SitesBLAST
Comparing WP_028321365.1 NCBI__GCF_000422285.1:WP_028321365.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4wd1A Acetoacetyl-coa synthetase from streptomyces lividans (see paper)
46% identity, 99% coverage: 5:650/651 of query aligns to 4:646/646 of 4wd1A
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
27% identity, 96% coverage: 5:627/651 of query aligns to 6:626/630 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 (= G392), E392 (≠ S393), P393 (= P394), T416 (≠ I416), W417 (≠ A417), W418 (≠ G418), Q419 (≠ G419), T420 (= T420), D502 (= D504), R517 (= R519), K523 (≠ N525), R528 (= R530)
- binding magnesium ion: V539 (≠ E541), H541 (≠ F543)
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)
27% identity, 93% coverage: 35:640/651 of query aligns to 22:636/648 of Q89WV5
- G263 (= G273) mutation to I: Loss of activity.
- G266 (= G276) mutation to I: Great decrease in activity.
- K269 (= K279) mutation to G: Great decrease in activity.
- E414 (≠ D421) mutation to Q: Great decrease in activity.
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)
28% identity, 92% coverage: 36:636/651 of query aligns to 58:668/689 of Q9NUB1
- V488 (≠ I460) to M: in dbSNP:rs6050249
- K642 (= K612) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
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)
28% identity, 91% coverage: 32:625/651 of query aligns to 31:631/662 of P78773
- T596 (= T585) modified: Phosphothreonine
Q99NB1 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 Mus musculus (Mouse) (see paper)
28% identity, 93% coverage: 36:639/651 of query aligns to 51:664/682 of Q99NB1
- K635 (= K612) modified: N6-acetyllysine
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
26% identity, 95% coverage: 21:640/651 of query aligns to 22:654/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G392), E399 (≠ S393), P400 (= P394), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (vs. gap), T427 (≠ I416), D513 (= D504), I525 (= I516), R528 (= R519), R539 (= R530)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
26% identity, 95% coverage: 21:640/651 of query aligns to 23:655/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G392), E400 (≠ S393), P401 (= P394), T424 (≠ A417), Y425 (≠ G418), W426 (≠ G419), Q427 (≠ T420), T428 (≠ D421), D514 (= D504), R529 (= R519), R540 (= R530)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
26% identity, 95% coverage: 21:640/651 of query aligns to 23:655/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ T391), G399 (= G392), E400 (≠ S393), P401 (= P394), T424 (≠ A417), Y425 (≠ G418), W426 (≠ G419), Q427 (≠ T420), T428 (≠ D421), D514 (= D504), I526 (= I516), R529 (= R519), R540 (= R530)
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)
26% identity, 91% coverage: 35:624/651 of query aligns to 23:621/652 of P27550
- K609 (= K612) modified: N6-acetyllysine; by autocatalysis
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)
27% identity, 97% coverage: 9:640/651 of query aligns to 2:645/651 of P9WQD1
- K617 (= K612) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
27% identity, 84% coverage: 81:625/651 of query aligns to 88:651/676 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 (= G392), P408 (= P394), T431 (≠ I416), Y432 (≠ A417), Q434 (≠ G419), T435 (= T420), D522 (= D504), R537 (= R519), K638 (= K612)
8w0jA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a propyne amp ester inhibitor
26% identity, 95% coverage: 21:640/651 of query aligns to 23:650/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G392), E400 (≠ S393), P401 (= P394), T424 (vs. gap), Y425 (vs. gap), W426 (vs. gap), Q427 (vs. gap), T428 (≠ I416), D514 (= D504), I526 (= I516), R529 (= R519), R540 (= R530)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
27% identity, 91% coverage: 34:624/651 of query aligns to 17:616/637 of 2p2fA
- active site: T259 (≠ S271), T411 (= T420), E412 (≠ D421), N516 (= N525), R521 (= R530), K604 (= K612)
- binding adenosine monophosphate: G382 (= G392), E383 (≠ S393), P384 (= P394), T407 (≠ I416), W408 (≠ A417), W409 (≠ G418), Q410 (≠ G419), T411 (= T420), D495 (= D504), I507 (= I516), R510 (= R519), N516 (= N525), R521 (= R530)
- binding coenzyme a: F158 (≠ S170), R186 (≠ F198), W304 (= W316), T306 (≠ M318), P329 (= P339), A352 (≠ S362), A355 (≠ Y365), S518 (≠ G527), R579 (= R587), P584 (= P592)
