SitesBLAST
Comparing WP_089301905.1 NCBI__GCF_900188115.1:WP_089301905.1 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)
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)
65% identity, 99% coverage: 1:657/665 of query aligns to 1:650/651 of P9WQD1
- K617 (= K624) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
52% identity, 93% coverage: 33:652/665 of query aligns to 25:636/648 of Q89WV5
- G263 (= G271) mutation to I: Loss of activity.
- G266 (= G274) mutation to I: Great decrease in activity.
- K269 (= K277) mutation to G: Great decrease in activity.
- E414 (= E423) mutation to Q: Great decrease in activity.
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
49% identity, 95% coverage: 12:643/665 of query aligns to 1:630/630 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 (= G393), E392 (= E394), P393 (= P395), T416 (= T418), W417 (= W419), W418 (= W420), Q419 (= Q421), T420 (= T422), D502 (= D508), R517 (= R523), K523 (≠ N529), R528 (= R534)
- binding magnesium ion: V539 (= V545), H541 (= H547)
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)
51% identity, 92% coverage: 45:654/665 of query aligns to 38:641/652 of P27550
- K609 (= K624) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
50% identity, 93% coverage: 35:654/665 of query aligns to 24:635/641 of 2p20A
- active site: T260 (= T269), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K624)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (≠ L520), R511 (= R523), R522 (= R534)
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)
50% identity, 93% coverage: 35:654/665 of query aligns to 28:641/652 of Q8ZKF6
- R194 (≠ K198) 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 (= T317) binding CoA
- N335 (= N341) binding CoA
- A357 (= A363) 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 (= D525) 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 (= S531) binding CoA
- G524 (= G532) 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 (= R534) 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 (≠ A599) 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 (= K624) 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)
50% identity, 93% coverage: 35:654/665 of query aligns to 24:634/640 of 5jrhA
- active site: T260 (= T269), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K624)
- binding (r,r)-2,3-butanediol: W93 (= W102), E140 (= E148), G169 (≠ T177), K266 (= K275), P267 (= P276)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (≠ L520), N517 (= N529), R522 (= R534)
- binding coenzyme a: F159 (= F167), G160 (= G168), G161 (= G169), R187 (= R195), S519 (= S531), R580 (≠ A599), P585 (= P604)
- binding magnesium ion: V533 (= V545), H535 (= H547), I538 (≠ V550)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
50% identity, 93% coverage: 35:654/665 of query aligns to 23:631/637 of 2p2fA
- active site: T259 (= T269), T411 (= T422), E412 (= E423), N516 (= N529), R521 (= R534), K604 (= K624)
- binding adenosine monophosphate: G382 (= G393), E383 (= E394), P384 (= P395), T407 (= T418), W408 (= W419), W409 (= W420), Q410 (= Q421), T411 (= T422), D495 (= D508), I507 (≠ L520), R510 (= R523), N516 (= N529), R521 (= R534)
- binding coenzyme a: F158 (= F167), R186 (= R195), W304 (= W315), T306 (= T317), P329 (= P340), A352 (= A363), A355 (≠ L366), S518 (= S531), R579 (≠ A599), P584 (= P604)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
50% identity, 93% coverage: 35:654/665 of query aligns to 24:628/634 of 1pg3A
- active site: T260 (= T269), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K624)
- binding coenzyme a: F159 (= F167), G160 (= G168), R187 (= R195), R190 (≠ K198), A301 (= A311), T307 (= T317), P330 (= P340), A356 (≠ L366), S519 (= S531), R580 (≠ A599), P585 (= P604)
- binding magnesium ion: V533 (= V545), H535 (= H547), I538 (≠ V550)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), R511 (= R523), R522 (= R534)
Q9NR19 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see paper)
46% identity, 96% coverage: 15:651/665 of query aligns to 26:689/701 of Q9NR19
- T363 (= T317) mutation to A: Loss of catalytic activity but no effect on its nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- 656:668 (vs. 619:631, 92% identical) Nuclear localization signal
- S659 (= S622) modified: Phosphoserine; by AMPK; mutation to A: No effect on catalytic activity. Loss of AMPK-mediated phosphorylation, interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- RR 664:665 (= RR 627:628) mutation to AA: No effect on catalytic activity. Loss of interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
Sites not aligning to the query:
- 1:107 Interaction with TFEB
Q9QXG4 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
