SitesBLAST
Comparing Dsui_2925 FitnessBrowser__PS:Dsui_2925 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
45% identity, 99% coverage: 3:628/630 of query aligns to 1:621/627 of 5gxdA
- active site: T238 (= T242), T390 (= T391), E391 (= E392), N498 (= N501), R503 (= R506), K587 (= K594)
- binding adenosine monophosphate: G364 (= G365), E365 (= E366), R366 (≠ P367), H386 (≠ N387), W387 (≠ Y388), W388 (= W389), Q389 (= Q390), T390 (= T391), D477 (= D480), I489 (= I492), R492 (= R495), N498 (= N501), R503 (= R506)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (≠ R168), R170 (≠ K171), S279 (= S283), K307 (≠ T311), P308 (= P312), A332 (= A335), T334 (= T337), A363 (= A364), A500 (= A503), H502 (= H505), K532 (= K535), R562 (≠ D569), P567 (≠ A574), V568 (≠ I575)
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)
41% identity, 99% coverage: 4:624/630 of query aligns to 24:641/652 of P27550
- K609 (= K594) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
40% identity, 99% coverage: 4:624/630 of query aligns to 20:635/641 of 2p20A
- active site: T260 (= T242), T412 (= T391), E413 (= E392), N517 (= N501), R522 (= R506), K605 (= K594)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G365), E384 (= E366), P385 (= P367), T408 (≠ N387), W409 (≠ Y388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D480), I508 (= I492), R511 (= R495), R522 (= R506)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
40% identity, 99% coverage: 4:624/630 of query aligns to 20:634/640 of 5jrhA
- active site: T260 (= T242), T412 (= T391), E413 (= E392), N517 (= N501), R522 (= R506), K605 (= K594)
- binding (r,r)-2,3-butanediol: W93 (≠ F74), E140 (= E121), G169 (≠ T150), K266 (= K248), P267 (= P249)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G365), E384 (= E366), P385 (= P367), T408 (≠ N387), W409 (≠ Y388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D480), I508 (= I492), N517 (= N501), R522 (= R506)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (= R168), S519 (≠ A503), R580 (≠ D569), P585 (≠ A574)
- binding magnesium ion: V533 (≠ Q517), H535 (= H519), I538 (≠ V522)
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)
40% identity, 99% coverage: 4:624/630 of query aligns to 24:641/652 of Q8ZKF6
- R194 (≠ K171) 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 (≠ V289) binding
- N335 (≠ I313) binding
- 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
- 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 (≠ D569) 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 (= K594) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
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, 99% coverage: 4:624/630 of query aligns to 23:638/648 of Q89WV5
- G263 (= G244) mutation to I: Loss of activity.
- G266 (= G247) mutation to I: Great decrease in activity.
- K269 (= K250) mutation to G: Great decrease in activity.
- E414 (= E392) mutation to Q: Great decrease in activity.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
40% identity, 99% coverage: 4:624/630 of query aligns to 19:631/637 of 2p2fA
- active site: T259 (= T242), T411 (= T391), E412 (= E392), N516 (= N501), R521 (= R506), K604 (= K594)
- binding adenosine monophosphate: G382 (= G365), E383 (= E366), P384 (= P367), T407 (≠ N387), W408 (≠ Y388), W409 (= W389), Q410 (= Q390), T411 (= T391), D495 (= D480), I507 (= I492), R510 (= R495), N516 (= N501), R521 (= R506)
- binding coenzyme a: F158 (= F140), R186 (= R168), W304 (= W287), T306 (≠ V289), P329 (= P312), A352 (= A335), A355 (= A338), S518 (≠ A503), R579 (≠ D569), P584 (≠ A574)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
40% identity, 96% coverage: 4:610/630 of query aligns to 20:623/634 of 1pg3A
- active site: T260 (= T242), T412 (= T391), E413 (= E392), N517 (= N501), R522 (= R506), K605 (= K594)
- binding coenzyme a: F159 (= F140), G160 (= G141), R187 (= R168), R190 (≠ K171), A301 (≠ S283), T307 (≠ V289), P330 (= P312), A356 (= A338), S519 (≠ A503), R580 (≠ D569), P585 (≠ A574)
- binding magnesium ion: V533 (≠ Q517), H535 (= H519), I538 (≠ V522)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G365), E384 (= E366), P385 (= P367), T408 (≠ N387), W409 (≠ Y388), W410 (= W389), Q411 (= Q390), T412 (= T391), D496 (= D480), R511 (= R495), R522 (= R506)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
39% identity, 98% coverage: 4:621/630 of query aligns to 3:615/615 of 1ry2A
- active site: T247 (= T242), T399 (= T391), N507 (= N501), K590 (= K594)
