SitesBLAST
Comparing WP_047005978.1 NCBI__GCF_001010925.1:WP_047005978.1 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)
67% identity, 97% coverage: 20:642/642 of query aligns to 22:645/648 of Q89WV5
- G263 (= G260) mutation to I: Loss of activity.
- G266 (= G263) mutation to I: Great decrease in activity.
- K269 (= K266) mutation to G: Great decrease in activity.
- E414 (= E411) 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)
63% identity, 97% coverage: 16:640/642 of query aligns to 19:646/652 of P27550
- K609 (= K603) modified: N6-acetyllysine; by autocatalysis
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)
64% identity, 97% coverage: 17:640/642 of query aligns to 20:646/652 of Q8ZKF6
- R194 (≠ K191) 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 (= T305) binding CoA
- N335 (= N329) binding CoA
- A357 (= A351) 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 (= D511) 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 (= S517) binding CoA
- G524 (= G518) 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 (= R520) 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 (= R578) 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 (= K603) 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)
64% identity, 97% coverage: 17:640/642 of query aligns to 16:639/640 of 5jrhA
- active site: T260 (= T258), T412 (= T410), E413 (= E411), N517 (= N515), R522 (= R520), K605 (= K603)
- binding (r,r)-2,3-butanediol: W93 (≠ F93), E140 (= E141), G169 (= G170), K266 (≠ T264), P267 (= P265)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G381), E384 (= E382), P385 (= P383), T408 (= T406), W409 (= W407), W410 (= W408), Q411 (= Q409), T412 (= T410), D496 (= D494), I508 (= I506), N517 (= N515), R522 (= R520)
- binding coenzyme a: F159 (= F160), G160 (= G161), G161 (= G162), R187 (= R188), S519 (= S517), R580 (= R578), P585 (= P583)
- binding magnesium ion: V533 (= V531), H535 (= H533), I538 (≠ V536)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
63% identity, 97% coverage: 17:640/642 of query aligns to 16:640/641 of 2p20A
- active site: T260 (= T258), T412 (= T410), E413 (= E411), N517 (= N515), R522 (= R520), K605 (= K603)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G381), E384 (= E382), P385 (= P383), T408 (= T406), W409 (= W407), W410 (= W408), Q411 (= Q409), T412 (= T410), D496 (= D494), I508 (= I506), R511 (= R509), R522 (= R520)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
63% identity, 97% coverage: 17:640/642 of query aligns to 15:636/637 of 2p2fA
- active site: T259 (= T258), T411 (= T410), E412 (= E411), N516 (= N515), R521 (= R520), K604 (= K603)
- binding adenosine monophosphate: G382 (= G381), E383 (= E382), P384 (= P383), T407 (= T406), W408 (= W407), W409 (= W408), Q410 (= Q409), T411 (= T410), D495 (= D494), I507 (= I506), R510 (= R509), N516 (= N515), R521 (= R520)
- binding coenzyme a: F158 (= F160), R186 (= R188), W304 (= W303), T306 (= T305), P329 (= P328), A352 (= A351), A355 (= A354), S518 (= S517), R579 (= R578), P584 (= P583)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
63% identity, 97% coverage: 17:640/642 of query aligns to 16:633/634 of 1pg3A
- active site: T260 (= T258), T412 (= T410), E413 (= E411), N517 (= N515), R522 (= R520), K605 (= K603)
- binding coenzyme a: F159 (= F160), G160 (= G161), R187 (= R188), R190 (≠ K191), A301 (= A299), T307 (= T305), P330 (= P328), A356 (= A354), S519 (= S517), R580 (= R578), P585 (= P583)
- binding magnesium ion: V533 (= V531), H535 (= H533), I538 (≠ V536)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G381), E384 (= E382), P385 (= P383), T408 (= T406), W409 (= W407), W410 (= W408), Q411 (= Q409), T412 (= T410), D496 (= D494), R511 (= R509), R522 (= R520)
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)
53% identity, 97% coverage: 19:639/642 of query aligns to 45:696/701 of Q9QXG4