SitesBLAST
Comparing Ac3H11_2208 FitnessBrowser__acidovorax_3H11:Ac3H11_2208 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: 6:633/633 of query aligns to 1:622/627 of 5gxdA
- active site: T238 (= T244), T390 (= T393), E391 (= E394), N498 (= N505), R503 (= R510), K587 (= K598)
- binding adenosine monophosphate: G364 (= G367), E365 (= E368), R366 (≠ P369), H386 (≠ N389), W387 (≠ Y390), W388 (= W391), Q389 (= Q392), T390 (= T393), D477 (= D484), I489 (= I496), R492 (= R499), N498 (= N505), R503 (= R510)
- binding coenzyme a: F139 (= F143), G140 (= G144), G141 (= G145), E167 (≠ R171), R170 (≠ K174), S279 (= S285), K307 (≠ L313), P308 (= P314), A332 (= A337), T334 (= T339), A363 (= A366), A500 (= A507), H502 (= H509), K532 (= K539), R562 (≠ D573), P567 (≠ A578), V568 (= V579)
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)
40% identity, 99% coverage: 4:628/633 of query aligns to 20:638/648 of Q89WV5
- G263 (= G246) mutation to I: Loss of activity.
- G266 (= G249) mutation to I: Great decrease in activity.
- K269 (= K252) mutation to G: Great decrease in activity.
- E414 (= E394) mutation to Q: Great decrease in activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
40% identity, 99% coverage: 7:630/633 of query aligns to 20:636/640 of 5jrhA
- active site: T260 (= T244), T412 (= T393), E413 (= E394), N517 (= N505), R522 (= R510), K605 (= K598)
- binding (r,r)-2,3-butanediol: W93 (≠ A77), E140 (= E124), G169 (≠ S153), K266 (= K250), P267 (= P251)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G367), E384 (= E368), P385 (= P369), T408 (≠ N389), W409 (≠ Y390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D484), I508 (= I496), N517 (= N505), R522 (= R510)
- binding coenzyme a: F159 (= F143), G160 (= G144), G161 (= G145), R187 (= R171), S519 (≠ A507), R580 (≠ D573), P585 (≠ A578)
- binding magnesium ion: V533 (≠ A521), H535 (= H523), I538 (= I526)
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, 99% coverage: 7:630/633 of query aligns to 24:643/652 of Q8ZKF6
- R194 (≠ K174) 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 (≠ V291) binding
- N335 (≠ I315) binding
- A357 (= A337) 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 (= D501) 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 (≠ A507) binding
- G524 (= G508) 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 (= R510) 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 (≠ D573) 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 (= K598) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
39% identity, 99% coverage: 7:630/633 of query aligns to 20:637/641 of 2p20A
- active site: T260 (= T244), T412 (= T393), E413 (= E394), N517 (= N505), R522 (= R510), K605 (= K598)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G367), E384 (= E368), P385 (= P369), T408 (≠ N389), W409 (≠ Y390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D484), I508 (= I496), R511 (= R499), R522 (= R510)
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, 99% coverage: 7:630/633 of query aligns to 24:643/652 of P27550
- K609 (= K598) modified: N6-acetyllysine; by autocatalysis
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)
38% identity, 99% coverage: 1:628/633 of query aligns to 34:669/683 of P52910
- K506 (= K472) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
39% identity, 99% coverage: 7:630/633 of query aligns to 19:633/637 of 2p2fA
- active site: T259 (= T244), T411 (= T393), E412 (= E394), N516 (= N505), R521 (= R510), K604 (= K598)
- binding adenosine monophosphate: G382 (= G367), E383 (= E368), P384 (= P369), T407 (≠ N389), W408 (≠ Y390), W409 (= W391), Q410 (= Q392), T411 (= T393), D495 (= D484), I507 (= I496), R510 (= R499), N516 (= N505), R521 (= R510)
- binding coenzyme a: F158 (= F143), R186 (= R171), W304 (= W289), T306 (≠ V291), P329 (= P314), A352 (= A337), A355 (= A340), S518 (≠ A507), R579 (≠ D573), P584 (≠ A578)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 99% coverage: 7:630/633 of query aligns to 20:630/634 of 1pg3A
- active site: T260 (= T244), T412 (= T393), E413 (= E394), N517 (= N505), R522 (= R510), K605 (= K598)
- binding coenzyme a: F159 (= F143), G160 (= G144), R187 (= R171), R190 (≠ K174), A301 (≠ S285), T307 (≠ V291), P330 (= P314), A356 (= A340), S519 (≠ A507), R580 (≠ D573), P585 (≠ A578)
- binding magnesium ion: V533 (≠ A521), H535 (= H523), I538 (= I526)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G367), E384 (= E368), P385 (= P369), T408 (≠ N389), W409 (≠ Y390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D484), R511 (= R499), R522 (= R510)
