SitesBLAST
Comparing WP_084275418.1 NCBI__GCF_900176045.1:WP_084275418.1 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)
55% identity, 99% coverage: 6:649/650 of query aligns to 5:643/648 of Q89WV5
- G263 (= G264) mutation to I: Loss of activity.
- G266 (= G267) mutation to I: Great decrease in activity.
- K269 (= K270) mutation to G: Great decrease in activity.
- E414 (= E415) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
52% identity, 98% coverage: 12:650/650 of query aligns to 8:641/641 of 2p20A
- active site: T260 (= T262), T412 (= T414), E413 (= E415), N517 (= N523), R522 (= R528), K605 (= K613)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G385), E384 (= E386), P385 (= P387), T408 (= T410), W409 (= W411), W410 (= W412), Q411 (= Q413), T412 (= T414), D496 (= D502), I508 (= I514), R511 (= R517), R522 (= R528)
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, 98% coverage: 12:646/650 of query aligns to 12:643/652 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 (= T309) binding CoA
- N335 (≠ V333) binding CoA
- A357 (= A355) 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 (= D519) 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 (= S525) binding CoA
- G524 (= G526) 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 (= R528) 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 (≠ T588) 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 (= K613) 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)
52% identity, 98% coverage: 12:646/650 of query aligns to 8:636/640 of 5jrhA
- active site: T260 (= T262), T412 (= T414), E413 (= E415), N517 (= N523), R522 (= R528), K605 (= K613)
- binding (r,r)-2,3-butanediol: W93 (= W96), E140 (= E143), G169 (≠ D172), K266 (= K268), P267 (= P269)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G385), E384 (= E386), P385 (= P387), T408 (= T410), W409 (= W411), W410 (= W412), Q411 (= Q413), T412 (= T414), D496 (= D502), I508 (= I514), N517 (= N523), R522 (= R528)
- binding coenzyme a: F159 (= F162), G160 (= G163), G161 (= G164), R187 (= R190), S519 (= S525), R580 (≠ T588), P585 (= P593)
- binding magnesium ion: V533 (≠ G539), H535 (= H541), I538 (≠ V544)
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, 98% coverage: 12:646/650 of query aligns to 12:643/652 of P27550
- K609 (= K613) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
52% identity, 98% coverage: 12:650/650 of query aligns to 7:637/637 of 2p2fA
- active site: T259 (= T262), T411 (= T414), E412 (= E415), N516 (= N523), R521 (= R528), K604 (= K613)
- binding adenosine monophosphate: G382 (= G385), E383 (= E386), P384 (= P387), T407 (= T410), W408 (= W411), W409 (= W412), Q410 (= Q413), T411 (= T414), D495 (= D502), I507 (= I514), R510 (= R517), N516 (= N523), R521 (= R528)
- binding coenzyme a: F158 (= F162), R186 (= R190), W304 (= W307), T306 (= T309), P329 (= P332), A352 (= A355), A355 (= A358), S518 (= S525), R579 (≠ T588), P584 (= P593)
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)
53% identity, 95% coverage: 27:644/650 of query aligns to 27:647/651 of P9WQD1
- K617 (= K613) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
52% identity, 98% coverage: 12:646/650 of query aligns to 8:630/634 of 1pg3A