SitesBLAST
Comparing GFF832 HP15_811 acetyl-CoA synthetase 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)
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)
71% identity, 99% coverage: 1:643/649 of query aligns to 1:642/652 of Q8ZKF6
- R194 (= R194) 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 (= T312) binding
- N335 (= N336) binding
- A357 (= A358) 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 (= D518) 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 (= S524) binding
- G524 (= G525) 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 (= R527) 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 (= R585) 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 (= K610) modified: N6-acetyllysine; by Pat; mutation to A: No 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)
70% identity, 99% coverage: 1:643/649 of query aligns to 1:642/652 of P27550
- K609 (= K610) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
71% identity, 98% coverage: 7:643/649 of query aligns to 3:635/640 of 5jrhA
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N522), R522 (= R527), K605 (= K610)
- binding (r,r)-2,3-butanediol: W93 (≠ F97), E140 (= E144), G169 (≠ A173), K266 (≠ A271), P267 (= P272)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D501), I508 (= I513), N517 (= N522), R522 (= R527)
- binding coenzyme a: F159 (= F163), G160 (= G164), G161 (= G165), R187 (= R191), S519 (= S524), R580 (= R585), P585 (= P590)
- binding magnesium ion: V533 (= V538), H535 (= H540), I538 (≠ V543)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
71% identity, 98% coverage: 7:643/649 of query aligns to 3:636/641 of 2p20A
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N522), R522 (= R527), K605 (= K610)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D501), I508 (= I513), R511 (= R516), R522 (= R527)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
71% identity, 98% coverage: 7:643/649 of query aligns to 2:632/637 of 2p2fA
- active site: T259 (= T265), T411 (= T417), E412 (= E418), N516 (= N522), R521 (= R527), K604 (= K610)
- binding adenosine monophosphate: G382 (= G388), E383 (= E389), P384 (= P390), T407 (= T413), W408 (= W414), W409 (= W415), Q410 (= Q416), T411 (= T417), D495 (= D501), I507 (= I513), R510 (= R516), N516 (= N522), R521 (= R527)
- binding coenzyme a: F158 (= F163), R186 (= R191), W304 (= W310), T306 (= T312), P329 (= P335), A352 (= A358), A355 (= A361), S518 (= S524), R579 (= R585), P584 (= P590)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
70% identity, 98% coverage: 7:643/649 of query aligns to 3:629/634 of 1pg3A
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N522), R522 (= R527), K605 (= K610)
- binding coenzyme a: F159 (= F163), G160 (= G164), R187 (= R191), R190 (= R194), A301 (= A306), T307 (= T312), P330 (= P335), A356 (= A361), S519 (= S524), R580 (= R585), P585 (= P590)
- binding magnesium ion: V533 (= V538), H535 (= H540), I538 (≠ V543)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D501), R511 (= R516), R522 (= R527)
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)
68% identity, 100% coverage: 4:649/649 of query aligns to 3:645/648 of Q89WV5
- G263 (= G267) mutation to I: Loss of activity.
- G266 (= G270) mutation to I: Great decrease in activity.
- K269 (= K273) mutation to G: Great decrease in activity.
- E414 (= E418) mutation to Q: Great decrease in activity.
