SitesBLAST
Comparing WP_011771371.1 NCBI__GCF_000015285.1:WP_011771371.1 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)
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)
72% identity, 100% coverage: 1:646/649 of query aligns to 1:646/652 of Q8ZKF6
- R194 (= R194) 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 (= T311) binding CoA
- N335 (= N335) binding CoA
- A357 (= A357) 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 (= D517) 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 (= S523) binding CoA
- G524 (= G524) 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 (= R526) 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 (= R584) 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 (= K609) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase 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)
72% identity, 100% coverage: 1:646/649 of query aligns to 1:646/652 of P27550
- K609 (= K609) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
72% identity, 99% coverage: 5:646/649 of query aligns to 1:639/640 of 5jrhA
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding (r,r)-2,3-butanediol: W93 (= W97), E140 (= E144), G169 (= G173), K266 (≠ T270), P267 (= P271)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), I508 (= I512), N517 (= N521), R522 (= R526)
- binding coenzyme a: F159 (= F163), G160 (= G164), G161 (= G165), R187 (= R191), S519 (= S523), R580 (= R584), P585 (≠ A589)
- binding magnesium ion: V533 (= V537), H535 (= H539), I538 (= I542)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
72% identity, 99% coverage: 5:646/649 of query aligns to 1:640/641 of 2p20A
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), I508 (= I512), R511 (= R515), R522 (= R526)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
72% identity, 99% coverage: 7:646/649 of query aligns to 2:636/637 of 2p2fA
- active site: T259 (= T264), T411 (= T416), E412 (= E417), N516 (= N521), R521 (= R526), K604 (= K609)
- binding adenosine monophosphate: G382 (= G387), E383 (= E388), P384 (= P389), T407 (= T412), W408 (= W413), W409 (= W414), Q410 (= Q415), T411 (= T416), D495 (= D500), I507 (= I512), R510 (= R515), N516 (= N521), R521 (= R526)
- binding coenzyme a: F158 (= F163), R186 (= R191), W304 (= W309), T306 (= T311), P329 (= P334), A352 (= A357), A355 (= A360), S518 (= S523), R579 (= R584), P584 (≠ A589)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
71% identity, 99% coverage: 5:646/649 of query aligns to 1:633/634 of 1pg3A
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding coenzyme a: F159 (= F163), G160 (= G164), R187 (= R191), R190 (= R194), A301 (= A305), T307 (= T311), P330 (= P334), A356 (= A360), S519 (= S523), R580 (= R584), P585 (≠ A589)
- binding magnesium ion: V533 (= V537), H535 (= H539), I538 (= I542)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), R511 (= R515), R522 (= R526)
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)
66% identity, 99% coverage: 4:648/649 of query aligns to 3:644/648 of Q89WV5
- G263 (= G266) mutation to I: Loss of activity.
- G266 (= G269) mutation to I: Great decrease in activity.
- K269 (= K272) mutation to G: Great decrease in activity.
- E414 (= E417) mutation to Q: Great decrease in activity.
Q9NR19 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see paper)
54% identity, 96% coverage: 22:645/649 of query aligns to 45:696/701 of Q9NR19