8w0dA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:633/633 of query aligns to 35:661/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G367), E399 (= E368), P400 (= P369), T423 (≠ N389), Y424 (= Y390), W425 (= W391), Q426 (= Q392), T427 (= T393), D513 (= D484), I525 (= I496), R528 (= R499), R539 (= R510)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
38% identity, 99% coverage: 5:633/633 of query aligns to 35:661/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G367), E399 (= E368), P400 (= P369), T423 (≠ N389), Y424 (= Y390), Q426 (= Q392), T427 (= T393), D513 (= D484), I525 (= I496), R528 (= R499), R539 (= R510)
- binding coenzyme a: F175 (= F143), R203 (= R171), R206 (≠ K174), G316 (≠ S285), H538 (= H509), R599 (≠ D573), F605 (≠ V579)
8w0cA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:633/633 of query aligns to 36:662/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G367), E400 (= E368), P401 (= P369), T424 (≠ N389), Y425 (= Y390), W426 (= W391), Q427 (= Q392), T428 (= T393), D514 (= D484), R529 (= R499), R540 (= R510)
8w0bA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:633/633 of query aligns to 36:662/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A366), G399 (= G367), E400 (= E368), P401 (= P369), T424 (≠ N389), Y425 (= Y390), W426 (= W391), Q427 (= Q392), T428 (= T393), D514 (= D484), I526 (= I496), R529 (= R499), R540 (= R510)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
38% identity, 99% coverage: 5:633/633 of query aligns to 35:656/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P120), A176 (≠ G144), G177 (= G145), R203 (= R171), T208 (≠ V176), D317 (= D286), E342 (= E311), G343 (= G312), P345 (= P314), G398 (= G367), E399 (= E368), P400 (= P369), T423 (≠ N389), W425 (= W391), Q426 (= Q392), T427 (= T393), D513 (= D484), I525 (= I496), R528 (= R499), R539 (= R510)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
38% identity, 99% coverage: 5:633/633 of query aligns to 35:656/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G367), E399 (= E368), P400 (= P369), T423 (≠ N389), Y424 (= Y390), W425 (= W391), Q426 (= Q392), T427 (= T393), D513 (= D484), I525 (= I496), R528 (= R499), R539 (= R510)
8w0jA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:633/633 of query aligns to 36:657/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G367), E400 (= E368), P401 (= P369), T424 (≠ N389), Y425 (= Y390), W426 (= W391), Q427 (= Q392), T428 (= T393), D514 (= D484), I526 (= I496), R529 (= R499), R540 (= R510)
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, 98% coverage: 7:628/633 of query aligns to 35:650/662 of P78773
- T596 (≠ Q575) modified: Phosphothreonine
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)
40% identity, 98% coverage: 8:629/633 of query aligns to 26:648/651 of P9WQD1
- K617 (= K598) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
37% identity, 98% coverage: 7:625/633 of query aligns to 3:615/615 of 1ry2A
- active site: T247 (= T244), T399 (= T393), N507 (= N505), K590 (= K598)
- binding adenosine monophosphate: G370 (= G367), E371 (= E368), P372 (= P369), T395 (≠ N389), Y396 (= Y390), W397 (= W391), Q398 (= Q392), T399 (= T393), D486 (= D484), I498 (= I496), R501 (= R499)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
37% identity, 99% coverage: 5:633/633 of query aligns to 35:651/654 of 7kdsA
- active site: T275 (= T244), T427 (= T393), E428 (= E394), N534 (= N505), R539 (= R510), K620 (= K598)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V290), G398 (= G367), E399 (= E368), P400 (= P369), D422 (= D388), T423 (≠ N389), Y424 (= Y390), W425 (= W391), Q426 (= Q392), T427 (= T393), D513 (= D484), R528 (= R499), N534 (= N505), R539 (= R510)
Query Sequence
>Ac3H11_2208 FitnessBrowser__acidovorax_3H11:Ac3H11_2208
MTAHSTYADFYRQSIDHRDAFWSEQAQLIDWKTPPQQVCDYSNPPFAKWFVGGTTNLCHN
AVDRHLATRASQAALVAISTETDTERSYSFAELHAEVQRMAAVLQSLGVKKGDRVLIYMP
MIAEAAFAMLACVRIGALHSVVFGGFASGSLASRIEDSEPVAVVSADAGSRGGKVVPYKP
LLDEAIALSKHKPAAVLMVNRGLAPMHLQPGRDHAWASLREQHLNTVVPCEWVDSTHPSY
TLYTSGTTGKPKGVQRDTGGYAVALAASMKHIFDAQPGEVYFATSDIGWVVGHSYIIYGP
LLAGMTTIMYEGLPIRPDAGVWWSIVEKYQVTHMFSAPTAVRVLKKQDPAFLTQYNVKSL
KALWLAGEPVDEPTARWIGAALNIPIIDNYWQTETGWPILAVANGIEANAARWGSPGKAV
YGYHVKLLDEATGEELTGANQKGVVAIEGPLPPGCMQTVWRDDARFVNTYWKSIPGRLIY
STFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESIASHPNIAEVAVVGVADSLKG
QVAMAFAVARDASGLDSDAARLKLEGEVMKQVDSQLGAVARPSRVYFVSVLPKTRSGKLL
RRALQAVAERRDPGDLTTMEDPAALQQVKELVG
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