SitesBLAST
Comparing WP_011766904.1 NCBI__GCF_000061505.1:WP_011766904.1 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
44% identity, 99% coverage: 3:628/630 of query aligns to 1:621/627 of 5gxdA
- active site: T238 (= T242), T390 (= T391), E391 (= E392), N498 (= N501), R503 (= R506), K587 (= K594)
- binding adenosine monophosphate: G364 (= G365), E365 (= E366), R366 (≠ P367), H386 (≠ N387), W387 (≠ Y388), W388 (= W389), Q389 (= Q390), T390 (= T391), D477 (= D480), I489 (= I492), R492 (= R495), N498 (= N501), R503 (= R506)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (≠ R168), R170 (≠ K171), S279 (= S283), K307 (≠ T311), P308 (= P312), A332 (= A335), T334 (= T337), A363 (= A364), A500 (= A503), H502 (= H505), K532 (= K535), R562 (≠ D569), P567 (≠ A574), V568 (≠ I575)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
39% identity, 99% coverage: 3:624/630 of query aligns to 19:635/641 of 2p20A
- active site: T260 (= T242), T412 (= T391), E413 (= E392), N517 (= N501), R522 (= R506), K605 (= K594)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G365), E384 (= E366), P385 (= P367), T408 (≠ N387), W409 (≠ Y388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D480), I508 (= I492), R511 (= R495), R522 (= R506)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
39% identity, 99% coverage: 3:624/630 of query aligns to 19:634/640 of 5jrhA
- active site: T260 (= T242), T412 (= T391), E413 (= E392), N517 (= N501), R522 (= R506), K605 (= K594)
- binding (r,r)-2,3-butanediol: W93 (≠ Y74), E140 (= E121), G169 (≠ T150), K266 (= K248), P267 (= P249)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G365), E384 (= E366), P385 (= P367), T408 (≠ N387), W409 (≠ Y388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D480), I508 (= I492), N517 (= N501), R522 (= R506)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (= R168), S519 (≠ A503), R580 (≠ D569), P585 (≠ A574)
- binding magnesium ion: V533 (≠ Q517), H535 (= H519), I538 (= I522)
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)
39% identity, 99% coverage: 3:624/630 of query aligns to 23:641/652 of Q8ZKF6
- R194 (≠ K171) 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 (≠ V289) binding CoA
- N335 (≠ L313) binding CoA
- A357 (= A335) 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 (= D497) 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 (≠ A503) binding CoA
- G524 (= G504) 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 (= R506) 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 (≠ D569) 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 (= K594) 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)
40% identity, 99% coverage: 2:624/630 of query aligns to 21:638/648 of Q89WV5
- G263 (= G244) mutation to I: Loss of activity.
- G266 (= G247) mutation to I: Great decrease in activity.
- K269 (= K250) mutation to G: Great decrease in activity.
- E414 (= E392) 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)
39% identity, 99% coverage: 3:624/630 of query aligns to 23:641/652 of P27550
- K609 (= K594) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
39% identity, 99% coverage: 3:624/630 of query aligns to 18:631/637 of 2p2fA
- active site: T259 (= T242), T411 (= T391), E412 (= E392), N516 (= N501), R521 (= R506), K604 (= K594)
- binding adenosine monophosphate: G382 (= G365), E383 (= E366), P384 (= P367), T407 (≠ N387), W408 (≠ Y388), W409 (= W389), Q410 (= Q390), T411 (= T391), D495 (= D480), I507 (= I492), R510 (= R495), N516 (= N501), R521 (= R506)
- binding coenzyme a: F158 (= F140), R186 (= R168), W304 (= W287), T306 (≠ V289), P329 (= P312), A352 (= A335), A355 (= A338), S518 (≠ A503), R579 (≠ D569), P584 (≠ A574)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 99% coverage: 3:624/630 of query aligns to 19:628/634 of 1pg3A