SitesBLAST
Comparing WP_100847194.1 NCBI__GCF_003031005.1:WP_100847194.1 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)
66% identity, 98% coverage: 15:645/645 of query aligns to 14:645/648 of Q89WV5
- G263 (= G263) mutation to I: Loss of activity.
- G266 (= G266) mutation to I: Great decrease in activity.
- K269 (= K269) mutation to G: Great decrease in activity.
- E414 (= E414) 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)
61% identity, 97% coverage: 19:642/645 of query aligns to 19:645/652 of P27550
- K609 (= K606) 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)
60% identity, 97% coverage: 19:642/645 of query aligns to 19:645/652 of Q8ZKF6
- R194 (≠ K193) 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 (= T308) binding CoA
- N335 (≠ S332) binding CoA
- A357 (= A354) 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 (= D514) 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 (= S520) binding CoA
- G524 (= G521) 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 (= R523) 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 (≠ S581) 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 (= K606) 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)
60% identity, 97% coverage: 19:642/645 of query aligns to 15:638/640 of 5jrhA
- active site: T260 (= T261), T412 (= T413), E413 (= E414), N517 (= N518), R522 (= R523), K605 (= K606)
- binding (r,r)-2,3-butanediol: W93 (= W96), E140 (= E143), G169 (≠ D172), K266 (= K267), P267 (= P268)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G384), E384 (= E385), P385 (= P386), T408 (= T409), W409 (= W410), W410 (= W411), Q411 (= Q412), T412 (= T413), D496 (= D497), I508 (= I509), N517 (= N518), R522 (= R523)
- binding coenzyme a: F159 (= F162), G160 (= G163), G161 (= G164), R187 (= R190), S519 (= S520), R580 (≠ S581), P585 (≠ S586)
- binding magnesium ion: V533 (= V534), H535 (= H536), I538 (= I539)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
60% identity, 97% coverage: 19:642/645 of query aligns to 15:639/641 of 2p20A
- active site: T260 (= T261), T412 (= T413), E413 (= E414), N517 (= N518), R522 (= R523), K605 (= K606)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G384), E384 (= E385), P385 (= P386), T408 (= T409), W409 (= W410), W410 (= W411), Q411 (= Q412), T412 (= T413), D496 (= D497), I508 (= I509), R511 (= R512), R522 (= R523)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
60% identity, 97% coverage: 19:642/645 of query aligns to 14:635/637 of 2p2fA
- active site: T259 (= T261), T411 (= T413), E412 (= E414), N516 (= N518), R521 (= R523), K604 (= K606)
- binding adenosine monophosphate: G382 (= G384), E383 (= E385), P384 (= P386), T407 (= T409), W408 (= W410), W409 (= W411), Q410 (= Q412), T411 (= T413), D495 (= D497), I507 (= I509), R510 (= R512), N516 (= N518), R521 (= R523)
- binding coenzyme a: F158 (= F162), R186 (= R190), W304 (= W306), T306 (= T308), P329 (= P331), A352 (= A354), A355 (= A357), S518 (= S520), R579 (≠ S581), P584 (≠ S586)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
59% identity, 97% coverage: 19:642/645 of query aligns to 15:632/634 of 1pg3A
- active site: T260 (= T261), T412 (= T413), E413 (= E414), N517 (= N518), R522 (= R523), K605 (= K606)
- binding coenzyme a: F159 (= F162), G160 (= G163), R187 (= R190), R190 (≠ K193), A301 (= A302), T307 (= T308), P330 (= P331), A356 (= A357), S519 (= S520), R580 (≠ S581), P585 (≠ S586)
- binding magnesium ion: V533 (= V534), H535 (= H536), I538 (= I539)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G384), E384 (= E385), P385 (= P386), T408 (= T409), W409 (= W410), W410 (= W411), Q411 (= Q412), T412 (= T413), D496 (= D497), R511 (= R512), R522 (= R523)
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)
54% identity, 98% coverage: 8:642/645 of query aligns to 31:696/701 of Q9NR19