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)
53% identity, 98% coverage: 11:647/649 of query aligns to 33:697/701 of Q9NR19
- T363 (= T312) mutation to A: Loss of catlytic 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. 605:617, 92% identical) Nuclear localization signal
- S659 (= S608) 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 613:614) 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)
53% identity, 98% coverage: 11:647/649 of query aligns to 33:697/701 of Q9QXG4
- K661 (= K610) modified: N6-acetyllysine
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
53% identity, 95% coverage: 26:644/649 of query aligns to 26:657/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V311), G400 (= G388), E401 (= E389), P402 (= P390), T425 (= T413), W426 (= W414), W427 (= W415), Q428 (= Q416), T429 (= T417), D513 (= D501), I525 (= I513), R528 (= R516), R539 (= R527)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
53% identity, 95% coverage: 26:644/649 of query aligns to 27:655/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G388), E399 (= E389), P400 (= P390), T423 (= T413), W424 (= W414), Q426 (= Q416), T427 (= T417), D511 (= D501), R526 (= R516), R537 (= R527)
- binding coenzyme a: F171 (= F163), G172 (= G164), G173 (= G165), R199 (= R191), K202 (≠ R194), R595 (= R585), P600 (= P590)
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)
51% identity, 96% coverage: 24:644/649 of query aligns to 51:669/682 of Q99NB1
- K635 (= K610) 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)
49% identity, 98% coverage: 15:649/649 of query aligns to 31:676/683 of P52910
- K506 (≠ S491) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
50% identity, 96% coverage: 23:644/649 of query aligns to 57:676/689 of Q9NUB1
- V488 (≠ L457) to M: in dbSNP:rs6050249
- K642 (= K610) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
55% identity, 87% coverage: 38:600/649 of query aligns to 10:559/559 of 7mmzA
- active site: T231 (= T265), T383 (= T417), E384 (= E418), N486 (= N522), R491 (= R527)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V311), G354 (= G388), E355 (= E389), P356 (= P390), T379 (= T413), W380 (= W414), W381 (= W415), Q382 (= Q416), T383 (= T417), D465 (= D501), I477 (= I513), R480 (= R516), R491 (= R527)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
52% identity, 99% coverage: 1:642/649 of query aligns to 24:663/668 of 7l4gB
- active site: T280 (= T265), T432 (= T417), E433 (= E418), N539 (= N522), R544 (= R527), K631 (= K610)
- 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 (= W310), G403 (= G388), E404 (= E389), P405 (= P390), T428 (= T413), Y429 (≠ W414), W430 (= W415), M431 (≠ Q416), T432 (= T417), D518 (= D501), I530 (= I513), R533 (= R516)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
52% identity, 99% coverage: 1:642/649 of query aligns to 24:663/668 of 5u29A
- active site: T280 (= T265), T432 (= T417), E433 (= E418), N539 (= N522), R544 (= R527), K631 (= K610)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W310), G403 (= G388), E404 (= E389), P405 (= P390), T428 (= T413), Y429 (≠ W414), W430 (= W415), M431 (≠ Q416), T432 (= T417), D518 (= D501), I530 (= I513), R533 (= R516)
8w0cA Acetyl-coenzyme A synthetase 2
49% identity, 100% coverage: 2:649/649 of query aligns to 18:664/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G388), E400 (= E389), P401 (= P390), T424 (= T413), Y425 (≠ W414), W426 (= W415), Q427 (= Q416), T428 (= T417), D514 (= D501), R529 (= R516), R540 (= R527)
8w0bA Acetyl-coenzyme A synthetase 2
49% identity, 100% coverage: 2:649/649 of query aligns to 18:664/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (= V387), G399 (= G388), E400 (= E389), P401 (= P390), T424 (= T413), Y425 (≠ W414), W426 (= W415), Q427 (= Q416), T428 (= T417), D514 (= D501), I526 (= I513), R529 (= R516), R540 (= R527)
8w0dA Acetyl-coenzyme A synthetase 2
49% identity, 100% coverage: 2:649/649 of query aligns to 17:663/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G388), E399 (= E389), P400 (= P390), T423 (= T413), Y424 (≠ W414), W425 (= W415), Q426 (= Q416), T427 (= T417), D513 (= D501), I525 (= I513), R528 (= R516), R539 (= R527)
Query Sequence
>GFF832 HP15_811 acetyl-CoA synthetase
MTGKQVYPVSPEVAKQALLNREQYEEMYRQSVEDPDTFWGEHGKRLEWIKPYTKVKNTTY
DYNNLSIKWFEDGQLNASANCLDRHLEKRGDQTAIIFEGDDPADSRNVTYRELHEETSKF
ANVLKGLGVKKGDVVTIYMPMIVETAVAMLACARIGAIHSVVFGGFSPEALGARIVNGKS
RFVVTADEGVRGGRKIPLKKNVDAALKNEDAANVEKVVVVTRTGNSEVPWNEARDERYED
LMKSASADCQPEPMNAEDPLFMLYTSGSTGAPKGVLHTTGGYMVYASMTHEYVFDYHEGD
VYWCTADFGWVTGHSYILYGPLANGAITVLFEGVPNYPDSSRMGQVVDKHKVNILYTAPT
AIRALMAEGESCMNGTTRESLKLLGSVGEPINPEAWEWYHRVIGNSKCPIVDTWWQTETG
GILISPLPGAIDLKPGSATVPFFGVQPALVDNDGNILEGKTEGNLVILDSWPGQMRTIYG
DHERFAQTYFSTYKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEVESALVSH
EKVAEAAVVGYPHDIKGQGIYVYVTLVHGQEPSDELKKELVQWVRKEIGPIASPDVIQWA
PGLPKTRSGKIMRRILRKIAANEHDQLGDTSTLADPGVVDDLISGRANQ
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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