SitesBLAST
Comparing WP_095511499.1 NCBI__GCF_002283365.1:WP_095511499.1 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)
36% identity, 96% coverage: 15:643/658 of query aligns to 9:630/630 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 (= G402), E392 (≠ S403), P393 (= P404), T416 (≠ Y427), W417 (≠ S428), W418 (≠ G429), Q419 (≠ G430), T420 (= T431), D502 (= D515), R517 (= R530), K523 (= K536), R528 (= R541)
- binding magnesium ion: V539 (≠ N552), H541 (≠ A554)
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)
40% identity, 100% coverage: 1:658/658 of query aligns to 1:651/651 of P9WQD1
- K617 (= K624) modified: N6-acetyllysine; mutation to R: Complete loss of 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)
38% identity, 88% coverage: 81:658/658 of query aligns to 67:642/648 of Q89WV5
- G263 (= G282) mutation to I: Loss of activity.
- G266 (= G285) mutation to I: Great decrease in activity.
- K269 (= K288) mutation to G: Great decrease in activity.
- E414 (= E432) 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)
35% identity, 95% coverage: 37:658/658 of query aligns to 24:645/652 of P27550
- K609 (= K624) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
35% identity, 95% coverage: 35:658/658 of query aligns to 18:638/640 of 5jrhA
- active site: T260 (= T280), T412 (= T431), E413 (= E432), N517 (≠ K536), R522 (= R541), K605 (= K624)
- binding (r,r)-2,3-butanediol: W93 (≠ Y111), E140 (= E157), G169 (≠ T186), K266 (≠ T286), P267 (= P287)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G402), E384 (≠ S403), P385 (= P404), T408 (≠ Y427), W409 (≠ S428), W410 (≠ G429), Q411 (≠ G430), T412 (= T431), D496 (= D515), I508 (≠ L527), N517 (≠ K536), R522 (= R541)
- binding coenzyme a: F159 (= F176), G160 (≠ S177), G161 (= G178), R187 (= R204), S519 (≠ A538), R580 (≠ T599), P585 (≠ K604)
- binding magnesium ion: V533 (≠ N552), H535 (≠ A554), I538 (≠ V557)
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)
35% identity, 95% coverage: 35:658/658 of query aligns to 22:645/652 of Q8ZKF6
- R194 (= R207) 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 (≠ M327) binding CoA
- N335 (≠ D350) binding CoA
- A357 (≠ S372) 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 (= D532) 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 (≠ A538) binding CoA
- G524 (= G539) 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 (= R541) 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 (≠ T599) 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 (= K624) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
34% identity, 95% coverage: 35:658/658 of query aligns to 18:639/641 of 2p20A
- active site: T260 (= T280), T412 (= T431), E413 (= E432), N517 (≠ K536), R522 (= R541), K605 (= K624)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G402), E384 (≠ S403), P385 (= P404), T408 (≠ Y427), W409 (≠ S428), W410 (≠ G429), Q411 (≠ G430), T412 (= T431), D496 (= D515), I508 (≠ L527), R511 (= R530), R522 (= R541)
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
35% identity, 93% coverage: 33:647/658 of query aligns to 35:663/676 of 8rwjD