SitesBLAST
Comparing WP_067644159.1 NCBI__GCF_001632775.1:WP_067644159.1 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
45% identity, 99% coverage: 3:625/631 of query aligns to 2:623/627 of 5gxdA
- active site: T238 (= T241), T390 (= T390), E391 (= E391), N498 (= N500), R503 (= R505), K587 (= K589)
- binding adenosine monophosphate: G364 (= G364), E365 (= E365), R366 (≠ P366), H386 (≠ N386), W387 (≠ Y387), W388 (= W388), Q389 (= Q389), T390 (= T390), D477 (= D479), I489 (= I491), R492 (= R494), N498 (= N500), R503 (= R505)
- binding coenzyme a: F139 (= F139), G140 (= G140), G141 (= G141), E167 (≠ R167), R170 (= R170), S279 (= S282), K307 (≠ L310), P308 (= P311), A332 (≠ S334), T334 (= T336), A363 (= A363), A500 (= A502), H502 (= H504), K532 (= K534), R562 (≠ V564), P567 (≠ G569), V568 (= V570)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
42% identity, 98% coverage: 2:618/631 of query aligns to 19:634/641 of 2p20A
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N500), R522 (= R505), K605 (= K589)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D479), I508 (= I491), R511 (= R494), R522 (= R505)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
42% identity, 98% coverage: 2:618/631 of query aligns to 19:633/640 of 5jrhA
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N500), R522 (= R505), K605 (= K589)
- binding (r,r)-2,3-butanediol: W93 (≠ A73), E140 (= E120), G169 (≠ L149), K266 (= K247), P267 (= P248)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D479), I508 (= I491), N517 (= N500), R522 (= R505)
- binding coenzyme a: F159 (= F139), G160 (= G140), G161 (= G141), R187 (= R167), S519 (≠ A502), R580 (≠ V564), P585 (≠ G569)
- binding magnesium ion: V533 (≠ A516), H535 (= H518), I538 (≠ V521)
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)
42% identity, 98% coverage: 2:618/631 of query aligns to 23:640/652 of Q8ZKF6
- R194 (= R170) 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 (≠ V288) binding CoA
- N335 (≠ T312) binding CoA
- A357 (≠ S334) 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 (≠ V564) 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.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
42% identity, 98% coverage: 2:618/631 of query aligns to 18:630/637 of 2p2fA
- active site: T259 (= T241), T411 (= T390), E412 (= E391), N516 (= N500), R521 (= R505), K604 (= K589)
- binding adenosine monophosphate: G382 (= G364), E383 (= E365), P384 (= P366), T407 (≠ N386), W408 (≠ Y387), W409 (= W388), Q410 (= Q389), T411 (= T390), D495 (= D479), I507 (= I491), R510 (= R494), N516 (= N500), R521 (= R505)
- binding coenzyme a: F158 (= F139), R186 (= R167), W304 (= W286), T306 (≠ V288), P329 (= P311), A352 (≠ S334), A355 (≠ G337), S518 (≠ A502), R579 (≠ V564), P584 (≠ G569)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
42% identity, 98% coverage: 2:618/631 of query aligns to 19:627/634 of 1pg3A
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N500), R522 (= R505), K605 (= K589)
- binding coenzyme a: F159 (= F139), G160 (= G140), R187 (= R167), R190 (= R170), A301 (≠ S282), T307 (≠ V288), P330 (= P311), A356 (≠ G337), S519 (≠ A502), R580 (≠ V564), P585 (≠ G569)
- binding magnesium ion: V533 (≠ A516), H535 (= H518), I538 (≠ V521)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D479), R511 (= R494), R522 (= R505)
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)
41% identity, 98% coverage: 2:618/631 of query aligns to 23:640/652 of P27550
- K609 (= K589) modified: N6-acetyllysine; by autocatalysis
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: 2:628/631 of query aligns to 22:647/648 of Q89WV5