SitesBLAST
Comparing WP_012567024.1 NCBI__GCF_000016185.1:WP_012567024.1 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
66% identity, 98% coverage: 5:629/636 of query aligns to 2:626/627 of 5gxdA
- active site: T238 (= T241), T390 (= T393), E391 (= E394), N498 (= N501), R503 (= R506), K587 (= K590)
- binding adenosine monophosphate: G364 (= G367), E365 (= E368), R366 (= R369), H386 (= H389), W387 (= W390), W388 (= W391), Q389 (= Q392), T390 (= T393), D477 (= D480), I489 (≠ V492), R492 (= R495), N498 (= N501), R503 (= R506)
- binding coenzyme a: F139 (= F142), G140 (= G143), G141 (= G144), E167 (= E170), R170 (= R173), S279 (= S282), K307 (= K310), P308 (= P311), A332 (= A335), T334 (= T337), A363 (= A366), A500 (= A503), H502 (= H505), K532 (= K535), R562 (= R565), P567 (= P570), V568 (= V571)
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)
42% identity, 97% coverage: 3:620/636 of query aligns to 21:638/648 of Q89WV5
- G263 (= G243) mutation to I: Loss of activity.
- G266 (= G246) mutation to I: Great decrease in activity.
- K269 (= K249) mutation to G: Great decrease in activity.
- E414 (= E394) mutation to Q: Great decrease in activity.
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, 98% coverage: 2:627/636 of query aligns to 21:648/652 of Q8ZKF6
- R194 (= R173) 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 (≠ V288) binding CoA
- N335 (≠ G313) binding CoA
- 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 CoA
- 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 (= R565) 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 (= K590) 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)
39% identity, 97% coverage: 2:620/636 of query aligns to 16:631/637 of 2p2fA
- active site: T259 (= T241), T411 (= T393), E412 (= E394), N516 (= N501), R521 (= R506), K604 (= K590)
- binding adenosine monophosphate: G382 (= G367), E383 (= E368), P384 (≠ R369), T407 (≠ H389), W408 (= W390), W409 (= W391), Q410 (= Q392), T411 (= T393), D495 (= D480), I507 (≠ V492), R510 (= R495), N516 (= N501), R521 (= R506)
- binding coenzyme a: F158 (= F142), R186 (≠ E170), W304 (= W286), T306 (≠ V288), P329 (= P311), A352 (= A335), A355 (= A338), S518 (≠ A503), R579 (= R565), P584 (= P570)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
38% identity, 97% coverage: 2:620/636 of query aligns to 17:635/641 of 2p20A
- active site: T260 (= T241), T412 (= T393), E413 (= E394), N517 (= N501), R522 (= R506), K605 (= K590)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G367), E384 (= E368), P385 (≠ R369), T408 (≠ H389), W409 (= W390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D480), I508 (≠ V492), R511 (= R495), R522 (= R506)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
39% identity, 97% coverage: 2:620/636 of query aligns to 17:634/640 of 5jrhA
- active site: T260 (= T241), T412 (= T393), E413 (= E394), N517 (= N501), R522 (= R506), K605 (= K590)
- binding (r,r)-2,3-butanediol: W93 (≠ Y76), E140 (= E123), G169 (≠ T152), K266 (≠ Q247), P267 (= P248)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G367), E384 (= E368), P385 (≠ R369), T408 (≠ H389), W409 (= W390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D480), I508 (≠ V492), N517 (= N501), R522 (= R506)
- binding coenzyme a: F159 (= F142), G160 (= G143), G161 (= G144), R187 (≠ E170), S519 (≠ A503), R580 (= R565), P585 (= P570)
- binding magnesium ion: V533 (≠ A517), H535 (= H519), I538 (≠ V522)
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)
37% identity, 98% coverage: 2:627/636 of query aligns to 21:648/652 of P27550
- K609 (= K590) modified: N6-acetyllysine; by autocatalysis
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
38% identity, 97% coverage: 2:620/636 of query aligns to 17:628/634 of 1pg3A
- active site: T260 (= T241), T412 (= T393), E413 (= E394), N517 (= N501), R522 (= R506), K605 (= K590)
- binding coenzyme a: F159 (= F142), G160 (= G143), R187 (≠ E170), R190 (= R173), A301 (≠ S282), T307 (≠ V288), P330 (= P311), A356 (= A338), S519 (≠ A503), R580 (= R565), P585 (= P570)
- binding magnesium ion: V533 (≠ A517), H535 (= H519), I538 (≠ V522)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G367), E384 (= E368), P385 (≠ R369), T408 (≠ H389), W409 (= W390), W410 (= W391), Q411 (= Q392), T412 (= T393), D496 (= D480), R511 (= R495), R522 (= R506)
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
36% identity, 98% coverage: 5:625/636 of query aligns to 39:675/676 of 8rwjD
