SitesBLAST
Comparing WP_086508401.1 NCBI__GCF_002151265.1:WP_086508401.1 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)
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)
33% identity, 93% coverage: 30:547/556 of query aligns to 72:620/652 of P27550
- K609 (= K536) modified: N6-acetyllysine; by autocatalysis
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)
33% identity, 92% coverage: 30:543/556 of query aligns to 82:625/662 of P78773
- T596 (≠ R513) modified: Phosphothreonine
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)
32% identity, 93% coverage: 30:547/556 of query aligns to 72:620/652 of Q8ZKF6
- R194 (vs. gap) 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 (≠ Y249) binding
- N335 (vs. gap) binding
- A357 (= A292) 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 (= D444) 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 (≠ A450) binding
- G524 (= G451) 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 (= R453) 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 (= R511) 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 (= K536) 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)
32% identity, 93% coverage: 30:547/556 of query aligns to 67:615/637 of 2p2fA
- active site: T259 (= T203), T411 (= T347), E412 (= E348), N516 (≠ T448), R521 (= R453), K604 (= K536)
- binding adenosine monophosphate: G382 (= G321), E383 (= E322), P384 (= P323), T407 (≠ H343), W408 (≠ Y344), W409 (≠ G345), Q410 (= Q346), T411 (= T347), D495 (= D427), I507 (≠ F439), R510 (= R442), N516 (≠ T448), R521 (= R453)
- binding coenzyme a: F158 (= F121), R186 (= R148), W304 (= W247), T306 (≠ Y249), P329 (vs. gap), A352 (= A292), A355 (= A295), S518 (≠ A450), R579 (= R511), P584 (≠ T516)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
32% identity, 93% coverage: 30:547/556 of query aligns to 68:616/640 of 5jrhA
- active site: T260 (= T203), T412 (= T347), E413 (= E348), N517 (≠ T448), R522 (= R453), K605 (= K536)
- binding (r,r)-2,3-butanediol: W93 (≠ H56), E140 (= E102), G169 (≠ Y131), K266 (= K209), P267 (= P210)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G321), E384 (= E322), P385 (= P323), T408 (≠ H343), W409 (≠ Y344), W410 (≠ G345), Q411 (= Q346), T412 (= T347), D496 (= D427), I508 (≠ F439), N517 (≠ T448), R522 (= R453)
- binding coenzyme a: F159 (= F121), G160 (≠ T122), G161 (≠ A123), R187 (= R148), S519 (≠ A450), R580 (= R511), P585 (≠ T516)
- binding magnesium ion: V533 (≠ L464), H535 (= H466), I538 (≠ V469)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
35% identity, 95% coverage: 17:542/556 of query aligns to 21:543/562 of 8bitA
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: W252 (≠ Y252), G321 (= G321), E322 (= E322), P323 (= P323), D342 (= D342), F343 (≠ H343), Y344 (= Y344), Q346 (= Q346), T347 (= T347), D428 (= D427), F440 (= F439), K449 (≠ T448), R454 (= R453)
- binding coenzyme a: N128 (≠ A123), W247 (= W247), K249 (≠ Y249), K273 (≠ A277), L274 (= L278), Q300 (≠ L298), D452 (≠ G451), Y453 (= Y452), R483 (= R482), P517 (≠ T516)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
32% identity, 93% coverage: 30:547/556 of query aligns to 68:616/641 of 2p20A
- active site: T260 (= T203), T412 (= T347), E413 (= E348), N517 (≠ T448), R522 (= R453), K605 (= K536)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G321), E384 (= E322), P385 (= P323), T408 (≠ H343), W409 (≠ Y344), W410 (≠ G345), Q411 (= Q346), T412 (= T347), D496 (= D427), I508 (≠ F439), R511 (= R442), R522 (= R453)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 95% coverage: 17:542/556 of query aligns to 20:542/562 of 8biqA
