SitesBLAST
Comparing WP_109939574.1 NCBI__GCF_003173335.1:WP_109939574.1 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)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
49% identity, 97% coverage: 19:625/629 of query aligns to 21:630/630 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 (= G386), E392 (= E387), P393 (= P388), T416 (= T411), W417 (= W412), W418 (= W413), Q419 (= Q414), T420 (= T415), D502 (= D497), R517 (= R512), K523 (≠ I518), R528 (≠ N523)
- binding magnesium ion: V539 (= V534), H541 (= H536)
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)
49% identity, 96% coverage: 29:629/629 of query aligns to 23:631/648 of Q89WV5
- G263 (= G265) mutation to I: Loss of activity.
- G266 (= G268) mutation to I: Great decrease in activity.
- K269 (= K271) mutation to G: Great decrease in activity.
- E414 (= E416) mutation to Q: Great decrease in activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
50% identity, 96% coverage: 29:629/629 of query aligns to 20:627/640 of 5jrhA
- active site: T260 (= T263), T412 (= T415), E413 (= E416), N517 (≠ I518), R522 (≠ N523), K605 (= K606)
- binding (r,r)-2,3-butanediol: W93 (= W99), E140 (= E145), G169 (≠ T174), K266 (≠ Q269), P267 (= P270)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G386), E384 (= E387), P385 (= P388), T408 (= T411), W409 (= W412), W410 (= W413), Q411 (= Q414), T412 (= T415), D496 (= D497), I508 (≠ V509), N517 (≠ I518), R522 (≠ N523)
- binding coenzyme a: F159 (= F164), G160 (≠ A165), G161 (= G166), R187 (= R192), S519 (≠ A520), R580 (= R581), P585 (= P586)
- binding magnesium ion: V533 (= V534), H535 (= H536), I538 (= I539)
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)
49% identity, 96% coverage: 29:629/629 of query aligns to 24:634/652 of P27550
- K609 (= K606) 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)
49% identity, 96% coverage: 29:629/629 of query aligns to 24:634/652 of Q8ZKF6
- R194 (≠ K195) 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 (= T310) binding CoA
- N335 (≠ D334) binding CoA
- A357 (= A356) 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 (= D514) 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 (≠ A520) binding CoA
- G524 (= G521) 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 (≠ N523) 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 (= R581) 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 (= K606) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
49% identity, 96% coverage: 29:629/629 of query aligns to 20:628/641 of 2p20A
- active site: T260 (= T263), T412 (= T415), E413 (= E416), N517 (≠ I518), R522 (≠ N523), K605 (= K606)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G386), E384 (= E387), P385 (= P388), T408 (= T411), W409 (= W412), W410 (= W413), Q411 (= Q414), T412 (= T415), D496 (= D497), I508 (≠ V509), R511 (= R512), R522 (≠ N523)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
49% identity, 96% coverage: 29:629/629 of query aligns to 19:633/637 of 2p2fA
- active site: T259 (= T263), T411 (= T415), E412 (= E416), N516 (≠ I518), R521 (≠ N523), K604 (= K606)
- binding adenosine monophosphate: G382 (= G386), E383 (= E387), P384 (= P388), T407 (= T411), W408 (= W412), W409 (= W413), Q410 (= Q414), T411 (= T415), D495 (= D497), I507 (≠ V509), R510 (= R512), N516 (≠ I518), R521 (≠ N523)
- binding coenzyme a: F158 (= F164), R186 (= R192), W304 (= W308), T306 (= T310), P329 (≠ L333), A352 (= A356), A355 (= A359), S518 (≠ A520), R579 (= R581), P584 (= P586)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
49% identity, 96% coverage: 29:629/629 of query aligns to 20:630/634 of 1pg3A