SitesBLAST
Comparing WP_033099083.1 NCBI__GCF_000763315.1:WP_033099083.1 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)
40% identity, 97% coverage: 13:568/572 of query aligns to 50:630/630 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 (= G333), E392 (= E334), P393 (= P335), T416 (≠ N355), W417 (= W356), W418 (= W357), Q419 (≠ M358), T420 (= T359), D502 (= D440), R517 (= R455), K523 (≠ N461), R528 (= R466)
- binding magnesium ion: V539 (= V477), H541 (= H479)
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)
38% identity, 94% coverage: 35:572/572 of query aligns to 67:628/652 of Q8ZKF6
- R194 (vs. gap) 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 (= T260) binding CoA
- N335 (vs. gap) binding CoA
- A357 (= A303) 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 (= D457) 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 (= S463) binding CoA
- G524 (= G464) 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 (= R466) 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 (≠ K524) 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 (= K549) 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)
39% identity, 94% coverage: 35:572/572 of query aligns to 63:627/640 of 5jrhA
- active site: T260 (= T214), T412 (= T359), E413 (= E360), N517 (= N461), R522 (= R466), K605 (= K549)
- binding (r,r)-2,3-butanediol: W93 (≠ Y66), E140 (≠ D111), G169 (≠ D140), K266 (= K220), P267 (= P221)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G333), E384 (= E334), P385 (= P335), T408 (≠ N355), W409 (= W356), W410 (= W357), Q411 (≠ M358), T412 (= T359), D496 (= D440), I508 (≠ F452), N517 (= N461), R522 (= R466)
- binding coenzyme a: F159 (= F130), G160 (≠ E131), G161 (≠ A132), R187 (vs. gap), S519 (= S463), R580 (≠ K524), P585 (≠ A529)
- binding magnesium ion: V533 (= V477), H535 (= H479), I538 (≠ V482)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
38% identity, 94% coverage: 35:572/572 of query aligns to 63:628/641 of 2p20A
- active site: T260 (= T214), T412 (= T359), E413 (= E360), N517 (= N461), R522 (= R466), K605 (= K549)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G333), E384 (= E334), P385 (= P335), T408 (≠ N355), W409 (= W356), W410 (= W357), Q411 (≠ M358), T412 (= T359), D496 (= D440), I508 (≠ F452), R511 (= R455), R522 (= R466)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
38% identity, 94% coverage: 35:569/572 of query aligns to 62:620/637 of 2p2fA
- active site: T259 (= T214), T411 (= T359), E412 (= E360), N516 (= N461), R521 (= R466), K604 (= K549)
- binding adenosine monophosphate: G382 (= G333), E383 (= E334), P384 (= P335), T407 (≠ N355), W408 (= W356), W409 (= W357), Q410 (≠ M358), T411 (= T359), D495 (= D440), I507 (≠ F452), R510 (= R455), N516 (= N461), R521 (= R466)
- binding coenzyme a: F158 (= F130), R186 (vs. gap), W304 (= W258), T306 (= T260), P329 (≠ F283), A352 (= A303), A355 (= A306), S518 (= S463), R579 (≠ K524), P584 (≠ A529)
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)
38% identity, 94% coverage: 34:572/572 of query aligns to 65:631/648 of Q89WV5
- G263 (= G216) mutation to I: Loss of activity.
- G266 (= G219) mutation to I: Great decrease in activity.
- K269 (= K222) mutation to G: Great decrease in activity.
- E414 (= E360) mutation to Q: Great decrease in activity.
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
38% identity, 93% coverage: 35:568/572 of query aligns to 63:620/634 of 1pg3A
- active site: T260 (= T214), T412 (= T359), E413 (= E360), N517 (= N461), R522 (= R466), K605 (= K549)
- binding coenzyme a: F159 (= F130), G160 (≠ E131), R187 (vs. gap), R190 (vs. gap), A301 (≠ V254), T307 (= T260), P330 (≠ F283), A356 (= A306), S519 (= S463), R580 (≠ K524), P585 (≠ A529)
- binding magnesium ion: V533 (= V477), H535 (= H479), I538 (≠ V482)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G333), E384 (= E334), P385 (= P335), T408 (≠ N355), W409 (= W356), W410 (= W357), Q411 (≠ M358), T412 (= T359), D496 (= D440), R511 (= R455), R522 (= R466)
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)
38% identity, 94% coverage: 37:572/572 of query aligns to 67:640/651 of P9WQD1