402), Q411 (= Q403), T412 (= T404), D496 (= D489), I508 (= I501), N517 (= N510), R522 (= R515)
- binding coenzyme a: F159 (= F149), G160 (= G150), G161 (= G151), R187 (= R177), S519 (= S512), R580 (≠ S573), P585 (≠ A578)
- binding magnesium ion: V533 (≠ N526), H535 (≠ F528), I538 (≠ V531)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
54% identity, 99% coverage: 9:634/635 of query aligns to 17:635/637 of 2p2fA
- active site: T259 (= T252), T411 (= T404), E412 (= E405), N516 (= N510), R521 (= R515), K604 (= K598)
- binding adenosine monophosphate: G382 (= G375), E383 (= E376), P384 (= P377), T407 (= T400), W408 (= W401), W409 (= W402), Q410 (= Q403), T411 (= T404), D495 (= D489), I507 (= I501), R510 (= R504), N516 (= N510), R521 (= R515)
- binding coenzyme a: F158 (= F149), R186 (= R177), W304 (= W297), T306 (= T299), P329 (= P322), A352 (= A345), A355 (= A348), S518 (= S512), R579 (≠ S573), P584 (≠ A578)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
54% identity, 99% coverage: 9:634/635 of query aligns to 18:632/634 of 1pg3A
- active site: T260 (= T252), T412 (= T404), E413 (= E405), N517 (= N510), R522 (= R515), K605 (= K598)
- binding coenzyme a: F159 (= F149), G160 (= G150), R187 (= R177), R190 (≠ K180), A301 (= A293), T307 (= T299), P330 (= P322), A356 (= A348), S519 (= S512), R580 (≠ S573), P585 (≠ A578)
- binding magnesium ion: V533 (≠ N526), H535 (≠ F528), I538 (≠ V531)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G375), E384 (= E376), P385 (= P377), T408 (= T400), W409 (= W401), W410 (= W402), Q411 (= Q403), T412 (= T404), D496 (= D489), R511 (= R504), R522 (= R515)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
53% identity, 97% coverage: 15:631/635 of query aligns to 28:656/664 of 8u2rA