SitesBLAST
Comparing Ac3H11_4867 FitnessBrowser__acidovorax_3H11:Ac3H11_4867 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4wd1A Acetoacetyl-coa synthetase from streptomyces lividans (see paper)
47% identity, 96% coverage: 25:704/710 of query aligns to 1:646/646 of 4wd1A
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)
29% identity, 86% coverage: 54:663/710 of query aligns to 28:617/651 of P9WQD1
- K617 (= K663) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
Q9NUB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see 3 papers)
26% identity, 89% coverage: 50:679/710 of query aligns to 57:658/689 of Q9NUB1
- V488 (= V492) to M: in dbSNP:rs6050249
- K642 (= K663) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
Q99NB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
26% identity, 88% coverage: 50:673/710 of query aligns to 50:645/682 of Q99NB1
- K635 (= K663) modified: N6-acetyllysine
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)
26% identity, 91% coverage: 51:694/710 of query aligns to 24:639/652 of P27550
- K609 (= K663) 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)
25% identity, 91% coverage: 49:694/710 of query aligns to 22:639/652 of Q8ZKF6
- R194 (= R220) 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 (≠ M343) binding
- N335 (≠ D369) binding
- A357 (≠ G391) 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 (= D571) 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 (≠ H577) binding
- G524 (= G578) 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 (= R580) 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 (= R638) binding ; 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 (= K663) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
26% identity, 91% coverage: 52:698/710 of query aligns to 37:655/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G421), E399 (≠ S422), P400 (= P423), D422 (= D443), T423 (≠ I444), W424 (= W445), W425 (= W446), Q426 (≠ N447), T427 (≠ N448), D511 (= D554), I523 (= I566), R526 (= R569), N532 (= N575), R537 (= R580)
- binding coenzyme a: F171 (≠ A189), G172 (≠ P190), G173 (≠ D191), R199 (≠ Y217), K202 (≠ R220), I204 (≠ H222), D317 (≠ S338), R595 (= R638), P600 (= P643)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
25% identity, 91% coverage: 49:694/710 of query aligns to 18:632/640 of 5jrhA