SitesBLAST
Comparing WP_009156574.1 NCBI__GCF_000244955.1:WP_009156574.1 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)
P9WQD1 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
66% identity, 99% coverage: 1:651/659 of query aligns to 1:650/651 of P9WQD1
- K617 (= K618) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
53% identity, 95% coverage: 33:656/659 of query aligns to 25:646/648 of Q89WV5
- G263 (= G268) mutation to I: Loss of activity.
- G266 (= G271) mutation to I: Great decrease in activity.
- K269 (= K274) mutation to G: Great decrease in activity.
- E414 (= E420) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
51% identity, 93% coverage: 35:648/659 of query aligns to 24:635/641 of 2p20A
- active site: T260 (= T266), T412 (= T419), E413 (= E420), N517 (= N526), R522 (= R531), K605 (= K618)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G390), E384 (= E391), P385 (= P392), T408 (= T415), W409 (= W416), W410 (= W417), Q411 (= Q418), T412 (= T419), D496 (= D505), I508 (≠ L517), R511 (= R520), R522 (= R531)
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)
51% identity, 93% coverage: 35:648/659 of query aligns to 28:641/652 of Q8ZKF6
- R194 (≠ K198) 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 (= T314) binding CoA
- N335 (= N338) binding CoA
- A357 (= A360) 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 (= D522) 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 (= S528) binding CoA
- G524 (= G529) 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 (= R531) 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 (≠ A593) 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 (= K618) 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)
51% identity, 93% coverage: 35:648/659 of query aligns to 24:634/640 of 5jrhA
- active site: T260 (= T266), T412 (= T419), E413 (= E420), N517 (= N526), R522 (= R531), K605 (= K618)
- binding (r,r)-2,3-butanediol: W93 (= W102), E140 (= E148), G169 (≠ S177), K266 (= K272), P267 (= P273)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G390), E384 (= E391), P385 (= P392), T408 (= T415), W409 (= W416), W410 (= W417), Q411 (= Q418), T412 (= T419), D496 (= D505), I508 (≠ L517), N517 (= N526), R522 (= R531)
- binding coenzyme a: F159 (= F167), G160 (= G168), G161 (= G169), R187 (= R195), S519 (= S528), R580 (≠ A593), P585 (= P598)
- binding magnesium ion: V533 (= V542), H535 (= H544), I538 (≠ V547)
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)
50% identity, 95% coverage: 23:646/659 of query aligns to 12:639/652 of P27550
- K609 (= K618) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
51% identity, 93% coverage: 35:648/659 of query aligns to 23:631/637 of 2p2fA
- active site: T259 (= T266), T411 (= T419), E412 (= E420), N516 (= N526), R521 (= R531), K604 (= K618)
- binding adenosine monophosphate: G382 (= G390), E383 (= E391), P384 (= P392), T407 (= T415), W408 (= W416), W409 (= W417), Q410 (= Q418), T411 (= T419), D495 (= D505), I507 (≠ L517), R510 (= R520), N516 (= N526), R521 (= R531)
- binding coenzyme a: F158 (= F167), R186 (= R195), W304 (= W312), T306 (= T314), P329 (= P337), A352 (= A360), A355 (≠ L363), S518 (= S528), R579 (≠ A593), P584 (= P598)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
51% identity, 93% coverage: 35:646/659 of query aligns to 24:626/634 of 1pg3A