SitesBLAST
Comparing WP_062735310.1 NCBI__GCF_001580365.1:WP_062735310.1 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)
50% identity, 96% coverage: 23:700/708 of query aligns to 36:647/651 of P9WQD1
- K617 (= K670) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase 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)
40% identity, 98% coverage: 9:702/708 of query aligns to 19:643/652 of P27550
- K609 (= K670) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
40% identity, 96% coverage: 26:702/708 of query aligns to 34:637/641 of 2p20A
- active site: T260 (= T281), T412 (≠ S458), E413 (= E459), N517 (= N580), R522 (= R585), K605 (= K670)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G429), E384 (= E430), P385 (≠ S431), T408 (= T454), W409 (= W455), W410 (= W456), Q411 (= Q457), T412 (≠ S458), D496 (= D559), I508 (= I571), R511 (= R574), R522 (= R585)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
41% identity, 94% coverage: 19:687/708 of query aligns to 38:628/630 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 (= G429), E392 (= E430), P393 (≠ S431), T416 (= T454), W417 (= W455), W418 (= W456), Q419 (= Q457), T420 (≠ S458), D502 (= D559), R517 (= R574), K523 (≠ N580), R528 (= R585)
- binding magnesium ion: V539 (= V596), H541 (= H598)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
40% identity, 96% coverage: 26:702/708 of query aligns to 34:636/640 of 5jrhA
- active site: T260 (= T281), T412 (≠ S458), E413 (= E459), N517 (= N580), R522 (= R585), K605 (= K670)
- binding (r,r)-2,3-butanediol: W93 (≠ F98), E140 (= E144), G169 (≠ F173), K266 (≠ R287), P267 (= P288)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G429), E384 (= E430), P385 (≠ S431), T408 (= T454), W409 (= W455), W410 (= W456), Q411 (= Q457), T412 (≠ S458), D496 (= D559), I508 (= I571), N517 (= N580), R522 (= R585)
- binding coenzyme a: F159 (= F163), G160 (= G164), G161 (= G165), R187 (= R191), S519 (= S582), R580 (≠ A645), P585 (= P650)
- binding magnesium ion: V533 (= V596), H535 (= H598), I538 (≠ V601)
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)
40% identity, 96% coverage: 26:702/708 of query aligns to 38:643/652 of Q8ZKF6
- R194 (≠ A194) 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 (= T352) binding CoA
- N335 (= N376) binding CoA
- A357 (= A398) 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 (= D576) 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 (= S582) binding CoA
- G524 (= G583) 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 (= R585) 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 (≠ A645) 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 (= K670) modified: N6-acetyllysine; by Pat; mutation to A: No 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)
42% identity, 96% coverage: 26:702/708 of query aligns to 37:640/648 of Q89WV5