SitesBLAST
Comparing WP_011938514.1 NCBI__GCF_000016745.1:WP_011938514.1 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)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
41% identity, 91% coverage: 47:579/584 of query aligns to 79:630/630 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 (= G341), E392 (= E342), P393 (= P343), T416 (≠ N363), W417 (= W364), W418 (= W365), Q419 (= Q366), T420 (= T367), D502 (= D451), R517 (= R466), K523 (= K472), R528 (≠ M477)
- binding magnesium ion: V539 (≠ M488), H541 (= H490)
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)
38% identity, 92% coverage: 47:581/584 of query aligns to 74:629/648 of Q89WV5
- G263 (= G224) mutation to I: Loss of activity.
- G266 (= G227) mutation to I: Great decrease in activity.
- K269 (= K230) mutation to G: Great decrease in activity.
- E414 (= E368) mutation to Q: Great decrease in 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)
37% identity, 92% coverage: 47:581/584 of query aligns to 75:632/652 of P27550
- K609 (= K560) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
36% identity, 92% coverage: 43:581/584 of query aligns to 67:626/641 of 2p20A
- active site: T260 (= T222), T412 (= T367), E413 (= E368), N517 (≠ K472), R522 (≠ M477), K605 (= K560)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G341), E384 (= E342), P385 (= P343), T408 (≠ N363), W409 (= W364), W410 (= W365), Q411 (= Q366), T412 (= T367), D496 (= D451), I508 (≠ F463), R511 (= R466), R522 (≠ M477)
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)
37% identity, 92% coverage: 43:581/584 of query aligns to 71:632/652 of Q8ZKF6
- R194 (≠ E171) 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 (= T268) binding CoA
- N335 (≠ D292) binding CoA
- A357 (= A311) 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 (= D468) 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 (= S474) binding CoA
- G524 (= G475) 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 (≠ M477) 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 (= R535) 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 (= K560) 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)
37% identity, 92% coverage: 43:581/584 of query aligns to 67:625/640 of 5jrhA
- active site: T260 (= T222), T412 (= T367), E413 (= E368), N517 (≠ K472), R522 (≠ M477), K605 (= K560)
- binding (r,r)-2,3-butanediol: W93 (= W70), E140 (≠ P116), G169 (≠ Q145), K266 (≠ M228), P267 (= P229)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G341), E384 (= E342), P385 (= P343), T408 (≠ N363), W409 (= W364), W410 (= W365), Q411 (= Q366), T412 (= T367), D496 (= D451), I508 (≠ F463), N517 (≠ K472), R522 (≠ M477)
- binding coenzyme a: F159 (= F135), G160 (≠ S136), G161 (≠ A137), R187 (= R170), S519 (= S474), R580 (= R535), P585 (≠ S540)
- binding magnesium ion: V533 (≠ M488), H535 (= H490), I538 (≠ V493)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
36% identity, 92% coverage: 43:580/584 of query aligns to 66:620/637 of 2p2fA
- active site: T259 (= T222), T411 (= T367), E412 (= E368), N516 (≠ K472), R521 (≠ M477), K604 (= K560)
- binding adenosine monophosphate: G382 (= G341), E383 (= E342), P384 (= P343), T407 (≠ N363), W408 (= W364), W409 (= W365), Q410 (= Q366), T411 (= T367), D495 (= D451), I507 (≠ F463), R510 (= R466), N516 (≠ K472), R521 (≠ M477)
- binding coenzyme a: F158 (= F135), R186 (= R170), W304 (= W266), T306 (= T268), P329 (≠ F291), A352 (= A311), A355 (= A314), S518 (= S474), R579 (= R535), P584 (≠ S540)
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)
36% identity, 90% coverage: 43:567/584 of query aligns to 97:668/701 of Q9NR19
- T363 (= T268) 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. 555:567, 77% identical) Nuclear localization signal
- S659 (= S558) 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 563:564) 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
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
36% identity, 90% coverage: 43:567/584 of query aligns to 67:612/634 of 1pg3A
- active site: T260 (= T222), T412 (= T367), E413 (= E368), N517 (≠ K472), R522 (≠ M477), K605 (= K560)
- binding coenzyme a: F159 (= F135), G160 (≠ S136), R187 (= R170), R190 (≠ E171), A301 (= A262), T307 (= T268), P330 (≠ F291), A356 (= A314), S519 (= S474), R580 (= R535), P585 (≠ S540)
