SitesBLAST
Comparing WP_043750495.1 NCBI__GCF_000022085.1:WP_043750495.1 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)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
34% identity, 97% coverage: 17:537/538 of query aligns to 6:533/536 of 3c5eA
- active site: T188 (= T192), T331 (= T339), E332 (= E340), N434 (≠ T440), R439 (= R445), K524 (= K528)
- binding adenosine-5'-triphosphate: T188 (= T192), S189 (= S193), G190 (= G194), T191 (= T195), S192 (≠ T196), G305 (= G313), E306 (= E314), S307 (≠ M315), G329 (= G337), Q330 (= Q338), T331 (= T339), D413 (= D419), F425 (= F431), R428 (= R434), K524 (= K528)
- binding magnesium ion: M450 (≠ L456), H452 (= H458), V455 (= V461)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
34% identity, 97% coverage: 17:537/538 of query aligns to 7:534/537 of 3b7wA
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
34% identity, 97% coverage: 17:537/538 of query aligns to 3:530/533 of 3eq6A
- active site: T185 (= T192), T328 (= T339), E329 (= E340), N431 (≠ T440), R436 (= R445), K521 (= K528)
- binding adenosine monophosphate: G302 (= G313), E303 (= E314), S304 (≠ M315), E323 (= E334), S324 (≠ A335), Y325 (= Y336), G326 (= G337), Q327 (= Q338), T328 (= T339), D410 (= D419), F422 (= F431), R425 (= R434), R436 (= R445)
- binding Butyryl Coenzyme A: W229 (= W238), F255 (= F264), I277 (≠ T286), V301 (≠ A312), S433 (= S442), G434 (= G443), Y435 (= Y444), P501 (≠ A508), Y502 (≠ H509), Y504 (= Y511), R506 (= R513)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
34% identity, 97% coverage: 17:537/538 of query aligns to 3:530/533 of 2wd9A
- active site: T185 (= T192), T328 (= T339), E329 (= E340), N431 (≠ T440), R436 (= R445), K521 (= K528)
- binding ibuprofen: I230 (≠ A239), L231 (≠ G240), G326 (= G337), Q327 (= Q338), T328 (= T339), R436 (= R445)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
34% identity, 97% coverage: 17:537/538 of query aligns to 3:530/533 of 2vzeA
- active site: T185 (= T192), T328 (= T339), E329 (= E340), N431 (≠ T440), R436 (= R445), K521 (= K528)
- binding adenosine monophosphate: W229 (= W238), G302 (= G313), E303 (= E314), S304 (≠ M315), E323 (= E334), Y325 (= Y336), G326 (= G337), Q327 (= Q338), T328 (= T339), D410 (= D419), F422 (= F431), R425 (= R434), R436 (= R445)
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)
34% identity, 97% coverage: 17:537/538 of query aligns to 39:566/577 of Q08AH3
- Q139 (≠ V111) binding CoA
- 221:229 (vs. 192:200, 89% identical) binding ATP
- ESYGQT 359:364 (≠ EAYGQT 334:339) binding ATP
- T364 (= T339) binding substrate
- D446 (= D419) binding ATP
- R461 (= R434) binding ATP
- SGY 469:471 (= SGY 442:444) binding CoA
- R472 (= R445) binding substrate
- R501 (= R474) binding CoA
- S513 (≠ P486) to L: in dbSNP:rs1133607
- K532 (≠ R503) binding CoA
- YPR 540:542 (= YPR 511:513) binding CoA
- K557 (= K528) binding ATP
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
34% identity, 97% coverage: 17:537/538 of query aligns to 4:529/532 of 3gpcA
- active site: T186 (= T192), T327 (= T339), E328 (= E340), N430 (≠ T440), R435 (= R445), K520 (= K528)
- binding coenzyme a: G301 (= G313), E302 (= E314), S303 (≠ M315), E322 (= E334), Y324 (= Y336), G325 (= G337), Q326 (= Q338), T327 (= T339), D409 (= D419), F421 (= F431), R424 (= R434), T516 (= T524), K520 (= K528), Q522 (≠ I530)
- binding magnesium ion: H448 (= H458), V451 (= V461)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
34% identity, 97% coverage: 17:537/538 of query aligns to 7:532/535 of 3dayA
- active site: T189 (= T192), T332 (= T339), E333 (= E340), N435 (≠ T440), R440 (= R445), K523 (= K528)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T192), S190 (= S193), G191 (= G194), T192 (= T195), S193 (≠ T196), K197 (= K200), G306 (= G313), E307 (= E314), S308 (≠ M315), Y329 (= Y336), G330 (= G337), Q331 (= Q338), T332 (= T339), D414 (= D419), F426 (= F431), R429 (= R434), K523 (= K528)
- binding magnesium ion: M451 (≠ L456), H453 (= H458), V456 (= V461)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
31% identity, 97% coverage: 14:535/538 of query aligns to 71:618/630 of 8rplB
- 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: G391 (= G313), E392 (= E314), P393 (≠ M315), T416 (≠ A335), W417 (≠ Y336), W418 (≠ G337), Q419 (= Q338), T420 (= T339), D502 (= D419), R517 (= R434), K523 (≠ T440), R528 (= R445)
- binding magnesium ion: V539 (≠ L456), H541 (= H458)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
33% identity, 89% coverage: 55:533/538 of query aligns to 72:541/562 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 (≠ L243), G321 (= G313), E322 (= E314), P323 (≠ M315), D342 (≠ E334), F343 (≠ A335), Y344 (= Y336), Q346 (= Q338), T347 (= T339), D428 (= D419), F440 (= F431), K449 (≠ T440), R454 (= R445)
- binding coenzyme a: N128 (≠ V111), W247 (= W238), K249 (≠ G240), K273 (= K263), L274 (≠ F264), Q300 (≠ M290), D452 (≠ G443), Y453 (= Y444), R483 (= R474), P517 (≠ A508)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
33% identity, 89% coverage: 55:533/538 of query aligns to 70:539/561 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 (= G313), E320 (= E314), P321 (≠ M315), D340 (≠ E334), F341 (≠ A335), Y342 (= Y336), G343 (= G337), Q344 (= Q338), T345 (= T339), D426 (= D419), F438 (= F431), K447 (≠ T440), R452 (= R445)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
33% identity, 89% coverage: 55:533/538 of query aligns to 71:540/562 of 8biqA
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)
29% identity, 95% coverage: 23:535/538 of query aligns to 75:613/648 of Q89WV5
- G263 (= G194) mutation to I: Loss of activity.