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 95% coverage: 17:542/556 of query aligns to 19:541/561 of 8biqB
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: G319 (= G321), E320 (= E322), P321 (= P323), D340 (= D342), F341 (≠ H343), Y342 (= Y344), G343 (= G345), Q344 (= Q346), T345 (= T347), D426 (= D427), F438 (= F439), K447 (≠ T448), R452 (= R453)
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
32% identity, 92% coverage: 30:543/556 of query aligns to 81:619/622 of 7kdnA
- active site: T271 (= T203), T422 (= T347), E423 (= E348), N529 (≠ T448), R534 (= R453), K612 (= K536)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G321), E394 (= E322), P395 (= P323), T418 (≠ H343), Y419 (= Y344), W420 (≠ G345), Q421 (= Q346), T422 (= T347), D508 (= D427), I520 (≠ F439), R523 (= R442), R534 (= R453)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
32% identity, 93% coverage: 30:547/556 of query aligns to 68:616/634 of 1pg3A
- active site: T260 (= T203), T412 (= T347), E413 (= E348), N517 (≠ T448), R522 (= R453), K605 (= K536)
- binding coenzyme a: F159 (= F121), G160 (≠ T122), R187 (= R148), R190 (vs. gap), A301 (= A243), T307 (≠ Y249), P330 (vs. gap), A356 (= A295), S519 (≠ A450), R580 (= R511), P585 (≠ T516)
- binding magnesium ion: V533 (≠ L464), H535 (= H466), I538 (≠ V469)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G321), E384 (= E322), P385 (= P323), T408 (≠ H343), W409 (≠ Y344), W410 (≠ G345), Q411 (= Q346), T412 (= T347), D496 (= D427), R511 (= R442), R522 (= R453)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
31% identity, 90% coverage: 31:531/556 of query aligns to 82:612/633 of 7kvyA
- active site: T271 (= T203), T422 (= T347), E423 (= E348), N529 (≠ T448), R534 (= R453), K612 (= K531)
- binding coenzyme a: F172 (= F121), G174 (≠ A123), R200 (vs. gap), G312 (≠ A243), Y362 (≠ A290), V363 (≠ A291), A364 (= A292), S531 (≠ A450), G532 (= G451), R592 (= R511), F598 (≠ H517)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G321), E394 (= E322), P395 (= P323), T418 (≠ H343), Y419 (= Y344), W420 (≠ G345), Q421 (= Q346), T422 (= T347), D508 (= D427), I520 (≠ F439), R523 (= R442), R534 (= R453)
7l3qA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-methylphosphate and co-enzyme a from coccidioides immitis rs
31% identity, 91% coverage: 31:537/556 of query aligns to 83:619/631 of 7l3qA
- active site: T272 (= T203), T423 (= T347), E424 (= E348), N530 (≠ T448), R535 (= R453)
- binding coenzyme a: F173 (= F121), A174 (≠ T122), G175 (≠ A123), R201 (vs. gap), G313 (≠ A243), Y363 (≠ A290), A365 (= A292), S532 (≠ A450), G533 (= G451), R593 (= R511), P598 (≠ T516), F599 (≠ H517)
- binding 5'-O-[(R)-hydroxy(methoxy)phosphoryl]adenosine: I318 (≠ A248), G394 (= G321), E395 (= E322), P396 (= P323), T419 (≠ H343), Y420 (= Y344), Q422 (= Q346), T423 (= T347), D509 (= D427), R524 (= R442), R535 (= R453)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
33% identity, 82% coverage: 86:543/556 of query aligns to 70:532/537 of 3b7wA
Q9NUB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see 3 papers)
30% identity, 94% coverage: 31:551/556 of query aligns to 106:657/689 of Q9NUB1
- V488 (≠ P388) to M: in dbSNP:rs6050249
- K642 (= K536) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