- binding adenosine monophosphate: G370 (= G365), E371 (= E366), P372 (= P367), T395 (≠ N387), Y396 (= Y388), W397 (= W389), Q398 (= Q390), T399 (= T391), D486 (= D480), I498 (= I492), R501 (= R495)
8w0dA Acetyl-coenzyme A synthetase 2
38% identity, 100% coverage: 1:630/630 of query aligns to 34:662/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G365), E399 (= E366), P400 (= P367), T423 (≠ N387), Y424 (= Y388), W425 (= W389), Q426 (= Q390), T427 (= T391), D513 (= D480), I525 (= I492), R528 (= R495), R539 (= R506)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
38% identity, 100% coverage: 1:630/630 of query aligns to 34:662/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G365), E399 (= E366), P400 (= P367), T423 (≠ N387), Y424 (= Y388), Q426 (= Q390), T427 (= T391), D513 (= D480), I525 (= I492), R528 (= R495), R539 (= R506)
- binding coenzyme a: F175 (= F140), R203 (= R168), R206 (≠ K171), G316 (≠ S283), H538 (= H505), R599 (≠ D569), F605 (≠ I575)
8w0cA Acetyl-coenzyme A synthetase 2
38% identity, 100% coverage: 1:630/630 of query aligns to 35:663/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G365), E400 (= E366), P401 (= P367), T424 (≠ N387), Y425 (= Y388), W426 (= W389), Q427 (= Q390), T428 (= T391), D514 (= D480), R529 (= R495), R540 (= R506)
8w0bA Acetyl-coenzyme A synthetase 2
38% identity, 100% coverage: 1:630/630 of query aligns to 35:663/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A364), G399 (= G365), E400 (= E366), P401 (= P367), T424 (≠ N387), Y425 (= Y388), W426 (= W389), Q427 (= Q390), T428 (= T391), D514 (= D480), I526 (= I492), R529 (= R495), R540 (= R506)
8w0jA Acetyl-coenzyme A synthetase 2
38% identity, 100% coverage: 1:630/630 of query aligns to 35:658/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G365), E400 (= E366), P401 (= P367), T424 (≠ N387), Y425 (= Y388), W426 (= W389), Q427 (= Q390), T428 (= T391), D514 (= D480), I526 (= I492), R529 (= R495), R540 (= R506)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
38% identity, 100% coverage: 1:630/630 of query aligns to 34:657/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P117), A176 (≠ G141), G177 (= G142), R203 (= R168), T208 (≠ V173), D317 (= D284), E342 (= E309), G343 (= G310), P345 (= P312), G398 (= G365), E399 (= E366), P400 (= P367), T423 (≠ N387), W425 (= W389), Q426 (= Q390), T427 (= T391), D513 (= D480), I525 (= I492), R528 (= R495), R539 (= R506)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
38% identity, 100% coverage: 1:630/630 of query aligns to 34:657/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G365), E399 (= E366), P400 (= P367), T423 (≠ N387), Y424 (= Y388), W425 (= W389), Q426 (= Q390), T427 (= T391), D513 (= D480), I525 (= I492), R528 (= R495), R539 (= R506)
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)
39% identity, 100% coverage: 1:628/630 of query aligns to 32:654/662 of P78773
- T596 (= T571) modified: Phosphothreonine
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
38% identity, 100% coverage: 1:630/630 of query aligns to 34:652/654 of 7kdsA
- active site: T275 (= T242), T427 (= T391), E428 (= E392), N534 (= N501), R539 (= R506), K620 (= K594)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V288), G398 (= G365), E399 (= E366), P400 (= P367), D422 (= D386), T423 (≠ N387), Y424 (= Y388), W425 (= W389), Q426 (= Q390), T427 (= T391), D513 (= D480), R528 (= R495), N534 (= N501), R539 (= R506)
P52910 Acetyl-coenzyme A synthetase 2; Acetate--CoA ligase 2; Acyl-activating enzyme 2; EC 6.2.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
37% identity, 100% coverage: 1:628/630 of query aligns to 37:673/683 of P52910
- K506 (≠ S468) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
39% identity, 99% coverage: 6:627/630 of query aligns to 27:650/651 of P9WQD1
- K617 (= K594) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
Query Sequence
>Dsui_2925 FitnessBrowser__PS:Dsui_2925
MTSYKEFHRRSIEQPDAFWSEQAQLIDWHKPFDQVCDYSRPPFAKWFVGGQTNLCYNAVD
RHAKTRPNDNALIFISTETDVEKVYSFAELQREVERMAAIYQSLGVKKGDRVLIYMPMIA
EACFAILACARIGAIHSVVFGGFASGSLATRIDDAKPVLIVSSDAGMRGGKAVPYKHLLD
DAINQAEHKPGKVLMVDRGLDKAFNKVEGRDVDYAALRAQFMDAQVPVTWVESSDPSYIL
YTSGTTGKPKGVQRDTGGYAVALASSIKHIYCGKPGETFFSTSDIGWVVGHSYIIYGPLI
GGMATIMYEGTPIRPDAGIWWQIVEKYKVNVMFSAPTAARVLKKHDPAFLHKYDLSSLKH
LFLAGEPLDQPTHEWIMGELKLPVIDNYWQTETGWPMLSTVRGVEDTKIKYGTPSFPVYG
YDVRIFREDGSECDANEKGILGVVPPLPPGCLTTVWGDDERFVNTYFSLFKEPLVYSSYD
WAIKDDEGYHFILGRTDDVINVAGHRLGTREIEEAVQGHPAVAEVAVVGVNDALKGQLPV
AFAVVKDASKIATPELVAALEKEVMKRVDETLGAIARPGRVYFISGLPKTRSGKLLRRSI
QALAEGRDPGDLTTIEDPTALEQIKAALSA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory