SitesBLAST
Comparing WP_065397344.1 NCBI__GCF_001684965.1:WP_065397344.1 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
51% identity, 97% coverage: 15:623/628 of query aligns to 14:621/627 of 5gxdA
- active site: T238 (= T240), T390 (= T392), E391 (= E393), N498 (= N500), R503 (= R505), K587 (= K589)
- binding adenosine monophosphate: G364 (= G366), E365 (= E367), R366 (= R368), H386 (= H388), W387 (= W389), W388 (= W390), Q389 (= Q391), T390 (= T392), D477 (= D479), I489 (= I491), R492 (= R494), N498 (= N500), R503 (= R505)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (= E168), R170 (≠ K171), S279 (= S281), K307 (= K309), P308 (= P310), A332 (= A334), T334 (= T336), A363 (= A365), A500 (= A502), H502 (= H504), K532 (= K534), R562 (= R564), P567 (≠ A569), V568 (= V570)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
37% identity, 99% coverage: 4:622/628 of query aligns to 21:637/640 of 5jrhA
- active site: T260 (= T240), T412 (= T392), E413 (= E393), N517 (= N500), R522 (= R505), K605 (= K589)
- binding (r,r)-2,3-butanediol: W93 (≠ Y74), E140 (≠ Q121), G169 (≠ V150), K266 (= K246), P267 (= P247)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G366), E384 (= E367), P385 (≠ R368), T408 (≠ H388), W409 (= W389), W410 (= W390), Q411 (= Q391), T412 (= T392), D496 (= D479), I508 (= I491), N517 (= N500), R522 (= R505)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (≠ E168), S519 (≠ A502), R580 (= R564), P585 (≠ A569)
- binding magnesium ion: V533 (≠ S516), H535 (= H518), I538 (≠ V521)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
37% identity, 99% coverage: 4:622/628 of query aligns to 20:634/637 of 2p2fA
- active site: T259 (= T240), T411 (= T392), E412 (= E393), N516 (= N500), R521 (= R505), K604 (= K589)
- binding adenosine monophosphate: G382 (= G366), E383 (= E367), P384 (≠ R368), T407 (≠ H388), W408 (= W389), W409 (= W390), Q410 (= Q391), T411 (= T392), D495 (= D479), I507 (= I491), R510 (= R494), N516 (= N500), R521 (= R505)
- binding coenzyme a: F158 (= F140), R186 (≠ E168), W304 (= W285), T306 (≠ V287), P329 (= P310), A352 (= A334), A355 (= A337), S518 (≠ A502), R579 (= R564), P584 (≠ A569)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
37% identity, 99% coverage: 4:622/628 of query aligns to 21:638/641 of 2p20A
- active site: T260 (= T240), T412 (= T392), E413 (= E393), N517 (= N500), R522 (= R505), K605 (= K589)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G366), E384 (= E367), P385 (≠ R368), T408 (≠ H388), W409 (= W389), W410 (= W390), Q411 (= Q391), T412 (= T392), D496 (= D479), I508 (= I491), R511 (= R494), R522 (= R505)
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)
37% identity, 99% coverage: 4:622/628 of query aligns to 25:644/652 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 (≠ V287) binding CoA
- N335 (≠ I311) binding CoA
- A357 (= A334) 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 (= D496) 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 (≠ A502) binding CoA
- G524 (= G503) 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 (= R505) 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 (= R564) 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 (= K589) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
37% identity, 98% coverage: 4:620/628 of query aligns to 21:633/634 of 1pg3A
- active site: T260 (= T240), T412 (= T392), E413 (= E393), N517 (= N500), R522 (= R505), K605 (= K589)
- binding coenzyme a: F159 (= F140), G160 (= G141), R187 (≠ E168), R190 (≠ K171), A301 (≠ S281), T307 (≠ V287), P330 (= P310), A356 (= A337), S519 (≠ A502), R580 (= R564), P585 (≠ A569)
- binding magnesium ion: V533 (≠ S516), H535 (= H518), I538 (≠ V521)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G366), E384 (= E367), P385 (≠ R368), T408 (≠ H388), W409 (= W389), W410 (= W390), Q411 (= Q391), T412 (= T392), D496 (= D479), R511 (= R494), R522 (= R505)
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)
37% identity, 98% coverage: 6:622/628 of query aligns to 26:645/648 of Q89WV5
- G263 (= G242) mutation to I: Loss of activity.
- G266 (= G245) mutation to I: Great decrease in activity.
- K269 (= K248) mutation to G: Great decrease in activity.
- E414 (= E393) 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)
36% identity, 99% coverage: 4:622/628 of query aligns to 25:644/652 of P27550