SitesBLAST
Comparing HSERO_RS15645 FitnessBrowser__HerbieS:HSERO_RS15645 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: 3:622/628 of query aligns to 2:617/627 of 5gxdA
- active site: T238 (= T240), T390 (= T389), E391 (= E390), N498 (= N499), R503 (= R504), K587 (= K592)
- binding adenosine monophosphate: G364 (= G363), E365 (= E364), R366 (≠ P365), H386 (≠ N385), W387 (≠ Y386), W388 (= W387), Q389 (= Q388), T390 (= T389), D477 (= D478), I489 (= I490), R492 (= R493), N498 (= N499), R503 (= R504)
- binding coenzyme a: F139 (= F139), G140 (= G140), G141 (= G141), E167 (≠ R167), R170 (≠ K170), S279 (= S281), K307 (≠ L309), P308 (= P310), A332 (= A333), T334 (= T335), A363 (= A362), A500 (= A501), H502 (= H503), K532 (= K533), R562 (≠ D567), P567 (≠ A572), V568 (= V573)
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: 2:622/628 of query aligns to 22:638/648 of Q89WV5
- G263 (= G242) mutation to I: Loss of activity.
- G266 (= G245) mutation to I: Great decrease in activity.
- K269 (= K248) mutation to G: Great decrease in activity.
- E414 (= E390) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
38% identity, 99% coverage: 2:622/628 of query aligns to 19:635/641 of 2p20A
- active site: T260 (= T240), T412 (= T389), E413 (= E390), N517 (= N499), R522 (= R504), K605 (= K592)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G363), E384 (= E364), P385 (= P365), T408 (≠ N385), W409 (≠ Y386), W410 (= W387), Q411 (= Q388), T412 (= T389), D496 (= D478), I508 (= I490), R511 (= R493), R522 (= R504)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
39% identity, 99% coverage: 2:622/628 of query aligns to 19:634/640 of 5jrhA
- active site: T260 (= T240), T412 (= T389), E413 (= E390), N517 (= N499), R522 (= R504), K605 (= K592)
- binding (r,r)-2,3-butanediol: W93 (≠ A73), E140 (= E120), G169 (≠ S149), K266 (= K246), P267 (= P247)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G363), E384 (= E364), P385 (= P365), T408 (≠ N385), W409 (≠ Y386), W410 (= W387), Q411 (= Q388), T412 (= T389), D496 (= D478), I508 (= I490), N517 (= N499), R522 (= R504)
- binding coenzyme a: F159 (= F139), G160 (= G140), G161 (= G141), R187 (= R167), S519 (≠ A501), R580 (≠ D567), P585 (≠ A572)
- binding magnesium ion: V533 (≠ S515), H535 (= H517), I538 (≠ V520)
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)
38% identity, 99% coverage: 2:622/628 of query aligns to 23:641/652 of Q8ZKF6
- R194 (≠ K170) 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 (≠ V287) binding
- N335 (≠ I311) binding
- A357 (= A333) 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 (= D495) 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 (≠ A501) binding
- G524 (= G502) 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 (= R504) 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 (≠ D567) 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 (= K592) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase 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)
39% identity, 99% coverage: 2:622/628 of query aligns to 23:641/652 of P27550
- K609 (= K592) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
38% identity, 99% coverage: 2:622/628 of query aligns to 18:631/637 of 2p2fA
- active site: T259 (= T240), T411 (= T389), E412 (= E390), N516 (= N499), R521 (= R504), K604 (= K592)
- binding adenosine monophosphate: G382 (= G363), E383 (= E364), P384 (= P365), T407 (≠ N385), W408 (≠ Y386), W409 (= W387), Q410 (= Q388), T411 (= T389), D495 (= D478), I507 (= I490), R510 (= R493), N516 (= N499), R521 (= R504)
- binding coenzyme a: F158 (= F139), R186 (= R167), W304 (= W285), T306 (≠ V287), P329 (= P310), A352 (= A333), A355 (= A336), S518 (≠ A501), R579 (≠ D567), P584 (≠ A572)
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)
40% identity, 99% coverage: 2:622/628 of query aligns to 34:650/662 of P78773
- T596 (≠ Q569) modified: Phosphothreonine
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 97% coverage: 2:608/628 of query aligns to 19:623/634 of 1pg3A
- active site: T260 (= T240), T412 (= T389), E413 (= E390), N517 (= N499), R522 (= R504), K605 (= K592)
- binding coenzyme a: F159 (= F139), G160 (= G140), R187 (= R167), R190 (≠ K170), A301 (≠ S281), T307 (≠ V287), P330 (= P310), A356 (= A336), S519 (≠ A501), R580 (≠ D567), P585 (≠ A572)
- binding magnesium ion: V533 (≠ S515), H535 (= H517), I538 (≠ V520)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G363), E384 (= E364), P385 (= P365), T408 (≠ N385), W409 (≠ Y386), W410 (= W387), Q411 (= Q388), T412 (= T389), D496 (= D478), R511 (= R493), R522 (= R504)