- G266 (= G197) mutation to I: Great decrease in activity.
- K269 (= K200) mutation to G: Great decrease in activity.
- E414 (= E340) mutation to Q: Great decrease in activity.
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)
31% identity, 97% coverage: 15:536/538 of query aligns to 66:625/651 of P9WQD1
- K617 (= K528) modified: N6-acetyllysine; mutation to R: Complete loss of 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)
29% identity, 97% coverage: 14:535/538 of query aligns to 67:616/652 of P27550
- K609 (= K528) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
29% identity, 97% coverage: 14:535/538 of query aligns to 62:611/637 of 2p2fA
- active site: T259 (= T192), T411 (= T339), E412 (= E340), N516 (≠ T440), R521 (= R445), K604 (= K528)
- binding adenosine monophosphate: G382 (= G313), E383 (= E314), P384 (≠ M315), T407 (≠ A335), W408 (≠ Y336), W409 (≠ G337), Q410 (= Q338), T411 (= T339), D495 (= D419), I507 (≠ F431), R510 (= R434), N516 (≠ T440), R521 (= R445)
- binding coenzyme a: F158 (≠ A109), R186 (vs. gap), W304 (= W238), T306 (≠ G240), P329 (vs. gap), A352 (≠ P284), A355 (= A287), S518 (= S442), R579 (= R503), P584 (≠ A508)
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)
29% identity, 97% coverage: 14:535/538 of query aligns to 67:616/652 of Q8ZKF6
- R194 (≠ K138) 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 (≠ G240) binding CoA
- N335 (vs. gap) binding CoA
- A357 (≠ P284) 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 (= D436) 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 (= S442) binding CoA
- G524 (= G443) 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 (= R445) 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 (= R503) 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 (= K528) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
29% identity, 97% coverage: 14:535/538 of query aligns to 63:612/640 of 5jrhA
- active site: T260 (= T192), T412 (= T339), E413 (= E340), N517 (≠ T440), R522 (= R445), K605 (= K528)
- binding (r,r)-2,3-butanediol: W93 (≠ D44), E140 (≠ A90), G169 (≠ H119), K266 (≠ L198), P267 (= P199)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G313), E384 (= E314), P385 (≠ M315), T408 (≠ A335), W409 (≠ Y336), W410 (≠ G337), Q411 (= Q338), T412 (= T339), D496 (= D419), I508 (≠ F431), N517 (≠ T440), R522 (= R445)
- binding coenzyme a: F159 (≠ A109), G160 (≠ V110), G161 (≠ V111), R187 (vs. gap), S519 (= S442), R580 (= R503), P585 (≠ A508)
- binding magnesium ion: V533 (≠ L456), H535 (= H458), I538 (≠ V461)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
31% identity, 97% coverage: 16:535/538 of query aligns to 82:632/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G313), E400 (= E314), P401 (≠ M315), T424 (≠ A335), Y425 (= Y336), W426 (≠ G337), Q427 (= Q338), T428 (= T339), D514 (= D419), R529 (= R434), R540 (= R445)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
31% identity, 97% coverage: 16:535/538 of query aligns to 82:632/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A312), G399 (= G313), E400 (= E314), P401 (≠ M315), T424 (≠ A335), Y425 (= Y336), W426 (≠ G337), Q427 (= Q338), T428 (= T339), D514 (= D419), I526 (≠ F431), R529 (= R434), R540 (= R445)
Query Sequence
>WP_043750495.1 NCBI__GCF_000022085.1:WP_043750495.1
MLRPATYEDFVSGFRWRIPERYNIAVDVCDRWAAADPQRPALLDVAADGRVETWSFAALR
EASNRFANALRAQGIARGDRVAVLLPQSPAVLIAHLAIYKLGAVALPLAVVFGPDALLHR
LGNAGARAVVTHAGGLAKLAPLRDALPDLALLVSTEGPGDGALGFAELLAASAPDFTPVD
TAADDPALMIYTSGTTGLPKGALHGHRVLLGHLPGFAMMHEFMPQPGDRMWTPADWAWAG
GLLNALLPSLHHGVAVVARKAEKFEPEEVFRLMADLAVANAFVPPTALRMLRTVERPRAR
FDLSRLRTLASAGEMLGPETFGWAQAELRLTVNEAYGQTECNLVLASCAGLGLARAGSTG
KPVPGHRVAVIRPDGTPAAAGEIGQIAVARPDPVMFLGYWRDPAATEAKFLGDCMTTGDQ
GRVDADGYVHFVGRDDDVITSSGYRIGPGEIEDCLLRHPAVALAAAVGKPDPVRTEIVKA
VVVLRPGYQASDALAAEIQDFVRRRLSAHEYPREIAFRPSLPLTTTGKIIRRVLRDEG
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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