33% identity, 82% coverage: 86:543/556 of query aligns to 69:531/536 of 3c5eA
- active site: T188 (= T203), T331 (= T347), E332 (= E348), N434 (≠ T448), R439 (= R453), K524 (= K536)
- binding adenosine-5'-triphosphate: T188 (= T203), S189 (= S204), G190 (= G205), T191 (= T206), S192 (≠ V207), G305 (= G321), E306 (= E322), S307 (≠ P323), G329 (= G345), Q330 (= Q346), T331 (= T347), D413 (= D427), F425 (= F439), R428 (= R442), K524 (= K536)
- binding magnesium ion: M450 (≠ L464), H452 (= H466), V455 (= V469)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
33% identity, 82% coverage: 86:543/556 of query aligns to 66:528/533 of 3eq6A
- active site: T185 (= T203), T328 (= T347), E329 (= E348), N431 (≠ T448), R436 (= R453), K521 (= K536)
- binding adenosine monophosphate: G302 (= G321), E303 (= E322), S304 (≠ P323), E323 (≠ D342), S324 (≠ H343), Y325 (= Y344), G326 (= G345), Q327 (= Q346), T328 (= T347), D410 (= D427), F422 (= F439), R425 (= R442), R436 (= R453)
- binding Butyryl Coenzyme A: W229 (= W247), F255 (= F272), I277 (≠ T294), V301 (≠ A320), S433 (≠ A450), G434 (= G451), Y435 (= Y452), P501 (≠ T516), Y502 (≠ H517), Y504 (≠ F519), R506 (= R521)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
33% identity, 82% coverage: 86:543/556 of query aligns to 66:528/533 of 2wd9A
- active site: T185 (= T203), T328 (= T347), E329 (= E348), N431 (≠ T448), R436 (= R453), K521 (= K536)
- binding ibuprofen: I230 (≠ A248), L231 (≠ Y249), G326 (= G345), Q327 (= Q346), T328 (= T347), R436 (= R453)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
33% identity, 82% coverage: 86:543/556 of query aligns to 66:528/533 of 2vzeA
- active site: T185 (= T203), T328 (= T347), E329 (= E348), N431 (≠ T448), R436 (= R453), K521 (= K536)
- binding adenosine monophosphate: W229 (= W247), G302 (= G321), E303 (= E322), S304 (≠ P323), E323 (≠ D342), Y325 (= Y344), G326 (= G345), Q327 (= Q346), T328 (= T347), D410 (= D427), F422 (= F439), R425 (= R442), R436 (= R453)
Q08AH3 Acyl-coenzyme A synthetase ACSM2A, mitochondrial; Acyl-CoA synthetase medium-chain family member 2A; Benzoate--CoA ligase; Butyrate--CoA ligase 2A; Butyryl-coenzyme A synthetase 2A; Middle-chain acyl-CoA synthetase 2A; EC 6.2.1.2; EC 6.2.1.25 from Homo sapiens (Human) (see 4 papers)
32% identity, 85% coverage: 86:556/556 of query aligns to 102:577/577 of Q08AH3
- Q139 (≠ A123) binding
- 221:229 (vs. 203:211, 78% identical) binding
- ESYGQT 359:364 (≠ DHYGQT 342:347) binding
- T364 (= T347) binding
- D446 (= D427) binding
- R461 (= R442) binding
- SGY 469:471 (≠ AGY 450:452) binding
- R472 (= R453) binding
- R501 (= R482) binding
- S513 (≠ E494) to L: in dbSNP:rs1133607
- K532 (≠ R511) binding
- YPR 540:542 (≠ FPR 519:521) binding
- K557 (= K536) binding
Query Sequence
>WP_086508401.1 NCBI__GCF_002151265.1:WP_086508401.1
MSTQSLPEYPAFMERFSIDEVIARLDDHGDGKFNAFESCCGRHLRAGRGEVLALVHEDTQ
GNVNRRTYAELEAESARLAGWFAERGLGVGDRIACMLPRSPELLVAVLATWRIGAVYQPL
FTAFGPDAVDYRLGRADTRLVITDHANRFKFDGLSQCPPVLAVGGPSEGHDGDLDWDEAL
AHSPIQANPPRLSPEAPFLQMFTSGTVGKPKGVAVPLSGMPAFALYMELAIDLRESDRFW
NMADPGWAYGLYYAIAGPLLLGVTTHFCEAGFSAEGALDFMRRHRITNFAAAPTAYRLMK
ASGLFDSAHESLELRVASSAGEPLNTEVVTWVERSLGCPVMDHYGQTETGMTCCNHHALG
HPKHVGAMGVPMPGYRLAILDAEHNELPPGEPGVLAVDIERSPAHFFQGYTWQEKHPFAN
GYYLTGDVVIRNEDGTFQFAGRDDDIITTAGYRVGPTDVENTVLTHPAVAESAAVGQPDE
IRGEIIKSYVVLREGFEASDELAEEIRQRVRERLSTHAFPRVIEFVDTLPKTPSGKIQRF
KLRADAAEKAEAAAAK
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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