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, 99% coverage: 5:624/628 of query aligns to 27:649/651 of P9WQD1
- K617 (= K592) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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: 2:628/628 of query aligns to 39:675/683 of P52910
- K506 (≠ R467) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
38% identity, 98% coverage: 2:619/628 of query aligns to 2:615/615 of 1ry2A
- active site: T247 (= T240), T399 (= T389), N507 (= N499), K590 (= K592)
- binding adenosine monophosphate: G370 (= G363), E371 (= E364), P372 (= P365), T395 (≠ N385), Y396 (= Y386), W397 (= W387), Q398 (= Q388), T399 (= T389), D486 (= D478), I498 (= I490), R501 (= R493)
8w0cA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 2:622/628 of query aligns to 37:657/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G363), E400 (= E364), P401 (= P365), T424 (≠ N385), Y425 (= Y386), W426 (= W387), Q427 (= Q388), T428 (= T389), D514 (= D478), R529 (= R493), R540 (= R504)
8w0bA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 2:622/628 of query aligns to 37:657/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A362), G399 (= G363), E400 (= E364), P401 (= P365), T424 (≠ N385), Y425 (= Y386), W426 (= W387), Q427 (= Q388), T428 (= T389), D514 (= D478), I526 (= I490), R529 (= R493), R540 (= R504)
8w0dA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 2:622/628 of query aligns to 36:656/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G363), E399 (= E364), P400 (= P365), T423 (≠ N385), Y424 (= Y386), W425 (= W387), Q426 (= Q388), T427 (= T389), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
38% identity, 99% coverage: 2:622/628 of query aligns to 36:656/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G363), E399 (= E364), P400 (= P365), T423 (≠ N385), Y424 (= Y386), Q426 (= Q388), T427 (= T389), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
- binding coenzyme a: F175 (= F139), R203 (= R167), R206 (≠ K170), G316 (≠ S281), H538 (= H503), R599 (≠ D567), F605 (≠ V573)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
39% identity, 99% coverage: 5:624/628 of query aligns to 27:655/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G363), E399 (= E364), P400 (= P365), T423 (≠ N385), W424 (≠ Y386), Q426 (= Q388), T427 (= T389), D511 (= D478), R526 (= R493), R537 (= R504)
- binding coenzyme a: F171 (= F139), G172 (= G140), G173 (= G141), R199 (= R167), K202 (= K170), R595 (≠ D567), P600 (≠ A572)
8w0jA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 2:622/628 of query aligns to 37:652/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G363), E400 (= E364), P401 (= P365), T424 (≠ N385), Y425 (= Y386), W426 (= W387), Q427 (= Q388), T428 (= T389), D514 (= D478), I526 (= I490), R529 (= R493), R540 (= R504)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
38% identity, 99% coverage: 2:622/628 of query aligns to 36:651/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P116), A176 (≠ G140), G177 (= G141), R203 (= R167), T208 (≠ I172), D317 (= D282), E342 (= E307), G343 (= G308), P345 (= P310), G398 (= G363), E399 (= E364), P400 (= P365), T423 (≠ N385), W425 (= W387), Q426 (= Q388), T427 (= T389), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
38% identity, 99% coverage: 2:622/628 of query aligns to 36:651/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G363), E399 (= E364), P400 (= P365), T423 (≠ N385), Y424 (= Y386), W425 (= W387), Q426 (= Q388), T427 (= T389), D513 (= D478), I525 (= I490), R528 (= R493), R539 (= R504)
Query Sequence
>HSERO_RS15645 FitnessBrowser__HerbieS:HSERO_RS15645
MQYEQFYRQSVEQPEAFWAQEAQRIHWQQPFSRTLDYSRPPFARWFIDGQTNLCHNAVDR
HLPERAQQAALIAISTETNSERVYTYAELQQEVMAMAASMQALGVQRGDRVLIYMPMIAE
AVFAMLACARIGAVHSVVFGGFASNSLASRIDDAQPRLIVSADAGSRGGKVIPYKGLLDE
AIAMAQHRPQHVLLVDRGLAPMARTAQRDVDYAPLRTQHLGQQVPVTWLESNASSYILYT
SGTTGKPKGVQRDVGGYAVALASSMQHIFCGQPGETYFCTSDIGWVVGHSYIVYGPLIAG
MATVLYEGLPIRPDAGIWWSIVEKYKVTRMFSAPTAIRVLKKQPPECMERYDTSSLKALY
LAGEPLDETTSSWISGALKVPVIDNYWQTESGWPIISIAKGIDDKPTRLGSPGVPMPGYR
LAILDEATGEPCGPDQKGVVAIEGPLPPGCMQTVYGDDERFVNTYWRSLPREVYSTFDWG
IRDKDGYYFILGRTDDVINVAGHRLGTREIEESISSHPNVSEVAVVGVEDKLKGQVAFAF
AIPKQAYTIATPEQRKALEAEIMAVVDKQIGAVGRPARVFFVSGLPKTRSGKLLRRAIQS
ICEGRDPGDLPTIEDPAALEQVRAVIKD
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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