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)
27% identity, 91% coverage: 34:624/651 of query aligns to 22:621/652 of Q8ZKF6
- R194 (≠ K201) 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 (≠ M318) binding CoA
- N335 (≠ F340) binding CoA
- A357 (≠ S362) 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 (= D521) 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 (≠ G527) binding CoA
- G524 (= G528) 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 (= R530) 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 (= R587) 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 (= K612) 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)
27% identity, 91% coverage: 34:624/651 of query aligns to 18:617/640 of 5jrhA
- active site: T260 (≠ S271), T412 (= T420), E413 (≠ D421), N517 (= N525), R522 (= R530), K605 (= K612)
- binding (r,r)-2,3-butanediol: W93 (≠ F105), E140 (≠ Q151), G169 (≠ D180), K266 (≠ L277), P267 (= P278)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ I416), W409 (≠ A417), W410 (≠ G418), Q411 (≠ G419), T412 (= T420), D496 (= D504), I508 (= I516), N517 (= N525), R522 (= R530)
- binding coenzyme a: F159 (≠ S170), G160 (≠ P171), G161 (≠ D172), R187 (≠ F198), S519 (≠ G527), R580 (= R587), P585 (= P592)
- binding magnesium ion: V533 (≠ E541), H535 (≠ F543), I538 (≠ V546)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
26% identity, 93% coverage: 34:636/651 of query aligns to 18:629/641 of 2p20A
- active site: T260 (≠ S271), T412 (= T420), E413 (≠ D421), N517 (= N525), R522 (= R530), K605 (= K612)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ I416), W409 (≠ A417), W410 (≠ G418), Q411 (≠ G419), T412 (= T420), D496 (= D504), I508 (= I516), R511 (= R519), R522 (= R530)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
27% identity, 83% coverage: 81:622/651 of query aligns to 52:600/615 of 1ry2A
- active site: T247 (≠ S271), T399 (= T420), N507 (= N525), K590 (= K612)
- binding adenosine monophosphate: G370 (= G392), E371 (≠ S393), P372 (= P394), T395 (≠ I416), Y396 (≠ A417), W397 (≠ G418), Q398 (≠ G419), T399 (= T420), D486 (= D504), I498 (= I516), R501 (= R519)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
26% identity, 91% coverage: 34:624/651 of query aligns to 18:617/634 of 1pg3A
- active site: T260 (≠ S271), T412 (= T420), E413 (≠ D421), N517 (= N525), R522 (= R530), K605 (= K612)
- binding coenzyme a: F159 (≠ S170), G160 (≠ P171), R187 (≠ F198), R190 (≠ K201), A301 (≠ T312), T307 (≠ M318), P330 (= P339), A356 (≠ Y365), S519 (≠ G527), R580 (= R587), P585 (= P592)
- binding magnesium ion: V533 (≠ E541), H535 (≠ F543), I538 (≠ V546)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ I416), W409 (≠ A417), W410 (≠ G418), Q411 (≠ G419), T412 (= T420), D496 (= D504), R511 (= R519), R522 (= R530)
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
28% identity, 84% coverage: 80:628/651 of query aligns to 86:647/656 of 5k8fA
- active site: T280 (≠ S271), T432 (≠ D421), E433 (≠ L422), N539 (= N525), R544 (= R530), K631 (= K612)
- 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: W325 (= W316), I326 (≠ M317), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (≠ A417), Y429 (≠ G418), W430 (≠ G419), M431 (≠ T420), T432 (≠ D421), D518 (= D504), I530 (= I516), R533 (= R519), K631 (= K612)
- binding adenosine-5'-triphosphate: T280 (≠ S271), S281 (= S272), G282 (= G273), S283 (≠ T274), T284 (= T275), K288 (= K279), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (≠ A417), Y429 (≠ G418), M431 (≠ T420), T432 (≠ D421), D518 (= D504), I530 (= I516), R533 (= R519), K631 (= K612)
Query Sequence
>WP_028321365.1 NCBI__GCF_000422285.1:WP_028321365.1
MAKLLWEPSEQRIQSSNMYRFMQHVNRRFGKTFDEYPSLYAWSVQNIPDFWAAFWEFSGV
IASEPYREVIDDLSKMPGAKWFSGARLNFAENLLRYRDDRTALIFKSEGRETIRWTYRRL
YEETAALAAALKRVGVAPGDRVVGFMPNMPQTTAAMLAAVSLGAVWSSCSPDFGIKGVLD
RFGQIKPTVLFTADGYPFKGKTFDSLARVAEILEDLPSTRQVVVVPYTQDRPDIGAVPRA
VLYDDFKEASPPPEMEFAQLPFDHPLYIMYSSGTTGLPKCMVQSTGGILVHHLKELMLHT
DLKREDTIFYFTTCGWMMWNWLTSSLALGATLVLFDGNPFHPAADALWELAQDEKITVFG
TSAGYLAALENAGVKPGHAFDLGPLRALLSTGSPLPVEGFEFVYRDIKQDLQLASIAGGT
DLNGCFALGNPMGPVYAGELQCRGLAMKVEAFDDNGRSVIDQKGELVCTAPWPSMPIYFW
DDPDGSKYHAAYFDVYPNVWRHGDFIEINDRGGVVIYGRSDATLNPGGVRIGTAEIYRQV
EQFKEVEDSLVVGQDWKNDVRVILFVKTAPGCMLDDDLKARLRSTIRTNASPRHVPAKIL
AVPDIPYTLNMKKVELAVKKTIQGQPVLNKDALRNPESLDFFAGLGELQSD
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