SitesBLAST
Comparing WP_036835183.1 NCBI__GCF_000775615.1:WP_036835183.1 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)
39% identity, 95% coverage: 25:567/571 of query aligns to 63:630/630 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 (= T355), W417 (= W356), W418 (= W357), Q419 (≠ M358), T420 (= T359), D502 (= D439), R517 (= R454), K523 (≠ N460), R528 (= R465)
- binding magnesium ion: V539 (≠ I476), H541 (= H478)
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)
39% identity, 94% coverage: 33:571/571 of query aligns to 66:634/652 of P27550
- K609 (= K548) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
39% identity, 94% coverage: 33:571/571 of query aligns to 62:628/641 of 2p20A
- active site: T260 (= T214), T412 (= T359), E413 (= E360), N517 (= N460), R522 (= R465), K605 (= K548)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G333), E384 (= E334), P385 (= P335), T408 (= T355), W409 (= W356), W410 (= W357), Q411 (≠ M358), T412 (= T359), D496 (= D439), I508 (≠ F451), R511 (= R454), R522 (= R465)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
39% identity, 94% coverage: 33:571/571 of query aligns to 62:627/640 of 5jrhA
- active site: T260 (= T214), T412 (= T359), E413 (= E360), N517 (= N460), R522 (= R465), K605 (= K548)
- binding (r,r)-2,3-butanediol: W93 (≠ Y66), E140 (= E111), G169 (≠ D140), K266 (= K220), P267 (= P221)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G333), E384 (= E334), P385 (= P335), T408 (= T355), W409 (= W356), W410 (= W357), Q411 (≠ M358), T412 (= T359), D496 (= D439), I508 (≠ F451), N517 (= N460), R522 (= R465)
- binding coenzyme a: F159 (= F130), G160 (≠ E131), G161 (≠ A132), R187 (≠ E158), S519 (= S462), R580 (≠ K523), P585 (≠ A528)
- binding magnesium ion: V533 (≠ I476), H535 (= H478), I538 (≠ V481)
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)
39% identity, 94% coverage: 33:571/571 of query aligns to 66:634/652 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 (= D456) 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 (= S462) binding CoA
- G524 (= G463) 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 (= R465) 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 (≠ K523) 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 (= K548) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
39% identity, 94% coverage: 33:568/571 of query aligns to 61:620/637 of 2p2fA
- active site: T259 (= T214), T411 (= T359), E412 (= E360), N516 (= N460), R521 (= R465), K604 (= K548)
- binding adenosine monophosphate: G382 (= G333), E383 (= E334), P384 (= P335), T407 (= T355), W408 (= W356), W409 (= W357), Q410 (≠ M358), T411 (= T359), D495 (= D439), I507 (≠ F451), R510 (= R454), N516 (= N460), R521 (= R465)
- binding coenzyme a: F158 (= F130), R186 (≠ E158), W304 (= W258), T306 (= T260), P329 (≠ F283), A352 (= A303), A355 (= A306), S518 (= S462), R579 (≠ K523), P584 (≠ A528)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 92% coverage: 33:560/571 of query aligns to 62:617/634 of 1pg3A
- active site: T260 (= T214), T412 (= T359), E413 (= E360), N517 (= N460), R522 (= R465), K605 (= K548)
- binding coenzyme a: F159 (= F130), G160 (≠ E131), R187 (≠ E158), R190 (vs. gap), A301 (= A254), T307 (= T260), P330 (≠ F283), A356 (= A306), S519 (= S462), R580 (≠ K523), P585 (≠ A528)
- binding magnesium ion: V533 (≠ I476), H535 (= H478), I538 (≠ V481)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G333), E384 (= E334), P385 (= P335), T408 (= T355), W409 (= W356), W410 (= W357), Q411 (≠ M358), T412 (= T359), D496 (= D439), R511 (= R454), R522 (= R465)
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)
36% identity, 94% coverage: 33:571/571 of query aligns to 65:631/648 of Q89WV5