48% identity, 91% coverage: 45:652/665 of query aligns to 61:690/701 of Q9QXG4
- K661 (= K624) modified: N6-acetyllysine
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)
47% identity, 96% coverage: 20:658/665 of query aligns to 29:673/683 of P52910
- K506 (≠ S496) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
47% identity, 92% coverage: 20:633/665 of query aligns to 23:621/633 of 7kvyA
- active site: T271 (= T269), T422 (= T422), E423 (= E423), N529 (= N529), R534 (= R534), K612 (= K624)
- binding coenzyme a: F172 (= F167), G174 (= G169), R200 (= R195), G312 (≠ A311), Y362 (= Y361), V363 (≠ T362), A364 (= A363), S531 (= S531), G532 (= G532), R592 (≠ A599), F598 (≠ I605)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G393), E394 (= E394), P395 (= P395), T418 (= T418), Y419 (≠ W419), W420 (= W420), Q421 (= Q421), T422 (= T422), D508 (= D508), I520 (≠ L520), R523 (= R523), R534 (= R534)
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
50% identity, 84% coverage: 73:633/665 of query aligns to 78:621/622 of 7kdnA
- active site: T271 (= T269), T422 (= T422), E423 (= E423), N529 (= N529), R534 (= R534), K612 (= K624)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G393), E394 (= E394), P395 (= P395), T418 (= T418), Y419 (≠ W419), W420 (= W420), Q421 (= Q421), T422 (= T422), D508 (= D508), I520 (≠ L520), R523 (= R523), R534 (= R534)
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
46% identity, 91% coverage: 45:651/665 of query aligns to 54:667/676 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 (= G393), P408 (= P395), T431 (= T418), Y432 (≠ W419), Q434 (= Q421), T435 (= T422), D522 (= D508), R537 (= R523), K638 (= K624)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
48% identity, 88% coverage: 72:655/665 of query aligns to 86:664/668 of 7l4gB
- active site: T280 (= T269), T432 (= T422), E433 (= E423), N539 (= N529), R544 (= R534), K631 (= K624)
- 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 (= W315), G403 (= G393), E404 (= E394), P405 (= P395), T428 (= T418), Y429 (≠ W419), W430 (= W420), M431 (≠ Q421), T432 (= T422), D518 (= D508), I530 (≠ L520), R533 (= R523)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
48% identity, 88% coverage: 72:655/665 of query aligns to 86:664/668 of 5u29A
- active site: T280 (= T269), T432 (= T422), E433 (= E423), N539 (= N529), R544 (= R534), K631 (= K624)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W315), G403 (= G393), E404 (= E394), P405 (= P395), T428 (= T418), Y429 (≠ W419), W430 (= W420), M431 (≠ Q421), T432 (= T422), D518 (= D508), I530 (≠ L520), R533 (= R523)
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)
45% identity, 94% coverage: 35:659/665 of query aligns to 39:655/662 of P78773
- T596 (≠ E601) modified: Phosphothreonine
7l3qA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-methylphosphate and co-enzyme a from coccidioides immitis rs
47% identity, 92% coverage: 20:633/665 of query aligns to 24:619/631 of 7l3qA
- active site: T272 (= T269), T423 (= T422), E424 (= E423), N530 (= N529), R535 (= R534)
- binding coenzyme a: F173 (= F167), A174 (≠ G168), G175 (= G169), R201 (= R195), G313 (≠ A311), Y363 (= Y361), A365 (= A363), S532 (= S531), G533 (= G532), R593 (≠ A599), P598 (= P604), F599 (≠ I605)
- binding 5'-O-[(R)-hydroxy(methoxy)phosphoryl]adenosine: I318 (≠ V316), G394 (= G393), E395 (= E394), P396 (= P395), T419 (= T418), Y420 (≠ W419), Q422 (= Q421), T423 (= T422), D509 (= D508), R524 (= R523), R535 (= R534)
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
49% identity, 85% coverage: 45:611/665 of query aligns to 10:556/559 of 7mmzA
- active site: T231 (= T269), T383 (= T422), E384 (= E423), N486 (= N529), R491 (= R534)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V316), G354 (= G393), E355 (= E394), P356 (= P395), T379 (= T418), W380 (= W419), W381 (= W420), Q382 (= Q421), T383 (= T422), D465 (= D508), I477 (≠ L520), R480 (= R523), R491 (= R534)
Query Sequence
>WP_089301905.1 NCBI__GCF_900188115.1:WP_089301905.1
MAEQSPALDNLLSESRTFPPSAEFAAQANATTDAYAKADADREGFWAEQAERLHWDTRWS
QVLDWSGAPFAKWFVGGKLNVAYNCVDRHVEAGHGDQVAIHWVGEPGDTRDITYAQLQRE
VCRAANALTSLGVSAHDRVAIQLQMIPEAIIAMLACARIGAMHSVVFGGFSPAALRTRVD
DASAKVVITSDGQYRRGKAAPMKSAVDEALDGAESVEKLLVVRRTGDEIGEIPWQEGRDL
WWHELLDSQPDEHTPQPFDSEHPLFILYTSGTTGKPKGILHTSGGYLTQAAYTHHTVFDH
KAGEDVYWCTADIGWVTGHTYIVYGPLANRARQVVYEGTPNTPHEGRHWEIVQNYRVSLY
YTAPTLIRTFMKWGDDIPARYDLSSLRLLGTVGEPINPEAWMWYREHIGGGSAPIVDTWW
QTETGAIMISPLPGVTHTKPGSAQRPIPGISAKVVDDSGTEVPFGSGGYLVIDKPWPGML
RTIWGDDQRYKDTYWSTFADAGYYFAGDGAKYDDDGDIWLLGRVDDVMNVSGHRISTTEV
ESALVSHPDVAEAAVVGATDETTGQGVVAFVILRGGTAGGTASDADNSETVNALRQHVAG
EIGPIAKPRQIMVVPELPKTRSGKIMRRLLRDVAENREVGDVTTLADSSVMDLISAGLHK
GSDED
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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