SitesBLAST
Comparing 2629598430 IMG__TrieryIMS101_FD:2629598430 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)
55% identity, 98% coverage: 13:651/655 of query aligns to 3:638/648 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.
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, 95% coverage: 32:651/655 of query aligns to 22:641/652 of P27550
- K609 (= K620) modified: N6-acetyllysine; by autocatalysis
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
53% identity, 96% coverage: 10:640/655 of query aligns to 1:630/630 of 8rplB
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: G391 (= G393), E392 (= E394), P393 (= P395), T416 (= T418), W417 (= W419), W418 (= W420), Q419 (= Q421), T420 (= T422), D502 (= D511), R517 (= R526), K523 (≠ N532), R528 (= R537)
- binding magnesium ion: V539 (= V548), H541 (= H550)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
54% identity, 95% coverage: 32:651/655 of query aligns to 18:635/641 of 2p20A
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N532), R522 (= R537), K605 (= K620)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D511), I508 (≠ V523), R511 (= R526), R522 (= R537)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
54% identity, 95% coverage: 32:651/655 of query aligns to 18:634/640 of 5jrhA
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N532), R522 (= R537), K605 (= K620)
- binding (r,r)-2,3-butanediol: W93 (= W105), E140 (= E151), G169 (≠ N180), K266 (≠ T276), 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 (= D511), I508 (≠ V523), N517 (= N532), R522 (= R537)
- binding coenzyme a: F159 (= F170), G160 (= G171), G161 (= G172), R187 (= R198), S519 (≠ A534), R580 (≠ V595), P585 (≠ A600)
- binding magnesium ion: V533 (= V548), H535 (= H550), I538 (≠ V553)
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)
54% identity, 95% coverage: 32:651/655 of query aligns to 22:641/652 of Q8ZKF6
- R194 (≠ A201) 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 (≠ R341) 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 (= D528) 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 (≠ A534) binding CoA
- G524 (= G535) 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 (= R537) 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 (≠ V595) 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 (= K620) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
54% identity, 95% coverage: 32:651/655 of query aligns to 17:631/637 of 2p2fA
- active site: T259 (= T270), T411 (= T422), E412 (= E423), N516 (= N532), R521 (= R537), K604 (= K620)
- binding adenosine monophosphate: G382 (= G393), E383 (= E394), P384 (= P395), T407 (= T418), W408 (= W419), W409 (= W420), Q410 (= Q421), T411 (= T422), D495 (= D511), I507 (≠ V523), R510 (= R526), N516 (= N532), R521 (= R537)
- binding coenzyme a: F158 (= F170), R186 (= R198), W304 (= W315), T306 (= T317), P329 (= P340), A352 (= A363), A355 (= A366), S518 (≠ A534), R579 (≠ V595), P584 (≠ A600)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
54% identity, 95% coverage: 32:651/655 of query aligns to 18:628/634 of 1pg3A