SitesBLAST
Comparing WP_097068839.1 NCBI__GCF_900217815.1:WP_097068839.1 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)
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)
69% identity, 100% coverage: 3:643/644 of query aligns to 7:645/648 of Q89WV5
- G263 (= G259) mutation to I: Loss of activity.
- G266 (= G262) mutation to I: Great decrease in activity.
- K269 (= K265) mutation to G: Great decrease in activity.
- E414 (= E410) mutation to Q: Great decrease in activity.
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)
63% identity, 97% coverage: 14:640/644 of query aligns to 20:645/652 of Q8ZKF6
- R194 (= R189) 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 (= T304) binding CoA
- N335 (≠ T328) binding CoA
- A357 (= A350) 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 (= D512) 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 (= S518) binding CoA
- G524 (= G519) 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 (= R521) 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 (= R579) 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 (= K604) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase 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)
63% identity, 97% coverage: 14:640/644 of query aligns to 20:645/652 of P27550
- K609 (= K604) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
63% identity, 97% coverage: 14:640/644 of query aligns to 16:638/640 of 5jrhA
- active site: T260 (= T257), T412 (= T409), E413 (= E410), N517 (= N516), R522 (= R521), K605 (= K604)
- binding (r,r)-2,3-butanediol: W93 (≠ F91), E140 (= E139), G169 (≠ N168), K266 (= K263), P267 (= P264)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G380), E384 (= E381), P385 (= P382), T408 (= T405), W409 (≠ F406), W410 (= W407), Q411 (= Q408), T412 (= T409), D496 (= D495), I508 (= I507), N517 (= N516), R522 (= R521)
- binding coenzyme a: F159 (= F158), G160 (≠ A159), G161 (= G160), R187 (= R186), S519 (= S518), R580 (= R579), P585 (= P584)
- binding magnesium ion: V533 (= V532), H535 (= H534), I538 (≠ V537)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
63% identity, 97% coverage: 14:640/644 of query aligns to 16:639/641 of 2p20A
- active site: T260 (= T257), T412 (= T409), E413 (= E410), N517 (= N516), R522 (= R521), K605 (= K604)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G380), E384 (= E381), P385 (= P382), T408 (= T405), W409 (≠ F406), W410 (= W407), Q411 (= Q408), T412 (= T409), D496 (= D495), I508 (= I507), R511 (= R510), R522 (= R521)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
63% identity, 97% coverage: 14:640/644 of query aligns to 15:635/637 of 2p2fA
- active site: T259 (= T257), T411 (= T409), E412 (= E410), N516 (= N516), R521 (= R521), K604 (= K604)
- binding adenosine monophosphate: G382 (= G380), E383 (= E381), P384 (= P382), T407 (= T405), W408 (≠ F406), W409 (= W407), Q410 (= Q408), T411 (= T409), D495 (= D495), I507 (= I507), R510 (= R510), N516 (= N516), R521 (= R521)
- binding coenzyme a: F158 (= F158), R186 (= R186), W304 (= W302), T306 (= T304), P329 (= P327), A352 (= A350), A355 (= A353), S518 (= S518), R579 (= R579), P584 (= P584)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
62% identity, 97% coverage: 14:640/644 of query aligns to 16:632/634 of 1pg3A
- active site: T260 (= T257), T412 (= T409), E413 (= E410), N517 (= N516), R522 (= R521), K605 (= K604)
- binding coenzyme a: F159 (= F158), G160 (≠ A159), R187 (= R186), R190 (= R189), A301 (= A298), T307 (= T304), P330 (= P327), A356 (= A353), S519 (= S518), R580 (= R579), P585 (= P584)
- binding magnesium ion: V533 (= V532), H535 (= H534), I538 (≠ V537)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G380), E384 (= E381), P385 (= P382), T408 (= T405), W409 (≠ F406), W410 (= W407), Q411 (= Q408), T412 (= T409), D496 (= D495), R511 (= R510), R522 (= R521)
Q9NR19 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see paper)
55% identity, 99% coverage: 5:640/644 of query aligns to 33:696/701 of Q9NR19