SitesBLAST
Comparing WP_034999697.1 NCBI__GCF_000745425.1:WP_034999697.1 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)
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)
75% identity, 100% coverage: 1:645/645 of query aligns to 1:644/648 of Q89WV5
- G263 (= G264) mutation to I: Loss of activity.
- G266 (= G267) mutation to I: Great decrease in activity.
- K269 (= K270) mutation to G: Great decrease in activity.
- E414 (= E415) 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)
65% identity, 98% coverage: 14:645/645 of query aligns to 15:647/652 of P27550
- K609 (= K607) modified: N6-acetyllysine; by autocatalysis
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)
65% identity, 98% coverage: 14:645/645 of query aligns to 15:647/652 of Q8ZKF6
- R194 (= R193) 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 (= T309) binding CoA
- N335 (= N333) binding CoA
- A357 (= A355) 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 (= D515) 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 (= S521) binding CoA
- G524 (= G522) 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 (= R524) 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 (= R582) 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 (= K607) 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)
65% identity, 98% coverage: 14:645/645 of query aligns to 11:640/640 of 5jrhA
- active site: T260 (= T262), T412 (= T414), E413 (= E415), N517 (= N519), R522 (= R524), K605 (= K607)
- binding (r,r)-2,3-butanediol: W93 (≠ F96), E140 (= E143), G169 (= G172), K266 (≠ A268), P267 (= P269)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G385), E384 (= E386), P385 (= P387), T408 (= T410), W409 (= W411), W410 (= W412), Q411 (= Q413), T412 (= T414), D496 (= D498), I508 (= I510), N517 (= N519), R522 (= R524)
- binding coenzyme a: F159 (= F162), G160 (= G163), G161 (= G164), R187 (= R190), S519 (= S521), R580 (= R582), P585 (= P587)
- binding magnesium ion: V533 (= V535), H535 (= H537), I538 (≠ V540)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
64% identity, 98% coverage: 14:645/645 of query aligns to 10:637/637 of 2p2fA
- active site: T259 (= T262), T411 (= T414), E412 (= E415), N516 (= N519), R521 (= R524), K604 (= K607)
- binding adenosine monophosphate: G382 (= G385), E383 (= E386), P384 (= P387), T407 (= T410), W408 (= W411), W409 (= W412), Q410 (= Q413), T411 (= T414), D495 (= D498), I507 (= I510), R510 (= R513), N516 (= N519), R521 (= R524)
- binding coenzyme a: F158 (= F162), R186 (= R190), W304 (= W307), T306 (= T309), P329 (= P332), A352 (= A355), A355 (= A358), S518 (= S521), R579 (= R582), P584 (= P587)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
64% identity, 98% coverage: 14:645/645 of query aligns to 11:641/641 of 2p20A
- active site: T260 (= T262), T412 (= T414), E413 (= E415), N517 (= N519), R522 (= R524), K605 (= K607)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G385), E384 (= E386), P385 (= P387), T408 (= T410), W409 (= W411), W410 (= W412), Q411 (= Q413), T412 (= T414), D496 (= D498), I508 (= I510), R511 (= R513), R522 (= R524)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
64% identity, 98% coverage: 14:645/645 of query aligns to 11:634/634 of 1pg3A
- active site: T260 (= T262), T412 (= T414), E413 (= E415), N517 (= N519), R522 (= R524), K605 (= K607)
- binding coenzyme a: F159 (= F162), G160 (= G163), R187 (= R190), R190 (= R193), A301 (= A303), T307 (= T309), P330 (= P332), A356 (= A358), S519 (= S521), R580 (= R582), P585 (= P587)
- binding magnesium ion: V533 (= V535), H535 (= H537), I538 (≠ V540)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G385), E384 (= E386), P385 (= P387), T408 (= T410), W409 (= W411), W410 (= W412), Q411 (= Q413), T412 (= T414), D496 (= D498), R511 (= R513), R522 (= R524)
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)
55% identity, 97% coverage: 22:644/645 of query aligns to 46:697/701 of Q9NR19
- T363 (= T309) 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. 602:614, 92% identical) Nuclear localization signal
- S659 (= S605) 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 610:611) 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)
54% identity, 97% coverage: 22:644/645 of query aligns to 46:697/701 of Q9QXG4
- K661 (= K607) modified: N6-acetyllysine