- 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: G406 (= G367), P408 (≠ R369), T431 (≠ H389), Y432 (≠ W390), Q434 (= Q392), T435 (= T393), D522 (= D480), R537 (= R495), K638 (= K590)
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, 97% coverage: 7:620/636 of query aligns to 27:647/651 of P9WQD1
- K617 (= K590) 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, 94% coverage: 5:599/636 of query aligns to 3:599/615 of 1ry2A
- active site: T247 (= T241), T399 (= T393), N507 (= N501), K590 (= K590)
- binding adenosine monophosphate: G370 (= G367), E371 (= E368), P372 (≠ R369), T395 (≠ H389), Y396 (≠ W390), W397 (= W391), Q398 (= Q392), T399 (= T393), D486 (= D480), I498 (≠ V492), R501 (= R495)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
37% identity, 94% coverage: 5:604/636 of query aligns to 31:625/630 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 (= G367), E392 (= E368), P393 (≠ R369), T416 (≠ H389), W417 (= W390), W418 (= W391), Q419 (= Q392), T420 (= T393), D502 (= D480), R517 (= R495), K523 (≠ N501), R528 (= R506)
- binding magnesium ion: V539 (≠ A517), H541 (= H519)
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)
36% identity, 99% coverage: 4:633/636 of query aligns to 39:682/683 of P52910
- K506 (≠ S470) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
37% identity, 99% coverage: 5:633/636 of query aligns to 35:660/662 of P78773
- T596 (≠ E567) modified: Phosphothreonine
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
35% identity, 98% coverage: 4:624/636 of query aligns to 36:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G367), E399 (= E368), P400 (≠ R369), T423 (≠ H389), Y424 (≠ W390), W425 (= W391), Q426 (= Q392), T427 (= T393), D513 (= D480), I525 (≠ V492), R528 (= R495), R539 (= R506)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
35% identity, 98% coverage: 4:624/636 of query aligns to 36:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G367), E399 (= E368), P400 (≠ R369), T423 (≠ H389), Y424 (≠ W390), Q426 (= Q392), T427 (= T393), D513 (= D480), I525 (≠ V492), R528 (= R495), R539 (= R506)
- binding coenzyme a: F175 (= F142), R203 (≠ E170), R206 (= R173), G316 (≠ S282), H538 (= H505), R599 (= R565), F605 (≠ V571)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
35% identity, 98% coverage: 4:624/636 of query aligns to 37:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G367), E400 (= E368), P401 (≠ R369), T424 (≠ H389), Y425 (≠ W390), W426 (= W391), Q427 (= Q392), T428 (= T393), D514 (= D480), R529 (= R495), R540 (= R506)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
35% identity, 98% coverage: 4:624/636 of query aligns to 37:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A366), G399 (= G367), E400 (= E368), P401 (≠ R369), T424 (≠ H389), Y425 (≠ W390), W426 (= W391), Q427 (= Q392), T428 (= T393), D514 (= D480), I526 (≠ V492), R529 (= R495), R540 (= R506)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
35% identity, 98% coverage: 4:624/636 of query aligns to 36:650/654 of 7kdsA
- active site: T275 (= T241), T427 (= T393), E428 (= E394), N534 (= N501), R539 (= R506), K620 (= K590)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V287), G398 (= G367), E399 (= E368), P400 (≠ R369), D422 (= D388), T423 (≠ H389), Y424 (≠ W390), W425 (= W391), Q426 (= Q392), T427 (= T393), D513 (= D480), R528 (= R495), N534 (= N501), R539 (= R506)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
35% identity, 98% coverage: 4:624/636 of query aligns to 36:655/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P119), A176 (≠ G143), G177 (= G144), R203 (≠ E170), T208 (≠ V175), D317 (= D283), E342 (= E308), G343 (= G309), P345 (= P311), G398 (= G367), E399 (= E368), P400 (≠ R369), T423 (≠ H389), W425 (= W391), Q426 (= Q392), T427 (= T393), D513 (= D480), I525 (≠ V492), R528 (= R495), R539 (= R506)
Query Sequence
>WP_012567024.1 NCBI__GCF_000016185.1:WP_012567024.1
MPARYEELHQRSLADPAGFWGEAAKDIDWIRPWDVVLDDSRAPLYRWFAGGELNTCWNAI
DRHVEGGRADQPAIIYDSPVTGTKRILTYRDFRDQVALFAGALRDRGVVKGDRVLVYMPM
VPEALVAMLACARLGAVHSVVFGGFAPHELATRINDAQPKVIVSASCGIEPGRVVKYKPM
LDSAIEQATHKPESCLILQRPQEQASLIDGRDHDWEAAVAATTPADCVPVAATDPLYILY
TSGTTGQPKGVVRDNGGHAVALKWTMEHFYGVKPGEVFWAASDVGWVVGHSYIVYAPLLH
GCTTVIYEGKPVGTPDAGAFWRMISEYRIQTLFTAPTAFRAIKRDDPNALLLKNYDVSCL
RALFLAGERSDPDTLHWAEDHLKVPVIDHWWQTETGWPIAGNPLGLGLFPVKYGSTCKPL
PGWDVRILGADGHEVKRGDIGAIVCKLPLPPGTLATLWNAEDRFRKSYLSEFSGYYQTAD
AGFVDADGYVYVMARTDDIINVAGHRLSTGGMEEVLAGHPDVAECAVIGVADQLKGQVPL
GFVVLKAGVTRPTEVIVREIVAKVRDEIGPVASFKQAIVVDRLPKTRSGKILRGTMQKIA
DAEPWKMPATIDDPMILEEIGDALRTIGYAVDKPAD
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