SitesBLAST
Comparing Pf6N2E2_2042 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2042 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)
42% identity, 98% coverage: 5:643/651 of query aligns to 4:632/646 of 4wd1A
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)
27% identity, 94% coverage: 32:643/651 of query aligns to 31:650/662 of P78773
- T596 (≠ N590) modified: Phosphothreonine
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
28% identity, 88% coverage: 73:646/651 of query aligns to 79:666/668 of 7l4gB
- active site: T280 (≠ S272), T432 (= T421), E433 (≠ D422), N539 (= N526), R544 (= R531), K631 (= K613)
- 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: W325 (= W317), G403 (= G393), E404 (≠ S394), P405 (≠ A395), T428 (≠ M417), Y429 (≠ S418), W430 (≠ G419), M431 (≠ G420), T432 (= T421), D518 (= D505), I530 (= I517), R533 (= R520)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
28% identity, 88% coverage: 73:646/651 of query aligns to 79:666/668 of 5u29A
- active site: T280 (≠ S272), T432 (= T421), E433 (≠ D422), N539 (= N526), R544 (= R531), K631 (= K613)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W317), G403 (= G393), E404 (≠ S394), P405 (≠ A395), T428 (≠ M417), Y429 (≠ S418), W430 (≠ G419), M431 (≠ G420), T432 (= T421), D518 (= D505), I530 (= I517), R533 (= R520)
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, 94% coverage: 36:648/651 of query aligns to 24:646/652 of P27550
- K609 (= K613) modified: N6-acetyllysine; by autocatalysis
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
25% identity, 97% coverage: 12:641/651 of query aligns to 13:644/654 of 7kdsA
- active site: T275 (≠ S272), T427 (≠ M417), E428 (≠ S418), N534 (= N526), R539 (= R531), K620 (= K613)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ M318), G398 (= G393), E399 (≠ S394), P400 (≠ A395), D422 (vs. gap), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (vs. gap), T427 (≠ M417), D513 (= D505), R528 (= R520), N534 (= N526), R539 (= R531)
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, 97% coverage: 13:643/651 of query aligns to 1:641/652 of Q8ZKF6
- R194 (≠ K201) 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 (≠ M319) binding
- N335 (≠ F341) binding
- A357 (≠ S363) 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 (= D522) 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 (≠ G528) binding
- G524 (= G529) 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 (= R531) 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 (= R588) 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 (= K613) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
26% identity, 93% coverage: 36:643/651 of query aligns to 20:635/641 of 2p20A