SitesBLAST
Comparing WP_008507389.1 NCBI__GCF_000182725.1:WP_008507389.1 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
64% identity, 98% coverage: 5:626/636 of query aligns to 2:621/627 of 5gxdA
- active site: T238 (= T243), T390 (= T395), E391 (= E396), N498 (= N503), R503 (= R508), K587 (= K592)
- binding adenosine monophosphate: G364 (= G369), E365 (= E370), R366 (= R371), H386 (= H391), W387 (= W392), W388 (= W393), Q389 (= Q394), T390 (= T395), D477 (= D482), I489 (= I494), R492 (= R497), N498 (= N503), R503 (= R508)
- binding coenzyme a: F139 (= F142), G140 (= G143), G141 (= G144), E167 (= E170), R170 (= R173), S279 (= S284), K307 (= K312), P308 (= P313), A332 (= A337), T334 (= T339), A363 (= A368), A500 (= A505), H502 (= H507), K532 (= K537), R562 (= R567), P567 (= P572), V568 (= V573)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
39% identity, 97% coverage: 4:622/636 of query aligns to 19:635/641 of 2p20A
- active site: T260 (= T243), T412 (= T395), E413 (= E396), N517 (= N503), R522 (= R508), K605 (= K592)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G369), E384 (= E370), P385 (≠ R371), T408 (≠ H391), W409 (= W392), W410 (= W393), Q411 (= Q394), T412 (= T395), D496 (= D482), I508 (= I494), R511 (= R497), R522 (= R508)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
39% identity, 97% coverage: 4:622/636 of query aligns to 18:631/637 of 2p2fA
- active site: T259 (= T243), T411 (= T395), E412 (= E396), N516 (= N503), R521 (= R508), K604 (= K592)
- binding adenosine monophosphate: G382 (= G369), E383 (= E370), P384 (≠ R371), T407 (≠ H391), W408 (= W392), W409 (= W393), Q410 (= Q394), T411 (= T395), D495 (= D482), I507 (= I494), R510 (= R497), N516 (= N503), R521 (= R508)
- binding coenzyme a: F158 (= F142), R186 (≠ E170), W304 (= W288), T306 (≠ V290), P329 (= P313), A352 (= A337), A355 (= A340), S518 (≠ A505), R579 (= R567), P584 (= P572)
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, 97% coverage: 4:622/636 of query aligns to 23:641/652 of Q8ZKF6
- R194 (= R173) 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 (≠ V290) binding CoA
- N335 (≠ G315) binding CoA
- A357 (= A337) 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 (= D499) 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 (≠ A505) binding CoA
- G524 (= G506) 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 (= R508) 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 (= R567) 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 (= K592) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
39% identity, 97% coverage: 4:622/636 of query aligns to 19:634/640 of 5jrhA
- active site: T260 (= T243), T412 (= T395), E413 (= E396), N517 (= N503), R522 (= R508), K605 (= K592)
- binding (r,r)-2,3-butanediol: W93 (≠ Y76), E140 (= E123), G169 (≠ T152), K266 (≠ E249), P267 (= P250)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G369), E384 (= E370), P385 (≠ R371), T408 (≠ H391), W409 (= W392), W410 (= W393), Q411 (= Q394), T412 (= T395), D496 (= D482), I508 (= I494), N517 (= N503), R522 (= R508)
- binding coenzyme a: F159 (= F142), G160 (= G143), G161 (= G144), R187 (≠ E170), S519 (≠ A505), R580 (= R567), P585 (= P572)
- binding magnesium ion: V533 (≠ S519), H535 (= H521), I538 (≠ V524)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 97% coverage: 4:622/636 of query aligns to 19:628/634 of 1pg3A
- active site: T260 (= T243), T412 (= T395), E413 (= E396), N517 (= N503), R522 (= R508), K605 (= K592)
- binding coenzyme a: F159 (= F142), G160 (= G143), R187 (≠ E170), R190 (= R173), A301 (≠ S284), T307 (≠ V290), P330 (= P313), A356 (= A340), S519 (≠ A505), R580 (= R567), P585 (= P572)
- binding magnesium ion: V533 (≠ S519), H535 (= H521), I538 (≠ V524)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G369), E384 (= E370), P385 (≠ R371), T408 (≠ H391), W409 (= W392), W410 (= W393), Q411 (= Q394), T412 (= T395), D496 (= D482), R511 (= R497), R522 (= R508)
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)
38% identity, 97% coverage: 3:622/636 of query aligns to 22:641/652 of P27550
- K609 (= K592) 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)
38% identity, 97% coverage: 3:622/636 of query aligns to 21:638/648 of Q89WV5