SitesBLAST
Comparing AZOBR_RS06340 FitnessBrowser__azobra:AZOBR_RS06340 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
69% identity, 98% coverage: 9:633/640 of query aligns to 2:626/627 of 5gxdA
- active site: T238 (= T245), T390 (= T397), E391 (= E398), N498 (= N505), R503 (= R510), K587 (= K594)
- binding adenosine monophosphate: G364 (= G371), E365 (= E372), R366 (= R373), H386 (= H393), W387 (= W394), W388 (= W395), Q389 (= Q396), T390 (= T397), D477 (= D484), I489 (= I496), R492 (= R499), N498 (= N505), R503 (= R510)
- binding coenzyme a: F139 (= F146), G140 (= G147), G141 (= G148), E167 (= E174), R170 (= R177), S279 (= S286), K307 (= K314), P308 (= P315), A332 (= A339), T334 (= T341), A363 (= A370), A500 (= A507), H502 (= H509), K532 (= K539), R562 (= R569), P567 (= P574), V568 (= V575)
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)
42% identity, 97% coverage: 8:630/640 of query aligns to 22:644/648 of Q89WV5
- G263 (= G247) mutation to I: Loss of activity.
- G266 (= G250) mutation to I: Great decrease in activity.
- K269 (= K253) mutation to G: Great decrease in activity.
- E414 (= E398) 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)
40% identity, 98% coverage: 7:631/640 of query aligns to 22:648/652 of Q8ZKF6
- R194 (= R177) 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 (≠ V292) binding CoA
- N335 (≠ G317) binding CoA
- A357 (= A339) 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 (= D501) 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 (≠ A507) binding CoA
- G524 (= G508) 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 (= R510) 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 (= R569) 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 (= K594) 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)
40% identity, 98% coverage: 7:630/640 of query aligns to 18:640/640 of 5jrhA
- active site: T260 (= T245), T412 (= T397), E413 (= E398), N517 (= N505), R522 (= R510), K605 (= K594)
- binding (r,r)-2,3-butanediol: W93 (≠ Y80), E140 (≠ Q127), G169 (≠ T156), K266 (≠ Q251), P267 (= P252)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G371), E384 (= E372), P385 (≠ R373), T408 (≠ H393), W409 (= W394), W410 (= W395), Q411 (= Q396), T412 (= T397), D496 (= D484), I508 (= I496), N517 (= N505), R522 (= R510)
- binding coenzyme a: F159 (= F146), G160 (= G147), G161 (= G148), R187 (≠ E174), S519 (≠ A507), R580 (= R569), P585 (= P574)
- binding magnesium ion: V533 (≠ A521), H535 (= H523), I538 (≠ V526)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
40% identity, 98% coverage: 7:630/640 of query aligns to 17:637/637 of 2p2fA
- active site: T259 (= T245), T411 (= T397), E412 (= E398), N516 (= N505), R521 (= R510), K604 (= K594)
- binding adenosine monophosphate: G382 (= G371), E383 (= E372), P384 (≠ R373), T407 (≠ H393), W408 (= W394), W409 (= W395), Q410 (= Q396), T411 (= T397), D495 (= D484), I507 (= I496), R510 (= R499), N516 (= N505), R521 (= R510)
- binding coenzyme a: F158 (= F146), R186 (≠ E174), W304 (= W290), T306 (≠ V292), P329 (= P315), A352 (= A339), A355 (= A342), S518 (≠ A507), R579 (= R569), P584 (= P574)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
40% identity, 98% coverage: 7:630/640 of query aligns to 18:641/641 of 2p20A
- active site: T260 (= T245), T412 (= T397), E413 (= E398), N517 (= N505), R522 (= R510), K605 (= K594)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G371), E384 (= E372), P385 (≠ R373), T408 (≠ H393), W409 (= W394), W410 (= W395), Q411 (= Q396), T412 (= T397), D496 (= D484), I508 (= I496), R511 (= R499), R522 (= R510)
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)
38% identity, 98% coverage: 8:631/640 of query aligns to 23:648/652 of P27550
- K609 (= K594) modified: N6-acetyllysine; by autocatalysis
P78773 Probable acetyl-coenzyme A synthetase; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
40% identity, 98% coverage: 4:629/640 of query aligns to 30:655/662 of P78773