SitesBLAST
Comparing WP_012277976.1 NCBI__GCF_000019185.1:WP_012277976.1 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
60% identity, 98% coverage: 6:629/634 of query aligns to 3:626/627 of 5gxdA
- active site: T238 (= T241), T390 (= T393), E391 (= E394), N498 (= N501), R503 (= R506), K587 (= K590)
- binding adenosine monophosphate: G364 (= G367), E365 (= E368), R366 (= R369), H386 (= H389), W387 (= W390), W388 (= W391), Q389 (= Q392), T390 (= T393), D477 (= D480), I489 (= I492), R492 (= R495), N498 (= N501), R503 (= R506)
- binding coenzyme a: F139 (= F142), G140 (= G143), G141 (= G144), E167 (= E170), R170 (≠ G173), S279 (= S282), K307 (= K310), P308 (= P311), A332 (= A335), T334 (= T337), A363 (= A366), A500 (= A503), H502 (= H505), K532 (= K535), R562 (= R565), P567 (= P570), V568 (= V571)
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)
41% identity, 98% coverage: 4:622/634 of query aligns to 22:641/648 of Q89WV5
- G263 (= G243) mutation to I: Loss of activity.
- G266 (= G246) mutation to I: Great decrease in activity.
- K269 (= K249) mutation to G: Great decrease in activity.
- E414 (= E394) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
41% identity, 96% coverage: 9:618/634 of query aligns to 24:633/641 of 2p20A
- active site: T260 (= T241), T412 (= T393), E413 (= E394), N517 (= N501), R522 (= R506), K605 (= K590)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G367), E384 (= E368), P385 (≠ R369), T408 (≠ H389), W409 (= W390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D480), I508 (= I492), R511 (= R495), R522 (= R506)
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)
41% identity, 96% coverage: 9:618/634 of query aligns to 28:639/652 of Q8ZKF6
- R194 (≠ G173) 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 (≠ V288) binding CoA
- N335 (≠ G313) binding CoA
- A357 (= A335) 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 (= D497) 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 (≠ A503) binding CoA
- G524 (= G504) 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 (= R506) 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 (= R565) 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 (= K590) 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)
41% identity, 96% coverage: 9:618/634 of query aligns to 23:629/637 of 2p2fA
- active site: T259 (= T241), T411 (= T393), E412 (= E394), N516 (= N501), R521 (= R506), K604 (= K590)
- binding adenosine monophosphate: G382 (= G367), E383 (= E368), P384 (≠ R369), T407 (≠ H389), W408 (= W390), W409 (= W391), Q410 (= Q392), T411 (= T393), D495 (= D480), I507 (= I492), R510 (= R495), N516 (= N501), R521 (= R506)
- binding coenzyme a: F158 (= F142), R186 (≠ E170), W304 (= W286), T306 (≠ V288), P329 (= P311), A352 (= A335), A355 (= A338), S518 (≠ A503), R579 (= R565), P584 (= P570)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
41% identity, 96% coverage: 9:618/634 of query aligns to 24:632/640 of 5jrhA
- active site: T260 (= T241), T412 (= T393), E413 (= E394), N517 (= N501), R522 (= R506), K605 (= K590)
- binding (r,r)-2,3-butanediol: W93 (≠ Y76), E140 (= E123), G169 (≠ T152), K266 (≠ Q247), P267 (= P248)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G367), E384 (= E368), P385 (≠ R369), T408 (≠ H389), W409 (= W390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D480), I508 (= I492), N517 (= N501), R522 (= R506)
- binding coenzyme a: F159 (= F142), G160 (= G143), G161 (= G144), R187 (≠ E170), S519 (≠ A503), R580 (= R565), P585 (= P570)
- binding magnesium ion: V533 (≠ C517), H535 (= H519), I538 (≠ V522)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
41% identity, 93% coverage: 9:600/634 of query aligns to 24:615/634 of 1pg3A
- active site: T260 (= T241), T412 (= T393), E413 (= E394), N517 (= N501), R522 (= R506), K605 (= K590)
- binding coenzyme a: F159 (= F142), G160 (= G143), R187 (≠ E170), R190 (≠ G173), A301 (≠ S282), T307 (≠ V288), P330 (= P311), A356 (= A338), S519 (≠ A503), R580 (= R565), P585 (= P570)
- binding magnesium ion: V533 (≠ C517), H535 (= H519), I538 (≠ V522)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G367), E384 (= E368), P385 (≠ R369), T408 (≠ H389), W409 (= W390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D480), R511 (= R495), R522 (= R506)
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)
41% identity, 98% coverage: 3:621/634 of query aligns to 23:648/651 of P9WQD1