SitesBLAST
Comparing WP_089322819.1 NCBI__GCF_900188395.1:WP_089322819.1 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)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
54% identity, 97% coverage: 15:627/631 of query aligns to 6:630/630 of 8rplB
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: G391 (= G388), E392 (= E389), P393 (= P390), T416 (= T413), W417 (= W414), W418 (= W415), Q419 (= Q416), T420 (= T417), D502 (= D499), R517 (= R514), K523 (≠ N520), R528 (= R525)
- binding magnesium ion: V539 (= V536), H541 (= H538)
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)
50% identity, 97% coverage: 18:631/631 of query aligns to 14:640/651 of P9WQD1
- K617 (= K608) 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)
50% identity, 96% coverage: 27:631/631 of query aligns to 16:627/640 of 5jrhA
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N520), R522 (= R525), K605 (= K608)
- binding (r,r)-2,3-butanediol: W93 (= W101), E140 (= E147), G169 (≠ H176), K266 (= K271), P267 (= P272)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D499), I508 (= I511), N517 (= N520), R522 (= R525)
- binding coenzyme a: F159 (≠ Y166), G160 (≠ A167), G161 (= G168), R187 (= R194), S519 (= S522), R580 (= R583), P585 (≠ A588)
- binding magnesium ion: V533 (= V536), H535 (= H538), I538 (≠ V541)
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)
49% identity, 97% coverage: 19:631/631 of query aligns to 9:631/648 of Q89WV5
- G263 (= G267) mutation to I: Loss of activity.
- G266 (= G270) mutation to I: Great decrease in activity.
- K269 (= K273) mutation to G: Great decrease in activity.
- E414 (= E418) 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)
50% identity, 96% coverage: 27:631/631 of query aligns to 20:634/652 of Q8ZKF6
- R194 (= R197) 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 (= T312) binding CoA
- N335 (= N336) binding CoA
- A357 (= A358) 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 (= D516) 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 (= S522) binding CoA
- G524 (= G523) 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 (= R525) 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 (= R583) 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 (= K608) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
50% identity, 96% coverage: 27:631/631 of query aligns to 16:628/641 of 2p20A
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N520), R522 (= R525), K605 (= K608)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D499), I508 (= I511), R511 (= R514), R522 (= R525)
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)
50% identity, 96% coverage: 27:631/631 of query aligns to 20:634/652 of P27550
- K609 (= K608) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
50% identity, 96% coverage: 27:629/631 of query aligns to 15:631/637 of 2p2fA