SitesBLAST
Comparing Synpcc7942_1352 FitnessBrowser__SynE:Synpcc7942_1352 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)
55% identity, 98% coverage: 13:652/656 of query aligns to 3:638/648 of Q89WV5
- G263 (= G273) mutation to I: Loss of activity.
- G266 (= G276) mutation to I: Great decrease in activity.
- K269 (= K279) mutation to G: Great decrease in activity.
- E414 (= E424) 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)
54% identity, 97% coverage: 20:654/656 of query aligns to 11:643/652 of P27550
- K609 (= K621) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
54% identity, 97% coverage: 20:654/656 of query aligns to 7:637/641 of 2p20A
- active site: T260 (= T271), T412 (= T423), E413 (= E424), N517 (= N533), R522 (= R538), K605 (= K621)
- binding adenosine-5'-monophosphate-propyl ester: V306 (≠ I317), T307 (= T318), G383 (= G394), E384 (= E395), P385 (= P396), D407 (= D418), T408 (= T419), W409 (= W420), W410 (= W421), Q411 (= Q422), T412 (= T423), D496 (= D512), I508 (≠ V524), R511 (= R527), N517 (= N533), R522 (= R538)
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)
54% identity, 97% coverage: 20:654/656 of query aligns to 11:643/652 of Q8ZKF6
- R194 (≠ A201) 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 (= T318) binding
- N335 (≠ R342) binding
- A357 (= A364) 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 (= D529) 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 (= S535) binding
- G524 (= G536) 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 (= R538) 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 (≠ A596) binding ; 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 (= K621) 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)
54% identity, 97% coverage: 20:654/656 of query aligns to 7:636/640 of 5jrhA
- active site: T260 (= T271), T412 (= T423), E413 (= E424), N517 (= N533), R522 (= R538), K605 (= K621)
- binding (r,r)-2,3-butanediol: W93 (= W105), K102 (≠ R113), V138 (≠ I149), E140 (= E151), G169 (≠ D180), R170 (= R181), L216 (≠ V227), R218 (= R229), Y259 (= Y270), K266 (= K277), P267 (= P278)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G394), E384 (= E395), P385 (= P396), D407 (= D418), T408 (= T419), W409 (= W420), W410 (= W421), Q411 (= Q422), T412 (= T423), D496 (= D512), I508 (≠ V524), R511 (= R527), N517 (= N533), R522 (= R538)
- binding coenzyme a: F159 (= F170), G160 (= G171), G161 (= G172), R187 (= R198), I192 (≠ V203), D302 (= D313), S519 (= S535), H521 (= H537), R580 (≠ A596), P585 (≠ A601)
- binding magnesium ion: V533 (= V549), H535 (= H551), I538 (≠ V554)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
54% identity, 97% coverage: 20:654/656 of query aligns to 6:633/637 of 2p2fA
- active site: T259 (= T271), T411 (= T423), E412 (= E424), N516 (= N533), R521 (= R538), K604 (= K621)
- binding adenosine monophosphate: G382 (= G394), E383 (= E395), P384 (= P396), D406 (= D418), T407 (= T419), W408 (= W420), W409 (= W421), Q410 (= Q422), T411 (= T423), D495 (= D512), I507 (≠ V524), R510 (= R527), N516 (= N533), R521 (= R538)
- binding coenzyme a: F158 (= F170), G159 (= G171), G160 (= G172), R186 (= R198), I191 (≠ V203), A300 (= A312), W304 (= W316), T306 (= T318), V328 (≠ A340), P329 (= P341), A352 (= A364), T354 (= T366), A355 (= A367), S518 (= S535), G519 (= G536), R579 (≠ A596), P584 (≠ A601)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
53% identity, 97% coverage: 20:654/656 of query aligns to 7:630/634 of 1pg3A
- active site: T260 (= T271), T412 (= T423), E413 (= E424), N517 (= N533), R522 (= R538), K605 (= K621)
- binding coenzyme a: F159 (= F170), G160 (= G171), G161 (= G172), R187 (= R198), R190 (≠ A201), I192 (≠ V203),