SitesBLAST
Comparing WP_028989221.1 NCBI__GCF_000423825.1:WP_028989221.1 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)
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, 97% coverage: 21:650/652 of query aligns to 12:641/652 of P27550
- K609 (= K619) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
56% identity, 97% coverage: 21:650/652 of query aligns to 8:635/641 of 2p20A
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K619)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (= I520), R511 (= R523), R522 (= R534)
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: 10:650/652 of query aligns to 1:641/652 of Q8ZKF6
- R194 (= R201) 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 (= T317) binding CoA
- N335 (≠ T341) binding CoA
- A357 (= A363) 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 (= D525) 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 (= S531) binding CoA
- G524 (= G532) 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 (= R534) 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 (≠ S594) 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 (= K619) 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)
56% identity, 97% coverage: 21:650/652 of query aligns to 8:634/640 of 5jrhA
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K619)
- binding (r,r)-2,3-butanediol: W93 (= W105), E140 (= E151), G169 (≠ D180), K266 (= K276), P267 (= P277)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (= I520), N517 (= N529), R522 (= R534)
- binding coenzyme a: F159 (= F170), G160 (= G171), G161 (= G172), R187 (= R198), S519 (= S531), R580 (≠ S594), P585 (= P599)
- binding magnesium ion: V533 (= V545), H535 (= H547), I538 (≠ V550)
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)
55% identity, 98% coverage: 14:650/652 of query aligns to 4:638/648 of Q89WV5
- G263 (= G272) mutation to I: Loss of activity.
- G266 (= G275) mutation to I: Great decrease in activity.
- K269 (= K278) mutation to G: Great decrease in activity.
- E414 (= E423) mutation to Q: Great decrease in activity.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
55% identity, 97% coverage: 21:650/652 of query aligns to 7:631/637 of 2p2fA
- active site: T259 (= T270), T411 (= T422), E412 (= E423), N516 (= N529), R521 (= R534), K604 (= K619)
- binding adenosine monophosphate: G382 (= G393), E383 (= E394), P384 (= P395), T407 (= T418), W408 (= W419), W409 (= W420), Q410 (= Q421), T411 (= T422), D495 (= D508), I507 (= I520), R510 (= R523), N516 (= N529), R521 (= R534)
- binding coenzyme a: F158 (= F170), R186 (= R198), W304 (= W315), T306 (= T317), P329 (= P340), A352 (= A363), A355 (= A366), S518 (= S531), R579 (≠ S594), P584 (= P599)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
56% identity, 94% coverage: 21:632/652 of query aligns to 8:618/634 of 1pg3A
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K619)
- binding coenzyme a: F159 (= F170), G160 (= G171), R187 (= R198), R190 (= R201), A301 (= A311), T307 (= T317), P330 (= P340), A356 (= A366), S519 (= S531), R580 (≠ S594), P585 (= P599)
- binding magnesium ion: V533 (= V545), H535 (= H547), I538 (≠ V550)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), R511 (= R523), R522 (= R534)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
52% identity, 96% coverage: 10:634/652 of query aligns to 1:626/630 of 8rplB