SitesBLAST
Comparing WP_037574635.1 NCBI__GCF_000744815.1:WP_037574635.1 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)
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)
67% identity, 96% coverage: 16:643/652 of query aligns to 12:649/651 of P9WQD1
- K617 (= K611) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
52% identity, 94% coverage: 33:644/652 of query aligns to 28:645/652 of Q8ZKF6
- R194 (≠ K196) 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 (≠ D335) 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 (≠ N526) 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 (≠ G586) 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 (= K611) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
52% identity, 94% coverage: 33:644/652 of query aligns to 24:639/641 of 2p20A
- active site: T260 (= T263), T412 (= T416), E413 (= E417), N517 (≠ L521), R522 (≠ N526), K605 (= K611)
- 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 (≠ L512), R511 (= R515), R522 (≠ N526)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
52% identity, 94% coverage: 33:644/652 of query aligns to 24:638/640 of 5jrhA
- active site: T260 (= T263), T412 (= T416), E413 (= E417), N517 (≠ L521), R522 (≠ N526), K605 (= K611)
- binding (r,r)-2,3-butanediol: W93 (≠ F100), E140 (= E146), G169 (≠ A175), K266 (= K269), P267 (= P270)
- 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 (≠ L512), N517 (≠ L521), R522 (≠ N526)
- binding coenzyme a: F159 (= F165), G160 (= G166), G161 (= G167), R187 (= R193), S519 (= S523), R580 (≠ G586), P585 (= P591)
- binding magnesium ion: V533 (= V537), H535 (= H539), I538 (≠ V542)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
50% identity, 95% coverage: 10:630/652 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 (= G387), E392 (= E388), P393 (= P389), T416 (= T412), W417 (= W413), W418 (= W414), Q419 (= Q415), T420 (= T416), D502 (= D500), R517 (= R515), K523 (≠ L521), R528 (≠ N526)
- binding magnesium ion: V539 (= V537), H541 (= H539)
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)
52% identity, 92% coverage: 43:644/652 of query aligns to 38:645/652 of P27550
- K609 (= K611) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
52% identity, 94% coverage: 33:644/652 of query aligns to 23:635/637 of 2p2fA
- active site: T259 (= T263), T411 (= T416), E412 (= E417), N516 (≠ L521), R521 (≠ N526), K604 (= K611)
- binding adenosine monophosphate: G382 (= G387), E383 (= E388), P384 (= P389), T407 (= T412), W408 (= W413), W409 (= W414), Q410 (= Q415), T411 (= T416), D495 (= D500), I507 (≠ L512), R510 (= R515), N516 (≠ L521), R521 (≠ N526)
- binding coenzyme a: F158 (= F165), R186 (= R193), W304 (= W309), T306 (= T311), P329 (= P334), A352 (= A357), A355 (= A360), S518 (= S523), R579 (≠ G586), P584 (= P591)
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)
52% identity, 93% coverage: 31:639/652 of query aligns to 25:636/648 of Q89WV5