SitesBLAST
Comparing WP_011766145.1 NCBI__GCF_000061505.1:WP_011766145.1 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)
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)
52% identity, 96% coverage: 26:652/654 of query aligns to 22:641/652 of P27550
- K609 (= K621) 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)
53% identity, 99% coverage: 8:652/654 of query aligns to 4:638/648 of Q89WV5
- G263 (= G268) mutation to I: Loss of activity.
- G266 (= G271) mutation to I: Great decrease in activity.
- K269 (= K274) mutation to G: Great decrease in activity.
- E414 (= E423) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
52% identity, 96% coverage: 26:652/654 of query aligns to 18:635/641 of 2p20A
- active site: T260 (= T266), T412 (= T422), E413 (= E423), N517 (= N530), R522 (= R535), K605 (= K621)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (≠ F419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (= I521), R511 (= R524), R522 (= R535)
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)
52% identity, 96% coverage: 26:652/654 of query aligns to 22:641/652 of Q8ZKF6
- R194 (≠ K196) 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 (= T313) binding CoA
- N335 (≠ T337) binding CoA
- A357 (= A359) 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 (= D526) 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 (= S532) binding CoA
- G524 (= G533) 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 (= R535) 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 (≠ G596) 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 (= K621) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
P9WQD1 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
54% identity, 95% coverage: 31:654/654 of query aligns to 28:649/651 of P9WQD1
- K617 (= K621) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
52% identity, 96% coverage: 26:652/654 of query aligns to 18:634/640 of 5jrhA
- active site: T260 (= T266), T412 (= T422), E413 (= E423), N517 (= N530), R522 (= R535), K605 (= K621)
- binding (r,r)-2,3-butanediol: W93 (≠ F100), E140 (= E146), G169 (≠ D175), K266 (= K272), P267 (= P273)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (≠ F419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (= I521), N517 (= N530), R522 (= R535)
- binding coenzyme a: F159 (= F165), G160 (= G166), G161 (= G167), R187 (= R193), S519 (= S532), R580 (≠ G596), P585 (= P601)
- binding magnesium ion: V533 (= V546), H535 (= H548), I538 (≠ V551)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
51% identity, 96% coverage: 26:652/654 of query aligns to 17:631/637 of 2p2fA
- active site: T259 (= T266), T411 (= T422), E412 (= E423), N516 (= N530), R521 (= R535), K604 (= K621)
- binding adenosine monophosphate: G382 (= G393), E383 (= E394), P384 (= P395), T407 (= T418), W408 (≠ F419), W409 (= W420), Q410 (= Q421), T411 (= T422), D495 (= D508), I507 (= I521), R510 (= R524), N516 (= N530), R521 (= R535)
- binding coenzyme a: F158 (= F165), R186 (= R193), W304 (= W311), T306 (= T313), P329 (= P336), A352 (= A359), A355 (= A362), S518 (= S532), R579 (≠ G596), P584 (= P601)
Q9QXG4 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 Mus musculus (Mouse) (see paper)
49% identity, 99% coverage: 4:652/654 of query aligns to 23:692/701 of Q9QXG4