- binding magnesium ion: V533 (≠ M488), H535 (= H490), I538 (≠ V493)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G341), E384 (= E342), P385 (= P343), T408 (≠ N363), W409 (= W364), W410 (= W365), Q411 (= Q366), T412 (= T367), D496 (= D451), R511 (= R466), R522 (≠ M477)
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)
37% identity, 96% coverage: 22:581/584 of query aligns to 40:638/651 of P9WQD1
- K617 (= K560) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
35% identity, 92% coverage: 43:581/584 of query aligns to 97:683/701 of Q9QXG4
- K661 (= K560) modified: N6-acetyllysine
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound) (see paper)
35% identity, 92% coverage: 43:581/584 of query aligns to 78:644/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G341), E399 (= E342), P400 (= P343), T423 (≠ N363), W424 (= W364), Q426 (= Q366), T427 (= T367), D511 (= D451), R526 (= R466), R537 (≠ M477)
- binding coenzyme a: F171 (= F135), G172 (≠ S136), G173 (≠ A137), R199 (= R170), K202 (≠ L173), R595 (= R535), P600 (≠ S540)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound) (see paper)
35% identity, 92% coverage: 43:581/584 of query aligns to 77:646/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V267), G400 (= G341), E401 (= E342), P402 (= P343), T425 (≠ N363), W426 (= W364), W427 (= W365), Q428 (= Q366), T429 (= T367), D513 (= D451), I525 (≠ F463), R528 (= R466), R539 (≠ M477)
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)
35% identity, 92% coverage: 44:582/584 of query aligns to 98:659/682 of Q99NB1
- K635 (= K560) modified: N6-acetyllysine
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)
35% identity, 92% coverage: 44:582/584 of query aligns to 105:666/689 of Q9NUB1
- V488 (≠ L409) to M: in dbSNP:rs6050249
- K642 (= K560) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
36% identity, 90% coverage: 44:567/584 of query aligns to 81:619/633 of 7kvyA
- active site: T271 (= T222), T422 (= T367), E423 (= E368), N529 (≠ K472), R534 (≠ M477), K612 (= K560)
- binding coenzyme a: F172 (= F135), G174 (≠ A137), R200 (≠ Y162), G312 (≠ A262), Y362 (= Y309), V363 (≠ T310), A364 (= A311), S531 (= S474), G532 (= G475), R592 (= R535), F598 (≠ A541)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G341), E394 (= E342), P395 (= P343), T418 (≠ N363), Y419 (≠ W364), W420 (= W365), Q421 (= Q366), T422 (= T367), D508 (= D451), I520 (≠ F463), R523 (= R466), R534 (≠ M477)
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)
36% identity, 86% coverage: 80:581/584 of query aligns to 118:641/662 of P78773
- T596 (≠ R537) modified: Phosphothreonine
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
36% identity, 87% coverage: 43:549/584 of query aligns to 42:558/559 of 7mmzA
- active site: T231 (= T222), T383 (= T367), E384 (= E368), N486 (≠ K472), R491 (≠ M477)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V267), G354 (= G341), E355 (= E342), P356 (= P343), T379 (≠ N363), W380 (= W364), W381 (= W365), Q382 (= Q366), T383 (= T367), D465 (= D451), I477 (≠ F463), R480 (= R466), R491 (≠ M477)
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
34% identity, 92% coverage: 47:583/584 of query aligns to 94:663/676 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 (= G341), P408 (= P343), T431 (≠ N363), Y432 (≠ W364), Q434 (= Q366), T435 (= T367), D522 (= D451), R537 (= R466), K638 (= K560)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
34% identity, 89% coverage: 47:567/584 of query aligns to 58:597/615 of 1ry2A
- active site: T247 (= T222), T399 (= T367), N507 (≠ K472), K590 (= K560)
- binding adenosine monophosphate: G370 (= G341), E371 (= E342), P372 (= P343), T395 (≠ N363), Y396 (≠ W364), W397 (= W365), Q398 (= Q366), T399 (= T367), D486 (= D451), I498 (≠ F463), R501 (= R466)
Query Sequence
>WP_011938514.1 NCBI__GCF_000016745.1:WP_011938514.1
MDWKPIRKSPELQAVRPHLLDYEKTCAGFSWEAVRSELSGLPEGKGLNIAHEAVDRQAAG
PLRDRLAFRWLGKDGAVQDFTFCDLKEQSSRFANVLKRLGVEKGERVFVLAGRIPPLYIA
ALGCLKNISVFCPLFSAFGPDPIRQRLSRGDARLLVTTERQYAKKIAGIRESLPQLRHVL
LTDIDDDLDETVLSLPRLMAEASADFTIPPTDPEDMAVLHFTSGTTGMPKGAVLVHDAVL
THLVTGRYVMDFHSADIFWCTADPGWVTGSSYGIIAPLLHGITSIIDEADFDAERWYRIL
EEQRVTVWYTAPTAIRMLMRAAIEPLKRFDLSPLRLIHSVGEPLNPEAVVWGERVLGLPI
HDNWWQTETGGIMIANYAAMEIRPGSMGRPLPGIEAAIVRRVDDSVDVLTEPDVEGDLAL
RPGWPSMFRAYLHDEERYRKCFVSGWYITGDLAKRDADGYYWFVGRGDDIIKTSGHMVGP
FEVESALMEHPAVAEAGVIGKPEPIIGEIVKAFVCLKPGFEPTDKLRLELIGFGRTRLGS
AVAPKEMEFVDSLPRTRSGKIMRRLLKARELGLPEGDTSTLETG
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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