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
53% identity, 95% coverage: 26:640/645 of query aligns to 27:656/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V308), G400 (= G385), E401 (= E386), P402 (= P387), T425 (= T410), W426 (= W411), W427 (= W412), Q428 (= Q413), T429 (= T414), D513 (= D498), I525 (= I510), R528 (= R513), R539 (= R524)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
53% identity, 95% coverage: 26:640/645 of query aligns to 28:654/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G385), E399 (= E386), P400 (= P387), T423 (= T410), W424 (= W411), Q426 (= Q413), T427 (= T414), D511 (= D498), R526 (= R513), R537 (= R524)
- binding coenzyme a: F171 (= F162), G172 (= G163), G173 (= G164), R199 (= R190), K202 (≠ R193), R595 (= R582), P600 (= P587)
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)
51% identity, 96% coverage: 23:640/645 of query aligns to 40:670/683 of P52910
- K506 (≠ S488) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
53% identity, 97% coverage: 15:639/645 of query aligns to 34:663/668 of 7l4gB
- active site: T280 (= T262), T432 (= T414), E433 (= E415), N539 (= N519), R544 (= R524), K631 (= K607)
- 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 (= W307), G403 (= G385), E404 (= E386), P405 (= P387), T428 (= T410), Y429 (≠ W411), W430 (= W412), M431 (≠ Q413), T432 (= T414), D518 (= D498), I530 (= I510), R533 (= R513)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
53% identity, 97% coverage: 15:639/645 of query aligns to 34:663/668 of 5u29A
- active site: T280 (= T262), T432 (= T414), E433 (= E415), N539 (= N519), R544 (= R524), K631 (= K607)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W307), G403 (= G385), E404 (= E386), P405 (= P387), T428 (= T410), Y429 (≠ W411), W430 (= W412), M431 (≠ Q413), T432 (= T414), D518 (= D498), I530 (= I510), R533 (= R513)
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)
51% identity, 96% coverage: 22:640/645 of query aligns to 34:651/662 of P78773
- T596 (≠ D584) 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)
51% identity, 97% coverage: 16:640/645 of query aligns to 44:668/682 of Q99NB1
- K635 (= K607) 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)
51% identity, 96% coverage: 23:640/645 of query aligns to 58:675/689 of Q9NUB1
- V488 (≠ L454) to M: in dbSNP:rs6050249
- K642 (= K607) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
52% identity, 97% coverage: 15:639/645 of query aligns to 34:661/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W307), I324 (≠ V308), V400 (= V384), G401 (= G385), E402 (= E386), P403 (= P387), T426 (= T410), Y427 (≠ W411), W428 (= W412), M429 (≠ Q413), T430 (= T414), D516 (= D498)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
52% identity, 97% coverage: 15:639/645 of query aligns to 34:661/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W307), I324 (≠ V308), G401 (= G385), E402 (= E386), P403 (= P387), T426 (= T410), Y427 (≠ W411), W428 (= W412), M429 (≠ Q413), T430 (= T414), D516 (= D498), I528 (= I510), R531 (= R513)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
52% identity, 97% coverage: 15:639/645 of query aligns to 34:661/666 of 7knoA
- active site: T280 (= T262), T430 (= T414), E431 (= E415), N537 (= N519), R542 (= R524), K629 (= K607)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W307), I324 (≠ V308), G401 (= G385), E402 (= E386), P403 (= P387), T426 (= T410), Y427 (≠ W411), W428 (= W412), M429 (≠ Q413), T430 (= T414), D516 (= D498), R531 (= R513)
Query Sequence
>WP_034999697.1 NCBI__GCF_000745425.1:WP_034999697.1
MSEKTYPVSAYWNDHAFINAAKYKEMYRRSVEEPDLFWGEEGKRIDWIKPYTKVKNTCFD
VPNVDIRWFEDGTTNVALNCIDRHLATRGDQTAIIFEGDDPNDSRSITYKELHESVCRLA
NVLKDHGVGKGDTVSIYLPMIPEAAFAMLACARIGAIHSVIFGGFSPDSLAGRIEGCRSK
IIITADEGLRGGRKVPLKANADLAIEKTGDIVETMIVVTRTGGQVAWTEGRDIRYEEAVA
KASPECPVTEVEAEHPLFILYTSGSTGAPKGVVHCTGGYLVYASMTHQYIFDYHDGDIYW
CTADVGWVTGHSYIIYGPLANGATTLMFEGVPNYPSVSRFWEVIDKHKVTIFYTAPTAIR
ALMGSGEEPVKKTSRASLRLLGSVGEPINPEAWEWYFRVVGEERCPIVDTWWQTETGGIL
ITPLPGATALKPGSATTPFFGVKPQIVDATGAVLEGVCEGNLVIADAWPAQMRTIYGDHD
RFMQTYFSTYPGKYFTGDGCRRDADGYYWITGRVDDVINVSGHRLGTAEVESSLVAHELV
SEAAVVGYPHEIKGQGIYAYVTLMNGIEPSDRLRTELVTWVRKDIGPIATPDIVHFAPGL
PKTRSGKIMRRILRKIAEKEFSALGDVSTLADPSIVDDLIRNRAS
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