SitesBLAST
Comparing 642683066 IMG__ChlphaBS1_FD:642683066 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)
Q9NR19 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see paper)
50% identity, 95% coverage: 26:656/663 of query aligns to 27:692/701 of Q9NR19
- T363 (= T327) mutation to A: Loss of catalytic activity but no effect on its nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- 656:668 (vs. 620:632, 92% identical) Nuclear localization signal
- S659 (= S623) modified: Phosphoserine; by AMPK; mutation to A: No effect on catalytic activity. Loss of AMPK-mediated phosphorylation, interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- RR 664:665 (= RR 628:629) mutation to AA: No effect on catalytic activity. Loss of interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
Sites not aligning to the query:
- 1:107 Interaction with TFEB
Q9QXG4 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
50% identity, 95% coverage: 26:656/663 of query aligns to 27:692/701 of Q9QXG4
- K661 (= K625) modified: N6-acetyllysine
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)
52% identity, 94% coverage: 31:656/663 of query aligns to 9:638/648 of Q89WV5
- G263 (= G282) mutation to I: Loss of activity.
- G266 (= G285) mutation to I: Great decrease in activity.
- K269 (= K288) mutation to G: Great decrease in activity.
- E414 (= E433) mutation to Q: Great decrease in activity.
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)
52% identity, 96% coverage: 22:656/663 of query aligns to 1:641/652 of P27550
- K609 (= K625) 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)
51% identity, 96% coverage: 22:656/663 of query aligns to 1:641/652 of Q8ZKF6
- R194 (≠ K212) 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 (= T327) binding CoA
- N335 (= N351) binding CoA
- A357 (= A373) 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 (= D533) 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 (= S539) binding CoA
- G524 (= G540) 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 (= R542) 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 (≠ A600) 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 (= K625) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
53% identity, 92% coverage: 44:656/663 of query aligns to 18:635/641 of 2p20A
- active site: T260 (= T280), T412 (= T432), E413 (= E433), N517 (= N537), R522 (= R542), K605 (= K625)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G403), E384 (= E404), P385 (= P405), T408 (= T428), W409 (= W429), W410 (= W430), Q411 (= Q431), T412 (= T432), D496 (= D516), I508 (= I528), R511 (= R531), R522 (= R542)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
53% identity, 92% coverage: 44:656/663 of query aligns to 18:634/640 of 5jrhA
- active site: T260 (= T280), T412 (= T432), E413 (= E433), N517 (= N537), R522 (= R542), K605 (= K625)
- binding (r,r)-2,3-butanediol: W93 (= W116), E140 (= E162), G169 (≠ E191), K266 (= K286), P267 (= P287)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G403), E384 (= E404), P385 (= P405), T408 (= T428), W409 (= W429), W410 (= W430), Q411 (= Q431), T412 (= T432), D496 (= D516), I508 (= I528), N517 (= N537), R522 (= R542)
- binding coenzyme a: F159 (= F181), G160 (≠ A182), G161 (= G183), R187 (= R209), S519 (= S539), R580 (≠ A600), P585 (= P605)
- binding magnesium ion: V533 (= V553), H535 (= H555), I538 (≠ V558)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
53% identity, 92% coverage: 44:656/663 of query aligns to 17:631/637 of 2p2fA